pteridines and molybdenum

pteridines has been researched along with molybdenum in 250 studies

Research

Studies (250)

TimeframeStudies, this research(%)All Research%
pre-199064 (25.60)18.7374
1990's88 (35.20)18.2507
2000's50 (20.00)29.6817
2010's38 (15.20)24.3611
2020's10 (4.00)2.80

Authors

AuthorsStudies
Amy, NK; Rajagopalan, KV1
Rothery, RA; Sambasivarao, D; Trieber, CA; Weiner, JH1
Casadesus, J; Flores, A; Garzón, A; Li, J; Stewart, V1
Boxer, DH; Chippaux, M; Cole, JA; DeMoss, JA; Giordano, G; Gunsalus, RP; Lin, EC; Rajagopalan, KV; Shanmugam, KT; Stewart, V1
Crawford, NM; Feldmann, KA; LaBrie, ST; Tsay, YF; Wilkinson, JQ1
Augier, V; Blasco, F; Chippaux, M; Giordano, G; Pommier, J1
Johnson, JL; Rajagopalan, KV4
Bray, RC; Burke, JF; Chovnick, A; Doyle, WA; Hughes, RK; Whittle, JR1
Chaudhury, M; Johnson, JL; Rajagopalan, KV1
Aguilar, MR; Cárdenas, J; Fernández, E1
Bennett, B; Bray, RC; Howes, BD; Koppenhöfer, A; Lowe, DJ1
Baker, KP; Boxer, DH1
Ferguson, SJ; Jackson, JB; McEwan, AG1
Bray, RC; Burke, JF; Cock, JM; Doyle, WA; Nicolson, RE; Walters, DE; Wootton, JC1
Bauder, R; Lingens, F; Tshisuaka, B1
Barber, MJ; Kay, CJ; Solomonson, LP1
Basu, SN; Condie, RG; Constantine, G; Desjacques, P; Dorche, C; Gray, RG; Green, A; Vianey-Liaud, C1
Bastian, NR; Johnson, JL; Rajagopalan, KV1
Gardlik, S; Rajagopalan, KV1
Grieve, C; Gurr, SJ; Kinghorn, JR; Ramsden, M; Spence, D; Unkles, SE; Whitehead, MP1
Dean, D; Hinton, SM1
Johnson, JL; Mandell, R; Shih, VE; Wuebbens, MM2
Johnson, JL; Rajagopalan, KV; Wuebbens, MM1
Boxer, D; Giordano, G; Karibian, D; Santini, CL; Vasishta, A1
Bray, RC; Deistung, J; Ventom, AM1
Duch, DS; Nichol, CA; Smith, GK1
Solomonson, LP; Zeiler, KG1
Fritz, B; Ninnemann, H; Siefermann-Harms, D1
Hageman, RV; Rajagopalan, KV1
Johnson, ME; Rajagopalan, KV2
Krüger, B; Meyer, O1
Kasai, Y; Nohno, T; Saito, T1
Stewart, V1
Rajagopalan, KV3
Baldwin, MC; Finnerty, V; Schott, DR1
Amy, NK; Miller, JB; Scott, DJ1
Johnson, JL1
Gheller, SF; Hedman, B; Hodgson, KO; Lough, SM; McDonald, JW; Newton, WE1
Giordano, G; Pommier, J; Silvestro, A1
Ishimoto, M; Okubo, N; Yamamoto, I1
Freyer, G; Hinton, SM1
Johnson, JL; Kramer, SP; Millington, DS; Rajagopalan, KV; Ribeiro, AA1
Ferry, JG; May, HD; Schauer, NL1
Hille, R; Massey, V1
Bimar, J; Collet, S; Desjacques, P; Divry, P; Lagier, P; Lando, A; Tessonnier, JM; Vianet-Liaud, C1
Berger, JP; Hervé, F; Soulier, J1
Hinton, SM; Mortenson, LE1
Beemer, FA; Cats, BP; Duran, M; Wadman, SK1
Monnet, JP; Nogues, C; Ogier, H; Roth, A; Saudubray, JM1
Fukui, S; Ishizuka, M; Kogushi, M; Toraya, T; Ushio, K1
Bray, RC; Hawkes, TR2
Hageman, RV; Rajagopalan, KV; Wahl, RC1
Hageman, RV; Kramer, S; Rajagopalan, KV1
Burns, A; Tennent, DL; Watt, GD1
Bray, RC; Malthouse, JP; Williams, JW1
Amy, NK; Miller, JB1
Coughlan, MP1
Buxton, RS; Drury, LS1
Fukui, S; Ishizuka, M; Toraya, T; Ushio, K1
Brill, WJ; Imperial, J; Shah, VK; Ugalde, RA1
Goldflam, M; Rowe, JJ1
Beemer, FA; Berger, R; Cats, BP; Charpentier, C; Duran, M; Johnson, JL; Ogier, H; Rajagopalan, KV; Saudubray, JM; Wadman, SK1
Campbell, A; del Campillo-Campbell, A1
Arison, BH; Hainline, BE; Johnson, JL; Rajagopalan, KV1
Bettenhaussen, CW; Claassen, VP; Fokkens, RH; Nibbering, NM; Oltmann, LF; Pinkse, FA; Stouthamer, AH; van 't Riet, J1
Meyer, O; Rajagopalan, KV1
Claassen, VP; Oltmann, LF; Stouthamer, AH; Vader, CE; van 't Riet, J1
Hainline, BE; Johnson, JL; Rajagopalan, KV1
Davis, MD; Olson, JS; Palmer, G1
Charpentier, C; Frezal, J; Kesseler, A; Munnich, A; Ogier, H; Perignon, JL; Saudubray, JM1
Finnerty, V; Warner, CK1
Beemer, FA; Duran, M; Johnson, JL; Rajagopalan, KV; Wadman, SK; Waud, WR1
Amy, NK1
Bus, S; Claassen, VP; Oltmann, LF; Stouthamer, AH; v 't Riet, J1
Ishimoto, M; Takagi, M; Tsuchiya, T1
Brill, WJ; Shah, VK; Shen, SC; Stacey, G; Zhu, J1
MacGregor, CH; Stewart, V1
Brinkman, UA; Claassen, VP; Oltmann, LF; Stouthamer, AH; Van't Riet, J1
Arst, HN; Sealy-Lewis, HM; Tollervey, DW1
Johnson, JL; Mize, C; Rajagopalan, KV1
Archer, M; Engh, R; Hof, P; Huber, R; LeGall, J; Moura, I; Moura, JJ; Romão, MJ; Schneider, M1
Hagen, WR; Hansen, TA; Hensgens, CM1
Artigas, M; Coll, MJ; Johnson, JL; Naranjo, MA; Pintos-Morell, G; Rajagopalan, KV; Rodes, M; Roge, M1
Mandel, H; Stroomer, LE; van Cruchten, AG; van Gennip, AH1
Deppenmeier, U; Gunsalus, RP; Rech, S1
Bastian, NR; Hilton, J; Kilpatrick, L; Pilato, RS; Rajagopalan, KV; Spiro, TG; Stiefel, EI1
Heck, IS; Ninnemann, H1
Krauss, F; Lottspeich, F; Simon, H; Trautwein, T1
Finnerty, V; Kamdar, KP; Shelton, ME1
Abeling, NG; Bakker, HD; Overweg-Plandsoen, WC; ten Houten, R; van den Blij, JF; van Gennip, AH; Wanders, RJ1
Garrett, RM; Hilton, JC; Johnson, JL; Pitterle, DM; Rajagopalan, KV; Wuebbens, MM; Zurick, TR1
Darwish, IS; Taylor, EC1
Dubler, E; Fischer, B; Schmalle, H; Viscontini, M1
Johnson, JL; Rajagopalan, KV; Wadman, SK1
Finnerty, V; Kamdar, P; Shelton, ME1
Abeling, NG; Bakker, HD; Barth, PG; Overweg-Plandsoen, WC; Slot, HM; Tamminga, P; Van Gennip, AH1
Eady, RR; Gangeswaran, R; Lowe, DJ1
Arnold, GL; Goodman, SI; Greene, CL; Stout, JP1
Bakker, HD1
Brinkmann, H; Mendel, RR; Nerlich, A; Schiemann, J; Stallmeyer, B1
Blasco, F; Buc, J; Cárdenas, ML; Chippaux, M; Cornish-Bowden, A; Giordani, R; Giordano, G; Santini, CL1
Hedderich, R; Hochheimer, A; Schmitz, RA; Thauer, RK1
Edmondson, DE; Xiang, Q1
Hille, R; Kim, JH; Knaut, H; Ryan, MG1
Kroneck, PM; Reichenbecher, W; Rüdiger, A; Schink, B1
Stiefel, EI1
Bray, RC; Chovnick, A; Doyle, WA; Whittle, JR1
Hanlon, SP; Holt, RA; McEwan, AG; Solomon, PS; Toh, TH1
Brandsch, R; Menéndez, C; Siebert, D1
Johnson, JL; Joshi, MS; Rajagopalan, KV1
Bellini, C; Bertola, A; Bonioli, E; Caruso, U; DiStefano, A; Dorche, C; Fantasia, AR; Minniti, G; Palmieri, A1
Eshed, Y; Fluhr, R; Ori, N; Paran, I; Pinto, P; Zamir, D1
Amaya, Y; Hosoya, T; Ichida, K; Kamatani, N; Nishino, T; Sakai, O1
Hanson, GR; Lane, I; McEwan, AG; Solomon, PS1
Kisker, C; Rees, DC; Schindelin, H1
Boxer, DH; Heck, IS; Kanan, GJ; Kinghorn, JR; Millar, LJ; Smith, J; Unkles, SE1
Archangeli, LL; Finnerty, V; Kamdar, KP; Primus, JP; Shelton, ME; Wittle, AE1
Bray, RC; Eisenthal, R; Godber, B; Harrison, R; Sanders, S1
Böttcher, B; Brandsch, R; Igloi, G; Menéndez, C; Nick, P; Otto, A; Schubach, B1
Hasona, A; Ray, RM; Shanmugam, KT1
Asso, M; Bertrand, P; Blasco, F; Giordano, G; Guigliarelli, B; Magalon, A; Rothery, RA1
Blasco, F; Dos Santos, JP; Frixon, C; Giordano, G; Guigliarelli, B; Magalon, A; Santini, CL1
Ishibashi, S; Matsuishi, T; Nakashima, M; Satoi, M1
Huber, R; Knäblein, J; Moura, JJ; Romão, MJ1
Enemark, JH; McMaster, J1
Bacher, A; Blanchard, S; Boyle, P; Eisenreich, W; Götze, E; O'Brien, J; Richter, G; Rieder, C; Simon, H1
Fernández, E; Igeño, MI; Mendel, R; Schwarz, G; Witte, CP1
Hänzelmann, P; Meyer, O1
Betz, H; Feng, G; Kirsch, J; Kuhse, J; Nichol, MC; Sanes, JR; Tintrup, H1
Couillault, C; Dos Santos, JP; Giordano, G; Iobbi-Nivol, C; Méjean, V1
Froehner, SC1
Christensen, E; Dorche, C; Kurlemann, G; Reiss, J; Zabot, MT1
Baas, D; Kisker, C; Kroneck, PM; Meckenstock, RU; Rétey, J; Schindelin, H1
Hoffmann, GF; Micheli, V; Pérignon, JL; Simmonds, HA; van Gennip, AH1
Maxwell, S; Waring, WS1
Confort-Gouny, S; Cozzone, PJ; Salvan, AM; Vion-Dury, J1
Hilton, JC; Rajagopalan, KV; Temple, CA1
Anemüller, S; Hansen, T; Kardinahl, S; Petersen, A; Schäfer, G; Schmidt, CL1
Klipp, W; Leimkühler, S2
Cole, JA; Potter, L; Thomas, G1
Hanson, GR; Lane, I; McEwan, AG; Palmer, T; Shaw, AL; Solomon, PS1
Götz, F; Lindgren, PE; Neubauer, H; Pantel, I1
Angermüller, S; Klipp, W; Leimkühler, S; Mendel, RR; Schwarz, G1
Fujiwara, T; Sakurai, T; Yoshimatsu, K1
Reiss, J1
Kishikawa, M; Nakanishi, T; Shimizu, A; Yoshino, M1
Kuper, J; Mendel, RR; Palmer, T; Schwarz, G1
Behrens, A; Fryxelius, J; Lorber, C; Nordlander, E; Thapper, A1
Dunn, RL; Kozmin, SG; Pavlov, YI; Schaaper, RM1
Demontis, S; Garattini, E; Kurosaki, M; Marini, M; Salmona, M; Saltini, G; Terao, M1
Adams, B; Bailey, S; Bennett, B; Bray, RC; Smith, AT1
Anderson, LA; Boxer, DH; Leubke, T; Lubke, T; McNairn, E; Pau, RN1
Christensen, E; Gross-Hardt, S; Mendel, RR; Reiss, J; Schmidt, P; Schwarz, G1
Donahue, JP; Holm, RH; Lim, BS1
Kisker, C; Rajagopalan, KV; Schindelin, H1
Heck, IS; Kana'n, GJ; Kinghorn, JR; Millar, LJ; Sloan, J; Unkles, SE1
Heck, IS; Kanan, G; Kinghorn, JR; Millar, LJ; Schrag, JD; Sloan, J; Unkles, SE1
Hille, R1
Hänsch, R; Mendel, RR1
Brandsch, R; Sandu, C1
Dobbek, H; Gremer, L; Huber, R; Kiefersauer, R; Meyer, O1
Holm, RH; Zhang, Y1
Araujo, JA; Freuer, A; Leimkuhler, S; Mendel, RR; Rajagopalan, KV1
Atabay, Y; Klimmek, O; Kröger, A; Lyubenova, S; MacMillan, F; Prisner, T1
Edmondson, DE; Hubálek, F; Ivanov, NV; Trani, M1
Fischer, B; Mendel, RR; Nimtz, M; Otte, T; Santamaria-Araujo, JA; Schwarz, G; Wray, V1
Ahlrichs, R; Coucouvanis, D; Han, J; Nava, P1
Hunter, WN1
Hecht, HJ; Kuper, J; Llamas, A; Mendel, RR; Schwarz, G1
Enemark, JH; Joshi, HK1
Bittner, F; Heidenreich, T; Mendel, RR; Wollers, S1
Nichols, JD; Rajagopalan, KV1
Yoshida, M1
Bray, RC; Eisenthal, R; Godber, BL; Harrison, R; Lowe, DJ; Mendel, RR; Schwarz, G1
Bardischewsky, F; Friedrich, CG; Hellwig, P; Kostka, S; Quentmeier, A; Rother, D1
Bittner, F; Mendel, RR1
Cannio, R; D'Errico, G; Di Salle, A; La Cara, F; Rossi, M1
Choi, EY; Hemann, C; Hille, R; Ilich, P; Stockert, AL1
Ataya, FS; Fernandez, E; Fischer, K; Galvan, A; Kuper, J; Llamas, A; Mendel, RR; Schrader, N; Schwarz, G; Tejada-Jimenez, M1
Nichols, JD; Rajagopalan, KV; Schindelin, H; Xiang, S1
Mendel, RR3
Marquet, A; Mendel, RR; Smith, AG; Warren, MJ1
Morozkina, EV; Zvyagilskaya, RA1
Barrick, JE; Breaker, RR; Moy, RH; Regulski, EE; Ruzzo, WL; Weinberg, Z; Yao, Z1
Gladyshev, VN; Zhang, Y1
Moquin, K; Rothery, RA; Weiner, JH; Workun, GJ1
Nishino, T; Okamoto, K1
Aznar, CP; Britt, RD; Curatti, L; Hernandez, JA; Perova, Z; Rubio, LM1
Leimkühler, S; Neumann, M1
Cao, H; Hille, R; Pauff, JM1
Fingrut, DR; Li, W; Maxwell, DP1
Ryde, U; Schulzke, C; Starke, K1
Enemark, JH; Johnson-Winters, K; Tollin, G1
Chi, JC; Fischer, K; Krizowski, S; Lambeck, I; Mehlmer, N; Mueller, S; Schwarz, G; Teige, M1
Davis, AC; Enemark, JH; Johnson-Winters, K; Nordstrom, AR; Tollin, G1
Fernández, E; Galván, A; Llamas, A; Tejada-Jiménez, M1
Shi, T; Xie, J1
Astashkin, AV; Bittner, F; Enemark, JH; Klein, EL; Mendel, RR; Rajapakshe, A; Reichmann, D1
Kruse, T; Mendel, RR1
Burgmayer, SJ; Fu, Y; Williams, BR; Yap, GP1
Belaidi, AA; Schwarz, G1
Curth, U; Herzog, S; Krausze, J; Kruse, T; Mendel, RR; Pierik, AJ; Ringel, P; van den Heuvel, J1
Gast, K; Haumann, M; Horn, S; Kaufmann, P; Leidel, N; Leimkühler, S; Reschke, S; Schulzke, C; Sigfridsson, KG1
Cotelesage, JJ; George, GN; Pushie, MJ1
Haumann, M; Hille, R; Leimkühler, S; Niks, D; Rajagopalan, KV; Reschke, S; Sigfridsson, KG; Wilson, H1
Arnoux, P; Bertrand, P; Biaso, F; Burlat, B; Etienne, E; Fourmond, V; Grosse, S; Guigliarelli, B; Jacques, JG; Léger, C; Pignol, D; Sabaty, M1
Cabrita, EJ; Leimkühler, S; Otrelo-Cardoso, AR; Rodrigues, D; Romão, MJ; Santos-Silva, T; Schwuchow, V1
Azarov, I; Basu, P; Gauthier, MC; Gladwin, MT; Merchant, BA; Ragireddy, V; Sparacino-Watkins, CE; Sun, B; Tejero, J; Thomas, J; Wang, J1
Alexander, MM; Boysen, V; Kruse, T; Mendel, RR; Probst, C; Ringel, P; Wirsing, L1
Leimkühler, S; Mendel, RR1
Leimkühler, S; Yokoyama, K1
Basu, P; Fischer-Schrader, K; Frizzell, S; Gladwin, MT; Hille, R; Kelley, EE; Krizowski, S; Niks, D; Ragireddy, V; Schwarz, G; Sparacino-Watkins, C; Tejero, J; Wang, J; Wang, L; Zhang, Y1
Li, J; Ryde, U1
Clement, B; Havemeyer, A; Ott, G1
Basu, P; Burgmayer, SJ1
Magalon, A; Mendel, RR1
Kasaragod, VB; Schindelin, H1
Ali, K; Hoffmann, MC; Masepohl, B; Narberhaus, F; Robrahn, L; Sonnenschein, M; Strauss, D1
Agresta, AM; Bittner, F; Di Silvestre, D; Donnini, S; Gehl, C; Mauri, P; Murgia, I; Vigani, G1
Duffus, BR; Iobbi-Nivol, C; Jänsch, L; Kaufmann, P; Leimkühler, S; Mitrova, B; Nimtz, M; Teutloff, C; Wollenberger, U1
Caldararu, O; Cioloboc, D; Feldt, M; Mata, RA; Nordlander, E; Ryde, U; Starke, K; van Severen, MC1
Blankenfeldt, W; Hercher, TW; Kirk, ML; Krausze, J; Kruse, T; Mendel, RR; Zwerschke, D1
Novotny, JA; Peterson, CA1
Bittner, F; Clement, B; Ginsel, C; Havemeyer, A; Kubitza, C; Scheidig, AJ1
Calatrava, V; Chamizo-Ampudia, A; Fernandez, E; Galvan, A; Llamas, A; Tejada-Jimenez, M1
Dau, H; Duffus, BR; Haumann, M; Leimkühler, S; Mebs, S; Reschke, S; Schrapers, P; Teutloff, C1
Martínez-Espinosa, RM; Miralles-Robledillo, JM; Pire, C; Torregrosa-Crespo, J1
Iobbi-Nivol, C; Leimkühler, S; Méjean, V; Zupok, A1
Blankenfeldt, W; Hercher, TW; Hoffmeister, S; Krausze, J; Kruse, T; Lindel, T; Mendel, RR; Zwerschke, D1
Leimkühler, S2
Mayr, SJ; Mendel, RR; Schwarz, G1
DeBeer, S; Decamps, L; Van Stappen, C1
Giles, LJ; Hercher, TW; Kc, K; Kirk, ML; Krausze, J; Kruse, T; Mendel, RR; Probst, C; Rees, DC; Richers, CP; Spatzal, T; Yang, J1
Enemark, JH1
Fettig, RR; Mendel, RR; Oliphant, KD; Snoozy, J; Warnhoff, K1
Behnecke, M; Biedendieck, R; Hänsch, R; Hänsch, VG; Hercher, TW; Hertweck, C; Kaufholdt, D; Knüppel, L; Mendel, RR; Minner-Meinen, R; Schulze, J; Sivov, S; van den Hout, L; Weber, JN1
Hassan, AH; Iacobucci, C; Ihling, C; Kastritis, PL; Kruse, T; Sinz, A1

Reviews

42 review(s) available for pteridines and molybdenum

ArticleYear
Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli.
    Biochimica et biophysica acta, 1992, Aug-28, Volume: 1102, Issue:1

    Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Coenzymes; Dimethyl Sulfoxide; Electron Spin Resonance Spectroscopy; Escherichia coli; Iron-Sulfur Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases, N-Demethylating; Pteridines

1992
The pterin molybdenum cofactors.
    The Journal of biological chemistry, 1992, May-25, Volume: 267, Issue:15

    Topics: Coenzymes; Escherichia coli; Genes, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines

1992
Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains.
    Biochimica et biophysica acta, 1991, Mar-29, Volume: 1057, Issue:2

    Topics: Amino Acid Sequence; Coenzymes; Enzymes; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Pteridines; Sequence Alignment

1991
Biogenesis of molybdenum cofactors.
    Critical reviews in microbiology, 1990, Volume: 17, Issue:3

    Topics: Biological Transport; Chlorates; Coenzymes; Drug Resistance, Microbial; Escherichia coli; Genes, Bacterial; Iron; Metalloproteins; Models, Biological; Molecular Structure; Molybdenum; Molybdenum Cofactors; Mutation; Nitrogenase; Pteridines; Pterins

1990
Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin.
    Annual review of biochemistry, 1985, Volume: 54

    Topics: Alcohol Oxidoreductases; Animals; Biopterins; Body Fluids; Coenzymes; GTP Cyclohydrolase; Humans; Immune System Diseases; Mental Disorders; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neoplasms; Nervous System Diseases; Phenylalanine; Phenylketonurias; Pteridines; Pterins; Tetrahydrofolate Dehydrogenase; Tissue Distribution; Tryptophan Hydroxylase; Tyrosine 3-Monooxygenase

1985
Nitrate respiration in relation to facultative metabolism in enterobacteria.
    Microbiological reviews, 1988, Volume: 52, Issue:2

    Topics: Anaerobiosis; Coenzymes; Enterobacteriaceae; Formates; Hydrogen; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Nitrates; Nitrites; Pteridines

1988
Molybdopterin--problems and perspectives.
    BioFactors (Oxford, England), 1988, Volume: 1, Issue:4

    Topics: Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Structure-Activity Relationship

1988
Molybdenum in nitrogenase.
    Annual review of biochemistry, 1984, Volume: 53

    Topics: Azotobacter; Coenzymes; Genes, Bacterial; Klebsiella pneumoniae; Metalloproteins; Molybdenum; Molybdenum Cofactors; Molybdoferredoxin; Nitrogen Fixation; Nitrogenase; Pteridines; Tungsten

1984
Chemistry and biology of the molybdenum cofactors.
    Advances in experimental medicine and biology, 1993, Volume: 338

    Topics: Animals; Bacteria; Coenzymes; Metalloproteins; Molecular Conformation; Molecular Structure; Molybdenum; Molybdenum Cofactors; Nucleotides; Oxidoreductases; Pteridines; Pterins

1993
Molybdenum-cofactor-containing enzymes: structure and mechanism.
    Annual review of biochemistry, 1997, Volume: 66

    Topics: Aldehyde Oxidoreductases; Animals; Bacteria; Coenzymes; Humans; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Conformation; Pteridines; Xanthine Oxidase

1997
Biosynthesis and processing of the molybdenum cofactors.
    Biochemical Society transactions, 1997, Volume: 25, Issue:3

    Topics: Biopterins; Coenzymes; Escherichia coli; Folic Acid; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Pteridines; Riboflavin; Sulfurtransferases

1997
Structure of the molybdenum cofactor genes in Drosophila.
    Biochemical Society transactions, 1997, Volume: 25, Issue:3

    Topics: Animals; Calcium-Binding Proteins; Calnexin; Carrier Proteins; Coenzymes; Drosophila; Drosophila Proteins; Genes, Insect; Genes, Lethal; Mammals; Membrane Glycoproteins; Membrane Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Pteridines; Xanthine Dehydrogenase

1997
[Molybdenum cofactor deficiency].
    Ryoikibetsu shokogun shirizu, 1998, Issue:19 Pt 2

    Topics: Biomarkers; Coenzymes; Cysteine; Diagnosis, Differential; Female; Humans; Infant; Infant, Newborn; Male; Metal Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfites; Xanthine

1998
Structure and function of molybdopterin containing enzymes.
    Progress in biophysics and molecular biology, 1997, Volume: 68, Issue:2-3

    Topics: Coenzymes; Crystallography, X-Ray; Desulfovibrio; Escherichia coli; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Conformation; Pteridines; Rhodobacter sphaeroides; Xanthine Oxidase

1997
The active sites of molybdenum- and tungsten-containing enzymes.
    Current opinion in chemical biology, 1998, Volume: 2, Issue:2

    Topics: Aldehyde Oxidoreductases; Bacterial Proteins; Binding Sites; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Tungsten

1998
A structural comparison of molybdenum cofactor-containing enzymes.
    FEMS microbiology reviews, 1998, Volume: 22, Issue:5

    Topics: Bacteria, Anaerobic; Coenzymes; Humans; Hydro-Lyases; Metalloproteins; Mixed Function Oxygenases; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Tungsten; Xanthine Oxidase

1998
Genetics of molybdenum cofactor deficiency.
    Human genetics, 2000, Volume: 106, Issue:2

    Topics: Carbon-Carbon Lyases; Carrier Proteins; Coenzymes; Deficiency Diseases; Genetic Complementation Test; Genetic Therapy; Humans; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Nuclear Proteins; Pteridines; Sulfurtransferases

2000
Molybdopterin from molybdenum and tungsten enzymes.
    Advances in protein chemistry, 2001, Volume: 58

    Topics: Amino Acid Sequence; Coenzymes; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Protein Conformation; Pteridines; Tungsten

2001
Molybdenum and tungsten in biology.
    Trends in biochemical sciences, 2002, Volume: 27, Issue:7

    Topics: Aldehyde Oxidoreductases; Animals; Bacterial Proteins; Binding Sites; Coenzymes; Formate Dehydrogenases; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Structure, Tertiary; Pteridines; Tungsten; Xanthine Oxidase

2002
Molybdoenzymes and molybdenum cofactor in plants.
    Journal of experimental botany, 2002, Volume: 53, Issue:375

    Topics: Abscisic Acid; Aldehyde Oxidase; Aldehyde Oxidoreductases; Arabidopsis Proteins; Coenzymes; Enzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on Sulfur Group Donors; Plants; Pteridines; Sulfur; Xanthine Dehydrogenase

2002
[Molybdenum].
    Nihon rinsho. Japanese journal of clinical medicine, 2004, Volume: 62 Suppl 12

    Topics: Biomarkers; Coenzymes; Humans; Kidney Diseases; Liver Diseases; Mass Spectrometry; Metalloproteins; Molybdenum; Molybdenum Cofactors; Occupational Exposure; Pteridines; Reference Values; Renal Dialysis; Specimen Handling; Uric Acid

2004
Cell biology of molybdenum.
    Biochimica et biophysica acta, 2006, Volume: 1763, Issue:7

    Topics: Aldehyde Oxidase; Cell Biology; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Pteridines; Xanthine Dehydrogenase

2006
Biology of the molybdenum cofactor.
    Journal of experimental botany, 2007, Volume: 58, Issue:9

    Topics: Apoenzymes; Arabidopsis; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrite Reductases; Pteridines; Sulfite Oxidase

2007
Metal and cofactor insertion.
    Natural product reports, 2007, Volume: 24, Issue:5

    Topics: Coenzymes; Copper; Iron; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Pteridines

2007
Nitrate reductases: structure, functions, and effect of stress factors.
    Biochemistry. Biokhimiia, 2007, Volume: 72, Issue:10

    Topics: Bacteria; Bacterial Physiological Phenomena; Binding Sites; Coenzymes; Electrons; Metalloproteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; NAD; Nitrate Reductase; Nitrogen; Oxygen; Protein Conformation; Pteridines; Substrate Specificity; Temperature

2007
Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold.
    Microbiology and molecular biology reviews : MMBR, 2008, Volume: 72, Issue:2

    Topics: Amino Acid Motifs; Amino Acid Sequence; Coenzymes; Conserved Sequence; Evolution, Molecular; Humans; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Phylogeny; Protein Folding; Protein Structure, Secondary; Pteridines; Pterins; Sequence Alignment; Sulfite Oxidase

2008
Elucidating the catalytic mechanism of sulfite oxidizing enzymes using structural, spectroscopic, and kinetic analyses.
    Biochemistry, 2010, Aug-31, Volume: 49, Issue:34

    Topics: Animals; Binding Sites; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Humans; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Spectrum Analysis; Sulfite Dehydrogenase; Sulfite Oxidase; Sulfites

2010
Molybdenum metabolism in the alga Chlamydomonas stands at the crossroad of those in Arabidopsis and humans.
    Metallomics : integrated biometal science, 2011, Volume: 3, Issue:6

    Topics: Amino Acid Sequence; Arabidopsis; Chlamydomonas; Coenzymes; Humans; Membrane Transport Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Phylogeny; Pteridines; Sequence Homology, Amino Acid

2011
Cell biology of molybdenum in plants.
    Plant cell reports, 2011, Volume: 30, Issue:10

    Topics: Aldehyde Oxidase; Coenzymes; Metalloproteins; Mitochondrial Proteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Plants; Pteridines; Sulfite Oxidase; Xanthine Dehydrogenase

2011
Molybdenum enzymes and molybdenum cofactor in mycobacteria.
    Journal of cellular biochemistry, 2011, Volume: 112, Issue:10

    Topics: Aldehyde Oxidoreductases; Bacterial Proteins; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Mycobacterium; Nitrate Reductase; Oxidoreductases; Pteridines

2011
Cell biology of molybdenum in plants and humans.
    Biochimica et biophysica acta, 2012, Volume: 1823, Issue:9

    Topics: Adenosine Triphosphate; Aldehyde Oxidase; Coenzymes; Copper; Heredodegenerative Disorders, Nervous System; Humans; Infant, Newborn; Iron; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Oxidoreductases; Plants; Pteridines; Sulfite Oxidase; Sulfurtransferases; Xanthine Dehydrogenase

2012
The molybdenum cofactor.
    The Journal of biological chemistry, 2013, May-10, Volume: 288, Issue:19

    Topics: Animals; Biosynthetic Pathways; Coenzymes; Humans; Metalloexopeptidases; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organophosphorus Compounds; Pteridines; Pterins

2013
Molybdenum and tungsten oxygen transferases--and functional diversity within a common active site motif.
    Metallomics : integrated biometal science, 2014, Volume: 6, Issue:1

    Topics: Binding Sites; Catalytic Domain; Coenzymes; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum; Molybdenum Cofactors; Oxygen; Protein Structure, Tertiary; Pteridines; Transferases; Tungsten

2014
The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.
    Biochimica et biophysica acta, 2015, Volume: 1853, Issue:6

    Topics: Bacteria; Bacterial Proteins; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Models, Biological; Models, Chemical; Molecular Structure; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines

2015
The mammalian molybdenum enzymes of mARC.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015, Volume: 20, Issue:2

    Topics: Animals; Coenzymes; Cytochromes b5; Electron Transport; Humans; Mammals; Membrane Proteins; Metabolic Detoxication, Phase I; Metalloproteins; Mitochondria; Mitochondrial Proteins; Molybdenum; Molybdenum Cofactors; NAD; Oxidoreductases; Pteridines

2015
Biosynthesis and Insertion of the Molybdenum Cofactor.
    EcoSal Plus, 2015, Volume: 6, Issue:2

    Topics: Archaea; Bacteria; Biocatalysis; Coenzymes; Enzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Pteridines; Pterins; Sulfur; Tungsten

2015
From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC.
    Molecules (Basel, Switzerland), 2018, Dec-11, Volume: 23, Issue:12

    Topics: Animals; Cardiac Myosins; Coenzymes; Enzymes; Eukaryotic Cells; Mammals; Metabolic Networks and Pathways; Metalloproteins; Molybdenum; Molybdenum Cofactors; Myosin Light Chains; Nitrate Reductase; Nitrites; Oxidoreductases; Pteridines

2018
DMSO Reductase Family: Phylogenetics and Applications of Extremophiles.
    International journal of molecular sciences, 2019, Jul-08, Volume: 20, Issue:13

    Topics: Coenzymes; Extremophiles; Iron-Sulfur Proteins; Isoenzymes; Metabolic Networks and Pathways; Metalloproteins; Molybdenum; Molybdenum Cofactors; Multigene Family; Nitrogen Cycle; Oxidation-Reduction; Oxidoreductases; Phylogeny; Pteridines; Structure-Activity Relationship; Tungsten

2019
The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria.
    Metallomics : integrated biometal science, 2019, 10-16, Volume: 11, Issue:10

    Topics: Bacteria; Bacterial Proteins; Biosynthetic Pathways; Coenzymes; Escherichia coli; Gene Expression Regulation, Bacterial; Genes, Bacterial; Iron; Metalloproteins; Molybdenum; Molybdenum Cofactors; Multigene Family; Pteridines; Rhodobacter capsulatus; Shewanella

2019
The biosynthesis of the molybdenum cofactors in Escherichia coli.
    Environmental microbiology, 2020, Volume: 22, Issue:6

    Topics: Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organophosphorus Compounds; Pteridines; Pterins

2020
Molybdenum cofactor biology, evolution and deficiency.
    Biochimica et biophysica acta. Molecular cell research, 2021, Volume: 1868, Issue:1

    Topics: Coenzymes; Eukaryota; Gene Fusion; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Substrate Specificity

2021
Metal-Containing Formate Dehydrogenases, a Personal View.
    Molecules (Basel, Switzerland), 2023, Jul-11, Volume: 28, Issue:14

    Topics: Catalytic Domain; Coenzymes; Formate Dehydrogenases; Metalloproteins; Molybdenum; Oxidation-Reduction; Pteridines

2023

Other Studies

208 other study(ies) available for pteridines and molybdenum

ArticleYear
Characterization of molybdenum cofactor from Escherichia coli.
    Journal of bacteriology, 1979, Volume: 140, Issue:1

    Topics: Centrifugation, Density Gradient; Chromatography, Gel; Coenzymes; Dialysis; Escherichia coli; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Pteridines

1979
Molybdenum cofactor (chlorate-resistant) mutants of Klebsiella pneumoniae M5al can use hypoxanthine as the sole nitrogen source.
    Journal of bacteriology, 1992, Volume: 174, Issue:19

    Topics: Chromosome Mapping; Coenzymes; Gene Expression Regulation, Bacterial; Genetic Complementation Test; Hypoxanthine; Hypoxanthines; Klebsiella pneumoniae; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis; Nitrate Reductase; Nitrate Reductases; Nitrogen; Pteridines; Transduction, Genetic; Tungsten; Tungsten Compounds

1992
Proposed nomenclature for the genes involved in molybdenum metabolism in Escherichia coli and Salmonella typhimurium.
    Molecular microbiology, 1992, Volume: 6, Issue:22

    Topics: Coenzymes; Escherichia coli; Genes, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Salmonella typhimurium; Terminology as Topic

1992
Identification of two tungstate-sensitive molybdenum cofactor mutants, chl2 and chl7, of Arabidopsis thaliana.
    Molecular & general genetics : MGG, 1992, Volume: 233, Issue:1-2

    Topics: Blotting, Northern; Blotting, Western; Coenzymes; Genetic Complementation Test; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Phenotype; Plant Development; Plants; Pteridines; RNA, Messenger; Tungsten; Tungsten Compounds

1992
Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli.
    Molecular microbiology, 1992, Volume: 6, Issue:2

    Topics: Blotting, Western; Coenzymes; Escherichia coli; Gene Expression; Iron; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Operon; Plasmids; Pteridines; Spectrometry, Fluorescence; Sulfur; Trypsin

1992
Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase.
    The Biochemical journal, 1992, Jul-15, Volume: 285 ( Pt 2)

    Topics: Amino Acid Sequence; Animals; Binding Sites; Chromatography, Gel; Coenzymes; Drosophila melanogaster; Flavin-Adenine Dinucleotide; Iron-Sulfur Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; NAD; Pteridines; Sequence Alignment; Structure-Activity Relationship; Xanthine Dehydrogenase

1992
Identification of a molybdopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa.
    BioFactors (Oxford, England), 1991, Volume: 3, Issue:2

    Topics: Animals; Chickens; Chromatography, Gel; Chromatography, High Pressure Liquid; Coenzymes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Pseudomonas aeruginosa; Pteridines; Spectrum Analysis; Xanthine Dehydrogenase

1991
Regulation of molybdenum cofactor species in the green alga Chlamydomonas reinhardtii.
    Biochimica et biophysica acta, 1991, Apr-09, Volume: 1073, Issue:3

    Topics: Ammonium Chloride; Carrier Proteins; Chlamydomonas; Chromatography, Gel; Coenzymes; Hot Temperature; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Nitrogen; Pteridines

1991
31P ENDOR studies of xanthine oxidase: coupling of phosphorus of the pterin cofactor to molybdenum (V).
    Biochemistry, 1991, Apr-23, Volume: 30, Issue:16

    Topics: Animals; Cattle; Coenzymes; Electron Spin Resonance Spectroscopy; Female; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; Phosphorus; Protein Binding; Pteridines; Xanthine Oxidase

1991
Regulation of the chlA locus of Escherichia coli K12: involvement of molybdenum cofactor.
    Molecular microbiology, 1991, Volume: 5, Issue:4

    Topics: Anaerobiosis; beta-Galactosidase; Chlorates; Coenzymes; Drug Resistance, Microbial; Escherichia coli; Gene Expression Regulation, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductase; Nitrate Reductases; Pteridines; Recombinant Fusion Proteins

1991
Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.
    The Biochemical journal, 1991, Feb-15, Volume: 274 ( Pt 1)

    Topics: Chromatography, Gel; Chromatography, Ion Exchange; Coenzymes; Electrophoresis, Polyacrylamide Gel; Iron-Sulfur Proteins; Kinetics; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines; Rhodobacter capsulatus; Spectrometry, Fluorescence; Spectrophotometry

1991
Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme.
    Biological chemistry Hoppe-Seyler, 1990, Volume: 371, Issue:12

    Topics: Coenzymes; Flavin-Adenine Dinucleotide; Flavoproteins; Iron; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Pseudomonas; Pteridines; Soil Microbiology; Spectrophotometry; Sulfur

1990
Oxidation-reduction potentials of flavin and Mo-pterin centers in assimilatory nitrate reductase: variation with pH.
    Biochemistry, 1990, Dec-04, Volume: 29, Issue:48

    Topics: Chlorella; Circular Dichroism; Coenzymes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Potentiometry; Pteridines

1990
Antenatal diagnosis of molybdenum cofactor deficiency.
    American journal of obstetrics and gynecology, 1990, Volume: 163, Issue:4 Pt 1

    Topics: Adult; Amniocentesis; Amniotic Fluid; Cells, Cultured; Chorionic Villi; Coenzymes; Female; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pregnancy; Prenatal Diagnosis; Pteridines

1990
Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans.
    Proceedings of the National Academy of Sciences of the United States of America, 1990, Volume: 87, Issue:8

    Topics: Chromatography, High Pressure Liquid; Coenzymes; Guanine Nucleotides; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines; Pterins; Rhodobacter sphaeroides; Spectrophotometry

1990
The state of reduction of molybdopterin in xanthine oxidase and sulfite oxidase.
    The Journal of biological chemistry, 1990, Aug-05, Volume: 265, Issue:22

    Topics: Animals; Cattle; Chickens; Coenzymes; Female; Liver; Metalloproteins; Milk; Molecular Structure; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Rats; Spectrophotometry; Xanthine Oxidase

1990
Homologous transformation of Cephalosporium acremonium with the nitrate reductase-encoding gene (niaD).
    Gene, 1990, Jun-15, Volume: 90, Issue:2

    Topics: Acremonium; Benomyl; Chlorates; Coenzymes; Drug Resistance, Microbial; Gene Frequency; Genes, Fungal; Genetic Markers; Hygromycin B; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductase; Nitrate Reductases; Pteridines; Restriction Mapping; Transformation, Genetic

1990
Molybdenum cofactor biosynthesis in humans. Identification of two complementation groups of cofactor-deficient patients and preliminary characterization of a diffusible molybdopterin precursor.
    The Journal of clinical investigation, 1989, Volume: 83, Issue:3

    Topics: Cells, Cultured; Coenzymes; Escherichia coli; Fibroblasts; Humans; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Precursors; Pteridines

1989
The structure of a molybdopterin precursor. Characterization of a stable, oxidized derivative.
    The Journal of biological chemistry, 1989, Aug-15, Volume: 264, Issue:23

    Topics: Alkaline Phosphatase; Animals; Chickens; Coenzymes; Escherichia coli; Intestines; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Mutation; Phosphorus; Pteridines; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfur

1989
Escherichia coli molybdoenzymes can be activated by protein FA from several gram-negative bacteria.
    Journal of general microbiology, 1989, Volume: 135, Issue:12

    Topics: Bacterial Proteins; Coenzymes; Enterobacteriaceae; Enzyme Activation; Escherichia coli; Formate Dehydrogenases; Metalloproteins; Molybdenum; Molybdenum Cofactors; NADH, NADPH Oxidoreductases; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on CH-NH Group Donors; Pteridines

1989
The isolation of demolybdo xanthine oxidase from bovine milk.
    The Biochemical journal, 1988, Nov-01, Volume: 255, Issue:3

    Topics: Animals; Chromatography, Affinity; Coenzymes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; NAD; Pteridines; Spectrophotometry; Xanthine Oxidase

1988
Regulation of Chlorella nitrate reductase: control of enzyme activity and immunoreactive protein levels by ammonia.
    Archives of biochemistry and biophysics, 1989, Feb-15, Volume: 269, Issue:1

    Topics: Ammonia; Animals; Chlorella; Coenzymes; Enzyme Activation; Enzyme Induction; Enzyme Repression; Enzyme-Linked Immunosorbent Assay; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Nitrates; Protein Biosynthesis; Protein Synthesis Inhibitors; Pteridines; Rabbits

1989
Evidence for a pterin-derivative associated with the molybdenum cofactor of Neurospora crassa nitrate reductase.
    Photochemistry and photobiology, 1985, Volume: 42, Issue:6

    Topics: Chromatography, Affinity; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora; Neurospora crassa; Nitrate Reductases; Pteridines

1985
Assay and detection of the molybdenum cofactor.
    Methods in enzymology, 1986, Volume: 122

    Topics: Coenzymes; Enzymes; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora crassa; Nitrate Reductases; Oxidation-Reduction; Protein Binding; Pteridines; Spectrophotometry

1986
Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis.
    Journal of bacteriology, 1987, Volume: 169, Issue:1

    Topics: Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; Formate Dehydrogenases; Genes, Bacterial; Genetic Complementation Test; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Nitrogenase; Pteridines; Spectrometry, Fluorescence

1987
The pterin (bactopterin) of carbon monoxide dehydrogenase from Pseudomonas carboxydoflava.
    European journal of biochemistry, 1986, May-15, Volume: 157, Issue:1

    Topics: Aldehyde Oxidoreductases; Chromatography, Gel; Chromatography, Thin Layer; Coenzymes; Cytosine Nucleotides; Flavin-Adenine Dinucleotide; Formamides; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Perchlorates; Phosphates; Pseudomonas; Pteridines; Pterins

1986
Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis.
    Journal of bacteriology, 1988, Volume: 170, Issue:9

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cloning, Molecular; Coenzymes; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Genes, Bacterial; Genetic Complementation Test; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Operon; Plasmids; Promoter Regions, Genetic; Pteridines

1988
Molybdenum hydroxylases in Drosophila. III. Further characterization of the low xanthine dehydrogenase gene.
    Biochemical genetics, 1986, Volume: 24, Issue:7-8

    Topics: Alleles; Animals; Coenzymes; Drosophila melanogaster; Ethyl Methanesulfonate; Genes; Genetic Complementation Test; Genotype; Homozygote; Ketone Oxidoreductases; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Pteridines; Xanthine Dehydrogenase

1986
Molybdenum-sensitive transcriptional regulation of the chlD locus of Escherichia coli.
    Journal of bacteriology, 1987, Volume: 169, Issue:5

    Topics: beta-Galactosidase; Coenzymes; Enzyme Induction; Escherichia coli; Gene Expression Regulation; Genes, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Nitrates; Pteridines; Recombinant Proteins; Transcription, Genetic; Tungsten

1987
Chemistry and biology of the molybdenum cofactor.
    Biochemical Society transactions, 1985, Volume: 13, Issue:2

    Topics: Animals; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora crassa; Oxidation-Reduction; Pteridines; Sulfhydryl Reagents

1985
Molybdenum cofactor deficiency in a patient previously characterized as deficient in sulfite oxidase.
    Biochemical medicine and metabolic biology, 1988, Volume: 40, Issue:1

    Topics: Cells, Cultured; Coenzymes; Fibroblasts; Humans; Hypoxanthine; Hypoxanthines; Infant; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Uric Acid; Xanthine; Xanthine Dehydrogenase; Xanthines

1988
Trimethylamine oxidation in liver tissue is not catalyzed by a molybdenum cofactor-dependent enzyme.
    BioFactors (Oxford, England), 1988, Volume: 1, Issue:2

    Topics: Animals; Coenzymes; Liver; Male; Metalloproteins; Methylamines; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Oxidoreductases, N-Demethylating; Pteridines; Rats; Reference Values; Tungsten

1988
Elicitation of thiomolybdates from the iron-molybdenum cofactor of nitrogenase. Comparison with synthetic Fe-Mo-S complexes.
    European journal of biochemistry, 1986, Aug-15, Volume: 159, Issue:1

    Topics: Azotobacter; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Oxidation-Reduction; Oxidoreductases; Pteridines; Spectrophotometry; Sulfur

1986
Molybdenum cofactor: a compound in the in vitro activation of both nitrate reductase and trimethylamine-N-oxide reductase activities in Escherichia coli K12.
    Biochimica et biophysica acta, 1986, Aug-15, Volume: 872, Issue:3

    Topics: Coenzymes; Enzyme Activation; Escherichia coli; Genetic Complementation Test; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; NADH, NADPH Oxidoreductases; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on CH-NH Group Donors; Pteridines

1986
Further characterization of trimethylamine N-oxide reductase from Escherichia coli, a molybdoprotein.
    Journal of biochemistry, 1986, Volume: 99, Issue:6

    Topics: Catalysis; Coenzymes; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; NADH, NADPH Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; Pteridines; Spectrometry, Fluorescence

1986
In vitro system for molybdopterin biosynthesis.
    Journal of bacteriology, 1987, Volume: 169, Issue:1

    Topics: Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; In Vitro Techniques; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxygen; Protein Precursors; Pteridines; Pterins

1987
Cloning, expression and sequencing the molybdenum-pterin binding protein (mop) gene of Clostridium pasteurianum in Escherichia coli.
    Nucleic acids research, 1986, Dec-09, Volume: 14, Issue:23

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Carrier Proteins; Chromosome Mapping; Cloning, Molecular; Clostridium; Coenzymes; DNA-Binding Proteins; DNA, Bacterial; Escherichia coli; Genes, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Pterins

1986
The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase.
    The Journal of biological chemistry, 1987, Dec-05, Volume: 262, Issue:34

    Topics: Animals; Cattle; Chemical Phenomena; Chemistry, Physical; Chickens; Coenzymes; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Pterins; Xanthine Oxidase

1987
Molybdopterin cofactor from Methanobacterium formicicum formate dehydrogenase.
    Journal of bacteriology, 1986, Volume: 166, Issue:2

    Topics: Aldehyde Oxidoreductases; Chromatography, Gel; Chromatography, High Pressure Liquid; Coenzymes; Euryarchaeota; Formate Dehydrogenases; Hydrogen-Ion Concentration; Metalloproteins; Molybdenum; Molybdenum Cofactors; Phosphates; Pteridines; Spectrometry, Fluorescence

1986
The equilibration of reducing equivalents within milk xanthine oxidase.
    The Journal of biological chemistry, 1986, Jan-25, Volume: 261, Issue:3

    Topics: Animals; Cattle; Chemical Phenomena; Chemistry, Physical; Female; Flavins; Hydrogen-Ion Concentration; Kinetics; Milk; Molybdenum; Oxidation-Reduction; Oxypurinol; Photolysis; Pteridines; Temperature; Xanthine Oxidase

1986
[Combined sulfite and xanthine oxidase deficiency due to an anomaly in the metabolism of molybdenum cofactor].
    Annales de pediatrie, 1986, Volume: 33, Issue:9

    Topics: Coenzymes; Humans; Infant, Newborn; Male; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfites; Uric Acid; Xanthine Oxidase

1986
[Sulfite and xanthine oxidase deficiency: a diagnosis based on 2 simple tests].
    Annales de pediatrie, 1986, Volume: 33, Issue:9

    Topics: Coenzymes; Female; Humans; Infant; Metabolism, Inborn Errors; Metalloproteins; Methods; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfites; Uric Acid; Xanthine Oxidase

1986
Identification of molybdoproteins in Clostridium pasteurianum.
    Journal of bacteriology, 1985, Volume: 162, Issue:2

    Topics: Anaerobiosis; Bacterial Proteins; Clostridium; Coenzymes; Formate Dehydrogenases; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrogenase; Pteridines; Sulfates

1985
Absence of hepatic molybdenum cofactor. An inborn error of metabolism associated with lens dislocation.
    Ophthalmic paediatrics and genetics, 1985, Volume: 5, Issue:3

    Topics: Coenzymes; Female; Humans; Infant; Infant, Newborn; Lens Subluxation; Liver; Male; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pregnancy; Prenatal Diagnosis; Pteridines

1985
Anatomo-pathological findings in a case of combined deficiency of sulphite oxidase and xanthine oxidase with a defect of molybdenum cofactor.
    Virchows Archiv. A, Pathological anatomy and histopathology, 1985, Volume: 405, Issue:3

    Topics: Amino Acid Metabolism, Inborn Errors; Amino Acids, Sulfur; Brain; Child, Preschool; Coenzymes; Female; Humans; Liver; Metalloproteins; Microcephaly; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; Sulfates; Syndrome; Xanthine Oxidase; Xanthines

1985
Identification of a dephosphorylated oxidation product of the molybdenum cofactor as 2-(1,2-dihydroxyethyl)thieno[3,2-g]pterin.
    Biochemical and biophysical research communications, 1986, Feb-26, Volume: 135, Issue:1

    Topics: Chromatography, Thin Layer; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Pteridines; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

1986
Studies by electron-paramagnetic-resonance spectroscopy of the environment of the metal in the molybdenum cofactor of molybdenum-containing enzymes.
    The Biochemical journal, 1984, Sep-15, Volume: 222, Issue:3

    Topics: Chromatography, Gel; Coenzymes; Electron Spin Resonance Spectroscopy; Mercaptoethanol; Metalloproteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Phenols; Pteridines; Sulfhydryl Compounds; Xanthine Oxidase

1984
The relationship of Mo, molybdopterin, and the cyanolyzable sulfur in the Mo cofactor.
    Archives of biochemistry and biophysics, 1984, Volume: 230, Issue:1

    Topics: Animals; Chemical Phenomena; Chemistry; Chickens; Chromatography, High Pressure Liquid; Coenzymes; Ethylmaleimide; Hydrogen-Ion Concentration; Liver; Mercury; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora crassa; Nitrate Reductase (NADH); Nitrate Reductases; Protein Denaturation; Pteridines; Sulfhydryl Compounds; Sulfides; Tungsten; Tungsten Compounds; Xanthine Dehydrogenase

1984
Quantitative transfer of the molybdenum cofactor from xanthine oxidase and from sulphite oxidase to the deficient enzyme of the nit-1 mutant of Neurospora crassa to yield active nitrate reductase.
    The Biochemical journal, 1984, Apr-15, Volume: 219, Issue:2

    Topics: Apoenzymes; Apoproteins; Coenzymes; Dithiothreitol; Enzyme Activation; Metalloproteins; Methods; Molybdenum; Molybdenum Cofactors; Mutation; NADP; Neurospora; Neurospora crassa; Nitrate Reductase (NADH); Nitrate Reductases; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Oxygen; Pteridines; Xanthine Oxidase

1984
In vitro reconstitution of nitrate reductase activity of the Neurospora crassa mutant nit-1: specific incorporation of molybdopterin.
    Archives of biochemistry and biophysics, 1984, Volume: 233, Issue:2

    Topics: Amino Acids; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora; Neurospora crassa; Nitrate Reductases; Pteridines; Spectrometry, Fluorescence

1984
Stoichiometry and spectral properties of the MoFe cofactor and noncofactor redox centers in the MoFe protein of nitrogenase from Azotobacter vinelandii.
    Biochemistry, 1981, Dec-08, Volume: 20, Issue:25

    Topics: Anaerobiosis; Azotobacter; Coenzymes; Electron Spin Resonance Spectroscopy; Ferredoxins; Kinetics; Metalloproteins; Methylene Blue; Molybdenum; Molybdenum Cofactors; Molybdoferredoxin; Nitrogenase; Oxidation-Reduction; Pteridines

1981
Molybdenum(V) e.p.r. signals obtained from xanthine oxidase on reduction with aldehyde substrates and with 2-amino-4-hydroxy-6-formylpteridine.
    The Biochemical journal, 1981, Aug-01, Volume: 197, Issue:2

    Topics: Aldehydes; Chemical Phenomena; Chemistry; Electron Spin Resonance Spectroscopy; Molybdenum; Oxidation-Reduction; Pteridines; Pterins; Xanthine Oxidase

1981
Molybdenum cofactor in chlorate-resistant and nitrate reductase-deficient insertion mutants of Escherichia coli.
    Journal of bacteriology, 1983, Volume: 155, Issue:2

    Topics: Chlorates; Coenzymes; DNA Transposable Elements; Drug Resistance, Microbial; Escherichia coli; Genes, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductases; Phenotype; Pteridines

1983
The role of molybdenum in human biology.
    Journal of inherited metabolic disease, 1983, Volume: 6 Suppl 1

    Topics: Chemical Phenomena; Chemistry; Coenzymes; Electron Probe Microanalysis; Electron Spin Resonance Spectroscopy; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Xanthine Dehydrogenase; Xanthine Oxidase

1983
Identification of the dye gene product, mutational loss of which alters envelope protein composition and also affects sex factor F expression in Escherichia coli K-12.
    Molecular & general genetics : MGG, 1984, Volume: 194, Issue:1-2

    Topics: Alkaline Phosphatase; Bacterial Outer Membrane Proteins; Bacterial Proteins; Biological Transport; Coenzymes; Coloring Agents; DNA Transposable Elements; Escherichia coli; Escherichia coli Proteins; F Factor; Gene Expression Regulation; Membrane Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Plasmids; Pteridines; Repressor Proteins

1984
Formation of thieno[3,2-g]pterines from the molybdenum cofactor.
    Biochemical and biophysical research communications, 1983, Mar-16, Volume: 111, Issue:2

    Topics: Animals; Cattle; Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Pteridines; Pterins; Spectrometry, Fluorescence; Xanthine Oxidase

1983
Evidence for gene sharing in the nitrate reduction systems of Pseudomonas aeruginosa.
    Journal of bacteriology, 1983, Volume: 155, Issue:3

    Topics: Coenzymes; Genes, Bacterial; Hypoxanthine; Hypoxanthines; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductases; Nitrates; Oxidation-Reduction; Pseudomonas aeruginosa; Pteridines

1983
Absence of hepatic molybdenum cofactor: an inborn error of metabolism leading to a combined deficiency of sulphite oxidase and xanthine dehydrogenase.
    Journal of inherited metabolic disease, 1983, Volume: 6 Suppl 1

    Topics: Child, Preschool; Coenzymes; Humans; Infant; Infant, Newborn; Ketone Oxidoreductases; Liver; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Xanthine Dehydrogenase

1983
Molybdenum cofactor requirement for biotin sulfoxide reduction in Escherichia coli.
    Journal of bacteriology, 1982, Volume: 149, Issue:2

    Topics: Acids; Bacteriophage lambda; Biotin; Chromosome Mapping; Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductases; Oxidation-Reduction; Oxidoreductases; Pteridines; Tungsten; Tungsten Compounds; Virus Activation

1982
The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.
    The Journal of biological chemistry, 1984, May-10, Volume: 259, Issue:9

    Topics: Animals; Chickens; Coenzymes; Liver; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Rats; Spectrometry, Fluorescence; Spectrophotometry; Xanthine Oxidase

1984
Mass spectrometric analysis of fluorescent products originating from the molybdenum cofactor.
    Biochemistry international, 1984, Volume: 8, Issue:1

    Topics: Animals; Cattle; Coenzymes; Female; Mass Spectrometry; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; Pteridines; Spectrometry, Fluorescence; Xanthine Oxidase

1984
Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria.
    Journal of bacteriology, 1984, Volume: 157, Issue:2

    Topics: Aldehyde Oxidoreductases; Animals; Cattle; Chickens; Coenzymes; Female; Flavin-Adenine Dinucleotide; Liver; Metalloproteins; Milk; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Pseudomonas; Pteridines; Species Specificity; Spectrophotometry; Xanthine Dehydrogenase

1984
Molybdenum cofactor from the cytoplasmic membrane of Proteus mirabilis.
    Archives of microbiology, 1982, Dec-03, Volume: 133, Issue:4

    Topics: Cell Membrane; Chlorates; Chromatography, Gel; Coenzymes; Cytoplasm; Fluorescence; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Proteus mirabilis; Pteridines; Xanthine Oxidase

1982
Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component.
    The Journal of biological chemistry, 1980, Mar-10, Volume: 255, Issue:5

    Topics: Animals; Chickens; Coenzymes; Liver; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Rats; Spectrometry, Fluorescence; Spectrophotometry; Xanthine Oxidase

1980
Charge transfer complexes between pteridine substrates and the active center molybdenum of xanthine oxidase.
    The Journal of biological chemistry, 1982, Dec-25, Volume: 257, Issue:24

    Topics: Anaerobiosis; Animals; Binding Sites; Cattle; Dithionite; Female; Kinetics; Milk; Molybdenum; Oxidation-Reduction; Pteridines; Spectrophotometry; Xanthine Oxidase

1982
[Double deficiency of sulfite and xanthine oxidase causing encephalopathy and due to a hereditary anomaly in the metabolism of molybdenum].
    Annales de medecine interne, 1982, Volume: 133, Issue:8

    Topics: Brain Diseases, Metabolic; Coenzymes; Consanguinity; Female; Humans; Infant; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; Xanthine Oxidase

1982
Molybdenum hydroxylases in Drosophila. II. Molybdenum cofactor in xanthine dehydrogenase, aldehyde oxidase and pyridoxal oxidase.
    Molecular & general genetics : MGG, 1981, Volume: 184, Issue:1

    Topics: Aldehyde Oxidoreductases; Animals; Coenzymes; Drosophila; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Pteridines; Pyridoxaminephosphate Oxidase; Xanthine Dehydrogenase

1981
Structural and metabolic relationship between the molybdenum cofactor and urothione.
    Proceedings of the National Academy of Sciences of the United States of America, 1982, Volume: 79, Issue:22

    Topics: Animals; Chickens; Coenzymes; Liver; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Spectrometry, Fluorescence; Spectrophotometry

1982
Inborn errors of molybdenum metabolism: combined deficiencies of sulfite oxidase and xanthine dehydrogenase in a patient lacking the molybdenum cofactor.
    Proceedings of the National Academy of Sciences of the United States of America, 1980, Volume: 77, Issue:6

    Topics: Child, Preschool; Coenzymes; Female; Fibroblasts; Humans; Immunologic Techniques; Intellectual Disability; Ketone Oxidoreductases; Lens Subluxation; Liver; Metal Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nervous System Diseases; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Xanthine Dehydrogenase

1980
Identification of the molybdenum cofactor in chlorate-resistant mutants of Escherichia coli.
    Journal of bacteriology, 1981, Volume: 148, Issue:1

    Topics: Chlorates; Coenzymes; Drug Resistance, Microbial; Enzyme Induction; Escherichia coli; Formate Dehydrogenases; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductases; Pteridines

1981
The influence of growth conditions on the synthesis of molybdenum cofactor in Proteins mirabilis.
    Archives of microbiology, 1981, Volume: 130, Issue:1

    Topics: Aerobiosis; Anaerobiosis; Chlorates; Coenzymes; Culture Media; Drug Resistance, Microbial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Proteus mirabilis; Pteridines; Tungsten; Tungsten Compounds

1981
Proton translocation coupled to trimethylamine N-oxide reduction in anaerobically grown Escherichia coli.
    Journal of bacteriology, 1981, Volume: 148, Issue:3

    Topics: Anaerobiosis; Chlorates; Coenzymes; Escherichia coli; Hydrogen; Hydrogen-Ion Concentration; Membrane Potentials; Metalloproteins; Methylamines; Molybdenum; Molybdenum Cofactors; NADH, NADPH Oxidoreductases; Nitrate Reductases; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Pteridines

1981
Intragenic complementation by the nifJ-coded protein of Klebsiella pneumoniae.
    Journal of bacteriology, 1982, Volume: 150, Issue:1

    Topics: Bacterial Proteins; Chromosome Mapping; Chromosomes, Bacterial; Coenzymes; Genes, Bacterial; Genetic Complementation Test; Hot Temperature; Iron; Klebsiella pneumoniae; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Mutation; Nitrogen Fixation; Nitrogenase; Pteridines

1982
Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci.
    Journal of bacteriology, 1982, Volume: 151, Issue:2

    Topics: Apoenzymes; Chlorates; Coenzymes; Escherichia coli; Genes; Genes, Bacterial; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductases; Pteridines

1982
Purification of molybdenum cofactor and its fluorescent oxidation products.
    FEBS letters, 1982, Jun-01, Volume: 142, Issue:1

    Topics: Chromatography, High Pressure Liquid; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Proteus mirabilis; Pteridines; Spectrometry, Fluorescence

1982
A possible regulatory gene for the molybdenum-containing cofactor in Aspergillus nidulans.
    Journal of general microbiology, 1982, Volume: 128, Issue:5

    Topics: Aspergillus nidulans; Chromosome Mapping; Coenzymes; Genes, Regulator; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductases; Phenotype; Pteridines; Xanthine Dehydrogenase

1982
Defective molybdopterin biosynthesis: clinical heterogeneity associated with molybdenum cofactor deficiency.
    Journal of inherited metabolic disease, 1995, Volume: 18, Issue:3

    Topics: Adult; Coenzymes; Humans; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; Purines; Radiography; Spine; Sulfur

1995
Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.
    Science (New York, N.Y.), 1995, Nov-17, Volume: 270, Issue:5239

    Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Animals; Coenzymes; Crystallization; Crystallography, X-Ray; Cytosine Nucleotides; Desulfovibrio; Drosophila melanogaster; Electron Transport; Hydrogen Bonding; Iron; Ligands; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Protein Conformation; Protein Folding; Protein Structure, Secondary; Pteridines; Pterins; Xanthine; Xanthine Oxidase; Xanthines

1995
Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas.
    Journal of bacteriology, 1995, Volume: 177, Issue:21

    Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Anaerobiosis; Benzyl Viologen; Coenzymes; Desulfovibrio; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Inhibitors; Metalloproteins; Molecular Sequence Data; Molecular Weight; Molybdenum; Molybdenum Cofactors; Protein Conformation; Pteridines; Sequence Analysis; Spectrometry, Fluorescence; Substrate Specificity; Sulfur; Tungsten

1995
An HPLC assay for detection of elevated urinary S-sulphocysteine, a metabolic marker of sulphite oxidase deficiency.
    Journal of inherited metabolic disease, 1995, Volume: 18, Issue:1

    Topics: Amino Acids; Biomarkers; Chromatography, High Pressure Liquid; Coenzymes; Cysteine; Humans; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Taurine

1995
Molybdenum cofactor deficiency associated with Dandy-Walker malformation.
    Journal of inherited metabolic disease, 1995, Volume: 18, Issue:1

    Topics: Coenzymes; Dandy-Walker Syndrome; Humans; Infant, Newborn; Kidney Calculi; Lens Subluxation; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nervous System Diseases; Pteridines; Ultrasonography

1995
Effect of allopurinol on the xanthinuria in a patient with molybdenum cofactor deficiency.
    Advances in experimental medicine and biology, 1994, Volume: 370

    Topics: Allopurinol; Coenzymes; Female; Humans; Male; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; Xanthine; Xanthine Dehydrogenase; Xanthines

1994
Regulation of the molybdate transport operon, modABCD, of Escherichia coli in response to molybdate availability.
    Journal of bacteriology, 1995, Volume: 177, Issue:4

    Topics: Alleles; Bacterial Proteins; Base Sequence; Biological Transport; Coenzymes; DNA-Binding Proteins; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; Nitrates; Operon; Oxygen; Phosphoproteins; Promoter Regions, Genetic; Protein Kinases; Pteridines; Recombinant Fusion Proteins; Repressor Proteins

1995
Resonance Raman spectroscopic characterization of the molybdopterin active site of DMSO reductase.
    Biochemistry, 1995, Mar-07, Volume: 34, Issue:9

    Topics: Binding Sites; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Models, Chemical; Molecular Structure; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Protein Denaturation; Pteridines; Pterins; Rhodobacter sphaeroides; Spectrophotometry; Spectrum Analysis, Raman

1995
Molybdenum cofactor biosynthesis in Neurospora crassa: biochemical characterization of pleiotropic molybdoenzyme mutants nit-7, nit-8, nit-9A, B and C.
    Photochemistry and photobiology, 1995, Volume: 61, Issue:1

    Topics: Coenzymes; Enzyme Precursors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Pteridines

1995
The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein.
    European journal of biochemistry, 1994, Jun-15, Volume: 222, Issue:3

    Topics: Amino Acid Sequence; Amino Acids; Bacterial Proteins; Coenzymes; Electrophoresis, Polyacrylamide Gel; Iron-Sulfur Proteins; Isoelectric Point; Metalloproteins; Molecular Sequence Data; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Proteus vulgaris; Pteridines; Pterins; Substrate Specificity; Viologens

1994
The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin.
    Genetics, 1994, Volume: 137, Issue:3

    Topics: Amino Acid Sequence; Animals; Bacterial Proteins; Base Sequence; Brain Chemistry; Carrier Proteins; Cloning, Molecular; Coenzymes; Conserved Sequence; Drosophila; Drosophila Proteins; Escherichia coli; Female; Genes, Insect; Male; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nerve Tissue Proteins; Oxidoreductases; Pteridines; Rats; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid

1994
Molybdenum cofactor deficiency can mimic postanoxic encephalopathy.
    Journal of inherited metabolic disease, 1993, Volume: 16, Issue:5

    Topics: Child, Preschool; Coenzymes; Humans; Hypoxia, Brain; Infant, Newborn; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines

1993
Studies on the molybdenum cofactor. Synthesis of (+/-)-form B (dephospho).
    Advances in experimental medicine and biology, 1993, Volume: 338

    Topics: Coenzymes; Indicators and Reagents; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Pteridines; Stereoisomerism

1993
Molybdenum-pterin complexes: a functional and structural model for the binding site in the enzyme dimethyl sulfoxide reductase.
    Advances in experimental medicine and biology, 1993, Volume: 338

    Topics: Binding Sites; Coenzymes; Dimethyl Sulfoxide; Iron-Sulfur Proteins; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Molecular Conformation; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Pteridines; Pterins

1993
Human molybdenum cofactor deficiency.
    Advances in experimental medicine and biology, 1993, Volume: 338

    Topics: Biomarkers; Coenzymes; Humans; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Pterins

1993
Molybdopterin biosynthesis in man. Properties of the converting factor in liver tissue from a molybdenum cofactor deficient patient.
    Advances in experimental medicine and biology, 1993, Volume: 338

    Topics: Coenzymes; Escherichia coli; Humans; Liver; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora crassa; Pteridines; Sulfurtransferases

1993
Cloning of a eukaryotic molybdenum cofactor gene.
    Advances in experimental medicine and biology, 1993, Volume: 338

    Topics: Amino Acid Sequence; Animals; Cloning, Molecular; Coenzymes; Conserved Sequence; Drosophila; Escherichia coli; Gene Expression; Genes, Bacterial; Genes, Insect; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Pteridines; Sequence Homology, Amino Acid

1993
Molybdenum-cofactor deficiency: an easily missed cause of neonatal convulsions.
    Neuropediatrics, 1993, Volume: 24, Issue:3

    Topics: Amino Acids; Brain; Brain Diseases; Calcinosis; Chorionic Villi Sampling; Coenzymes; Female; Humans; Infant, Newborn; Male; Metabolic Diseases; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pregnancy; Prenatal Diagnosis; Prognosis; Pteridines; Spasms, Infantile; Tomography, X-Ray Computed; Xanthine Dehydrogenase

1993
Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii.
    The Biochemical journal, 1993, Jan-15, Volume: 289 ( Pt 2)

    Topics: Azotobacter vinelandii; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Coenzymes; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Iron; Kinetics; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Pteridines; Selenium; Spectrophotometry; Sulfides

1993
Molybdenum cofactor deficiency.
    The Journal of pediatrics, 1993, Volume: 123, Issue:4

    Topics: Coenzymes; Female; Genes, Recessive; Humans; Infant, Newborn; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Seizures

1993
[Remember hereditary metabolic diseases in children in which no satisfactory diagnosis can be established].
    Nederlands tijdschrift voor geneeskunde, 1993, May-08, Volume: 137, Issue:19

    Topics: Amidohydrolases; Amino Acid Metabolism, Inborn Errors; Biotinidase; Child; Child, Preschool; Coenzymes; Female; Humans; Infant, Newborn; Lysine; Male; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Multiple Carboxylase Deficiency; Pteridines

1993
Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three Escherichia coli proteins.
    The Plant journal : for cell and molecular biology, 1995, Volume: 8, Issue:5

    Topics: Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Base Sequence; Blotting, Southern; Calnexin; Carrier Proteins; Chromosome Mapping; Coenzymes; Drosophila Proteins; Escherichia coli; Genetic Complementation Test; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Plant Proteins; Pteridines; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Species Specificity

1995
Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants with altered beta subunits.
    European journal of biochemistry, 1995, Dec-15, Volume: 234, Issue:3

    Topics: Benzyl Viologen; Binding Sites; Coenzymes; Electron Transport; Escherichia coli; Iron-Sulfur Proteins; Kinetics; Metalloproteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Nitrates; Oxidation-Reduction; Pteridines; Solubility

1995
The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide.
    European journal of biochemistry, 1995, Dec-15, Volume: 234, Issue:3

    Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Base Sequence; Binding Sites; Chromosome Mapping; Cloning, Molecular; Coenzymes; DNA Primers; Escherichia coli; Ferredoxins; Genes, Bacterial; Iron-Sulfur Proteins; Metalloproteins; Methanobacterium; Molecular Sequence Data; Molecular Weight; Molybdenum; Molybdenum Cofactors; Operon; Pteridines; Sequence Alignment; Sequence Analysis; Tungsten

1995
Purification and characterization of a prokaryotic xanthine dehydrogenase from Comamonas acidovorans.
    Biochemistry, 1996, Apr-30, Volume: 35, Issue:17

    Topics: Animals; Cattle; Chickens; Circular Dichroism; Coenzymes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Gram-Negative Aerobic Bacteria; Iron-Sulfur Proteins; Kinetics; Macromolecular Substances; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Phosphates; Protein Structure, Secondary; Pteridines; Substrate Specificity; Xanthine Dehydrogenase

1996
The reductive half-reaction of xanthine oxidase. The involvement of prototropic equilibria in the course of the catalytic sequence.
    The Journal of biological chemistry, 1996, Mar-22, Volume: 271, Issue:12

    Topics: Catalysis; Electron Spin Resonance Spectroscopy; Fluorescent Dyes; Hydrogen-Ion Concentration; Kinetics; Molybdenum; Oxidation-Reduction; Pteridines; Purines; Solvents; Substrate Specificity; Xanthine; Xanthine Oxidase; Xanthines

1996
One molecule of molybdopterin guanine dinucleotide is associated with each subunit of the heterodimeric Mo-Fe-S protein transhydroxylase of Pelobacter acidigallici as determined by SDS/PAGE and mass spectrometry.
    European journal of biochemistry, 1996, Apr-15, Volume: 237, Issue:2

    Topics: Amino Acid Sequence; Bacteria, Anaerobic; Binding Sites; Coenzymes; Electron Spin Resonance Spectroscopy; Guanine Nucleotides; Iron-Sulfur Proteins; Mass Spectrometry; Metalloproteins; Mixed Function Oxygenases; Molecular Sequence Data; Molecular Structure; Molecular Weight; Molybdenum; Molybdenum Cofactors; Protein Conformation; Pteridines; Pterins

1996
Molybdenum bolsters the bioinorganic brigade.
    Science (New York, N.Y.), 1996, Jun-14, Volume: 272, Issue:5268

    Topics: Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oceans and Seas; Oxidoreductases; Protein Conformation; Pteridines; Sulfides

1996
Role and oxidation state of the pterin molybdenum cofactor of molybdenum enzymes: studies of a Drosophila melanogaster xanthine dehydrogenase (rosy) variant, G1011E.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Animals; Coenzymes; Cytochrome c Group; Drosophila melanogaster; Genetic Variation; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; NAD; Oxidation-Reduction; Pteridines; Xanthine Dehydrogenase

1996
Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor.
    European journal of biochemistry, 1996, Jul-15, Volume: 239, Issue:2

    Topics: Chromatography; Chromatography, Gel; Chromatography, Ion Exchange; Coenzymes; Dimethyl Sulfoxide; Durapatite; Electrophoresis, Polyacrylamide Gel; Heme; Kinetics; Macromolecular Substances; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Pteridines; Rhodobacter; Spectrophotometry; Substrate Specificity

1996
MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-pterin cofactor synthesis is an Fe-S protein.
    FEBS letters, 1996, Aug-05, Volume: 391, Issue:1-2

    Topics: Amino Acid Sequence; Arthrobacter; Base Sequence; Coenzymes; DNA Primers; Electron Spin Resonance Spectroscopy; Glutathione Transferase; Iron-Sulfur Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Pteridines; Recombinant Fusion Proteins; Sequence Tagged Sites

1996
Molybdenum cofactor biosynthesis in Escherichia coli mod and mog mutants.
    Journal of bacteriology, 1996, Volume: 178, Issue:14

    Topics: Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Pteridines

1996
Combined deficiency of xanthine oxidase and sulphite oxidase due to a deficiency of molybdenum cofactor.
    Journal of inherited metabolic disease, 1996, Volume: 19, Issue:5

    Topics: Coenzymes; Female; Fibroblasts; Humans; Hypoxanthine; Infant; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nervous System Diseases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Uric Acid; Xanthine; Xanthine Oxidase; Xanthines

1996
TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato.
    The Journal of biological chemistry, 1997, Jan-10, Volume: 272, Issue:2

    Topics: Aldehyde Oxidase; Aldehyde Oxidoreductases; Amino Acid Sequence; Animals; Base Sequence; Chromosome Mapping; Coenzymes; Humans; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Pteridines; Rats; Sequence Analysis, DNA; Solanum lycopersicum; Structure-Activity Relationship

1997
Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria.
    The Journal of clinical investigation, 1997, May-15, Volume: 99, Issue:10

    Topics: Adult; Aged; Codon; Coenzymes; DNA Primers; Duodenum; Humans; Intestinal Mucosa; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Point Mutation; Polymerase Chain Reaction; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; RNA, Messenger; Sequence Deletion; Xanthine; Xanthine Dehydrogenase; Xanthines

1997
Characterisation of the pterin molybdenum cofactor in dimethylsulfoxide reductase of Rhodobacter capsulatus.
    European journal of biochemistry, 1997, May-15, Volume: 246, Issue:1

    Topics: 2,6-Dichloroindophenol; Bacterial Proteins; Coenzymes; Electron Transport; Guanine Nucleotides; Guanosine Monophosphate; Iron-Sulfur Proteins; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Oxidation-Reduction; Oxidoreductases; Phosphates; Protein Denaturation; Pteridines; Pterins; Rhodobacter capsulatus; Spectrophotometry

1997
The Aspergillus nidulans cnxABC locus is a single gene encoding two catalytic domains required for synthesis of precursor Z, an intermediate in molybdenum cofactor biosynthesis.
    The Journal of biological chemistry, 1997, Nov-07, Volume: 272, Issue:45

    Topics: Amino Acid Sequence; Aspergillus nidulans; Base Sequence; Binding Sites; Catalysis; Chromatography, High Pressure Liquid; Cloning, Molecular; Coenzymes; Cosmids; DNA, Fungal; Enzyme Precursors; Fungal Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Pteridines; Restriction Mapping; Sequence Analysis, DNA

1997
> or = 95% of xanthine oxidase in human milk is present as the demolybdo form, lacking molybdopterin.
    Biochemical Society transactions, 1997, Volume: 25, Issue:3

    Topics: Coenzymes; Electron Spin Resonance Spectroscopy; Female; Humans; Metalloproteins; Milk, Human; Molybdenum; Molybdenum Cofactors; Pteridines; Xanthine Oxidase

1997
Molybdate-uptake genes and molybdopterin-biosynthesis genes on a bacterial plasmid--characterization of MoeA as a filament-forming protein with adenosinetriphosphatase activity.
    European journal of biochemistry, 1997, Dec-01, Volume: 250, Issue:2

    Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Base Sequence; Coenzymes; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multigene Family; Plasmids; Protein Conformation; Pteridines; Rats; Recombinant Proteins

1997
Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli.
    Journal of bacteriology, 1998, Volume: 180, Issue:6

    Topics: Bacterial Proteins; Chlorates; Cloning, Molecular; Coenzymes; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Formate Dehydrogenases; Genetic Complementation Test; Glucose; Hydrogen Sulfide; Hydrogenase; Metalloproteins; Methyltransferases; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitrate Reductase; Nitrate Reductases; Plasmids; Pteridines; Restriction Mapping; Sequence Deletion; Sulfates; Sulfides; Sulfotransferases; Sulfur; Sulfurtransferases

1998
Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit.
    Biochemistry, 1998, May-19, Volume: 37, Issue:20

    Topics: Cell Membrane; Coenzymes; Conserved Sequence; Electron Spin Resonance Spectroscopy; Enzyme Activation; Escherichia coli; Histidine; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Protein Binding; Pteridines

1998
NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli.
    Molecular microbiology, 1998, Volume: 28, Issue:3

    Topics: Cell Fractionation; Coenzymes; Electron Spin Resonance Spectroscopy; Enzyme Activation; Escherichia coli; Histidine; Metalloproteins; Molecular Chaperones; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Plasmids; Pteridines; Recombinant Proteins; Spectrometry, Fluorescence

1998
Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors.
    European journal of biochemistry, 1998, Jul-01, Volume: 255, Issue:1

    Topics: Carbon Isotopes; Coenzymes; Escherichia coli; Escherichia coli Proteins; Glucose; Guanine; Isotope Labeling; Metalloproteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; Mutation; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Pteridines; Ribulosephosphates; Sulfurtransferases

1998
The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopterin cofactor in a molybdate charged form.
    FEBS letters, 1998, Jul-17, Volume: 431, Issue:2

    Topics: Animals; Carrier Proteins; Chlamydomonas reinhardtii; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Tungsten Compounds

1998
Effect of molybdate and tungstate on the biosynthesis of CO dehydrogenase and the molybdopterin cytosine-dinucleotide-type of molybdenum cofactor in Hydrogenophaga pseudoflava.
    European journal of biochemistry, 1998, Aug-01, Volume: 255, Issue:3

    Topics: Aldehyde Oxidoreductases; Circular Dichroism; Coenzymes; Cytosine Nucleotides; Metalloproteins; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Oxidation-Reduction; Pseudomonas; Pteridines; Pterins; Tungsten Compounds

1998
Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity.
    Science (New York, N.Y.), 1998, Nov-13, Volume: 282, Issue:5392

    Topics: Animals; Animals, Newborn; Brain; Carrier Proteins; Chimera; Coenzymes; Gene Targeting; Glycine; Humans; Membrane Proteins; Metalloproteins; Mice; Molybdenum; Molybdenum Cofactors; Motor Neurons; Oxidoreductases Acting on Sulfur Group Donors; Phenotype; Pteridines; Receptor Aggregation; Receptors, Glycine; Spinal Cord; Stem Cells; Synapses; Synaptic Transmission; Xanthine Dehydrogenase

1998
Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species.
    Journal of molecular biology, 1998, Nov-27, Volume: 284, Issue:2

    Topics: Amino Acid Sequence; Anaerobiosis; Bacterial Proteins; Base Sequence; Coenzymes; Cytochrome c Group; Electron Transport; Enzyme Induction; Escherichia coli Proteins; Genes, Bacterial; Gram-Negative Facultatively Anaerobic Rods; Marine Biology; Metalloproteins; Methylamines; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Operon; Oxidoreductases, N-Demethylating; Polymerase Chain Reaction; Pteridines; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Substrate Specificity

1998
Gathering glycine receptors at synapses.
    Science (New York, N.Y.), 1998, Nov-13, Volume: 282, Issue:5392

    Topics: Adaptor Proteins, Signal Transducing; Animals; Brain; Carrier Proteins; Coenzymes; Gene Targeting; Glycine; Membrane Proteins; Metalloproteins; Mice; Molybdenum; Molybdenum Cofactors; Muscle Proteins; Nerve Tissue Proteins; Neurons; Presynaptic Terminals; Pteridines; Receptor Aggregation; Receptors, Glycine; Receptors, Nicotinic; Signal Transduction; Spinal Cord; Strychnine; Synapses; Synaptic Transmission

1998
Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A.
    Human genetics, 1998, Volume: 103, Issue:6

    Topics: Amino Acid Sequence; Carbon-Carbon Lyases; Coenzymes; Europe; Exons; Genes, Recessive; Genetic Complementation Test; Genetic Testing; Heterozygote; Homozygote; Humans; Israel; Metabolism, Inborn Errors; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; Nuclear Proteins; Pteridines; RNA Splicing

1998
Diagnosis of molybdenum cofactor deficiency.
    Lancet (London, England), 1999, Feb-20, Volume: 353, Issue:9153

    Topics: Child, Preschool; Coenzymes; Diagnosis, Differential; Humans; Infant; Infant, Newborn; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Purines; Reagent Strips; Reproducibility of Results; Seizures; Uric Acid; Xanthine Dehydrogenase

1999
Diagnosis of molybdenum cofactor deficiency.
    Lancet (London, England), 1999, Feb-20, Volume: 353, Issue:9153

    Topics: Antioxidants; Coenzymes; Diagnosis, Differential; Free Radical Scavengers; Free Radicals; Humans; Hypoxia, Brain; Infant, Newborn; Magnetic Resonance Imaging; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Reactive Oxygen Species; Seizures; Sulfites; Tomography, X-Ray Computed; Uric Acid

1999
Atlas of brain proton magnetic resonance spectra. Part II: Inherited metabolic encephalopathies.
    Journal of neuroradiology = Journal de neuroradiologie, 1998, Volume: 25, Issue:4

    Topics: Adipates; Adult; Anatomy, Artistic; Argininosuccinic Acid; Argininosuccinic Aciduria; Brain; Brain Diseases; Child; Coenzymes; Glutarates; Glycine; Homocystinuria; Humans; Magnetic Resonance Spectroscopy; Medical Illustration; Metalloproteins; Mevalonic Acid; Molybdenum; Molybdenum Cofactors; Ornithine Carbamoyltransferase Deficiency Disease; Pteridines

1998
Re-design of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Enhancement of adenosine N1-oxide reductase activity.
    The Journal of biological chemistry, 1999, Mar-26, Volume: 274, Issue:13

    Topics: Adenosine; Bacterial Proteins; Cloning, Molecular; Coenzymes; Cyclic N-Oxides; Escherichia coli; Guanine; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Oxidoreductases; Protein Engineering; Pteridines; Recombinant Proteins; Rhodobacter sphaeroides; Substrate Specificity

1999
The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase.
    European journal of biochemistry, 1999, Volume: 260, Issue:2

    Topics: Aldehyde Oxidoreductases; Anaerobiosis; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Glucose; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Pteridines; Spectrometry, Fluorescence; Sulfolobus acidocaldarius

1999
Role of XDHC in Molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus.
    Journal of bacteriology, 1999, Volume: 181, Issue:9

    Topics: Coenzymes; Enzyme Stability; Flavin-Adenine Dinucleotide; Genes, Bacterial; Iron; Metalloproteins; Models, Biological; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Insertional; Open Reading Frames; Pteridines; Rhodobacter capsulatus; Spectrometry, Fluorescence; Spectrophotometry; Sulfur; Transcription, Genetic; Xanthine Dehydrogenase

1999
The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site.
    FEMS microbiology letters, 1999, May-01, Volume: 174, Issue:1

    Topics: Amino Acid Sequence; Arginine; Base Sequence; Coenzymes; Cytochrome c Group; Dimerization; Escherichia coli; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Periplasm; Protein Precursors; Protein Sorting Signals; Pteridines; Tungsten Compounds

1999
The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor.
    FEMS microbiology letters, 1999, May-15, Volume: 174, Issue:2

    Topics: Bacterial Proteins; Blotting, Southern; Chromosome Mapping; Coenzymes; DNA, Bacterial; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Guanine Nucleotides; Iron-Sulfur Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Insertional; Nitrate Reductase; Nitrate Reductases; Oxidoreductases; Pteridines; Pterins; Rhodobacter capsulatus; Sulfurtransferases; Xanthine Dehydrogenase

1999
Characterization of a molybdenum cofactor biosynthetic gene cluster in Rhodobacter capsulatus which is specific for the biogenesis of dimethylsulfoxide reductase.
    Microbiology (Reading, England), 1999, Volume: 145 ( Pt 6)

    Topics: Amino Acid Sequence; Chromosome Mapping; Coenzymes; Escherichia coli; Genes, Bacterial; Iron-Sulfur Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multigene Family; Mutation; Oxidoreductases; Pteridines; Rhodobacter capsulatus; Sequence Homology, Amino Acid

1999
Characterization of the molybdate transport system ModABC of Staphylococcus carnosus.
    Archives of microbiology, 1999, Volume: 172, Issue:2

    Topics: ATP-Binding Cassette Transporters; Bacterial Proteins; Biological Transport; Carrier Proteins; Coenzymes; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Lipoproteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multigene Family; Mutagenesis, Insertional; Nitrate Reductase; Nitrate Reductases; Nitrates; Oxidation-Reduction; Periplasmic Binding Proteins; Pteridines; Staphylococcus

1999
Activity of the molybdopterin-containing xanthine dehydrogenase of Rhodobacter capsulatus can be restored by high molybdenum concentrations in a moeA mutant defective in molybdenum cofactor biosynthesis.
    Journal of bacteriology, 1999, Volume: 181, Issue:19

    Topics: Amino Acid Sequence; Coenzymes; DNA Mutational Analysis; Escherichia coli; Escherichia coli Proteins; Eukaryotic Cells; Guanine Nucleotides; Iron-Sulfur Proteins; Metalloproteins; Models, Biological; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Insertional; Mutation; Nitrate Reductases; Organometallic Compounds; Oxidoreductases; Pteridines; Rhodobacter capsulatus; Sequence Homology, Amino Acid; Sulfurtransferases; Xanthine; Xanthine Oxidase

1999
Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui.
    FEBS letters, 2000, Mar-24, Volume: 470, Issue:2

    Topics: Bacteria; Catalysis; Chlorates; Coenzymes; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Stability; Haloarcula marismortui; Iron; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Nitrates; Nitrites; Oxidation-Reduction; Protein Structure, Quaternary; Pteridines; Sodium Chloride; Sulfur; Thermodynamics

2000
Detection by mass spectrometry of highly increased amount of S-sulfonated transthyretin in serum from a patient with molybdenum cofactor deficiency.
    Pediatric research, 2000, Volume: 47, Issue:4 Pt 1

    Topics: Child, Preschool; Coenzymes; Humans; Infant; Male; Metabolism, Inborn Errors; Metalloproteins; Molybdenum; Molybdenum Cofactors; Prealbumin; Pteridines; Spectrometry, Mass, Secondary Ion; Sulfonic Acids

2000
Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilization.
    Proceedings of the National Academy of Sciences of the United States of America, 2000, Jun-06, Volume: 97, Issue:12

    Topics: Amino Acid Sequence; Arabidopsis Proteins; Calnexin; Coenzymes; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; Plant Proteins; Pteridines

2000
Synthesis and reactivity studies of model complexes for molybdopterin-dependent enzymes.
    Journal of inorganic biochemistry, 2000, Volume: 79, Issue:1-4

    Topics: Animals; Chickens; Coenzymes; Crystallography, X-Ray; Dithionite; Iron-Sulfur Proteins; Kinetics; Liver; Metalloproteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Xanthine Oxidase

2000
Hypersensitivity of Escherichia coli Delta(uvrB-bio) mutants to 6-hydroxylaminopurine and other base analogs is due to a defect in molybdenum cofactor biosynthesis.
    Journal of bacteriology, 2000, Volume: 182, Issue:12

    Topics: Adenine; Bacterial Proteins; Coenzymes; DNA Helicases; DNA Transposable Elements; Drug Resistance, Microbial; Escherichia coli; Escherichia coli Proteins; Gene Deletion; Metalloproteins; Molybdenum; Molybdenum Cofactors; Operon; Point Mutation; Pteridines; Sulfurtransferases

2000
Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase.
    The Journal of biological chemistry, 2000, Sep-29, Volume: 275, Issue:39

    Topics: Aldehyde Oxidase; Aldehyde Oxidoreductases; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Coenzymes; Consensus Sequence; Desulfovibrio; DNA, Complementary; Evolution, Molecular; Female; Humans; Male; Metalloproteins; Mice; Mitochondrial Proteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Phylogeny; Plant Proteins; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Sex Characteristics; Tissue Distribution; Xanthine Oxidase

2000
Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family.
    Biochemistry, 2000, Sep-19, Volume: 39, Issue:37

    Topics: Buffers; Coenzymes; Crystallography, X-Ray; Enzyme Stability; HEPES; Iron-Sulfur Proteins; Ligands; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Oxygen; Pteridines; Rhodobacter capsulatus; Sodium Chloride; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Taurine; Tromethamine

2000
ModE-dependent molybdate regulation of the molybdenum cofactor operon moa in Escherichia coli.
    Journal of bacteriology, 2000, Volume: 182, Issue:24

    Topics: Aerobiosis; Anaerobiosis; Bacterial Proteins; Base Sequence; Coenzymes; Escherichia coli; Escherichia coli Proteins; Gene Deletion; Gene Expression Regulation, Bacterial; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Operon; Promoter Regions, Genetic; Pteridines; Transcription Factors; Transcription, Genetic; Tungsten

2000
A mutation in the gene for the neurotransmitter receptor-clustering protein gephyrin causes a novel form of molybdenum cofactor deficiency.
    American journal of human genetics, 2001, Volume: 68, Issue:1

    Topics: Base Sequence; Carbon-Carbon Lyases; Carrier Proteins; Coenzymes; DNA Mutational Analysis; Exons; Fibroblasts; Gene Deletion; Humans; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; Nuclear Proteins; Pteridines; Receptor Aggregation; Receptors, Neurotransmitter; Reverse Transcriptase Polymerase Chain Reaction; Sulfurtransferases

2001
Synthesis and structures of bis(dithiolene)molybdenum complexes related to the active sites of the DMSO reductase enzyme family.
    Inorganic chemistry, 2000, Jan-24, Volume: 39, Issue:2

    Topics: Binding Sites; Chemical Phenomena; Chemistry, Physical; Coenzymes; Crystallography, X-Ray; Iron-Sulfur Proteins; Ligands; Magnetic Resonance Spectroscopy; Metalloproteins; Molecular Conformation; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Oxidoreductases; Pteridines

2000
Deletion of the cnxE gene encoding the gephyrin-like protein involved in the final stages of molybdenum cofactor biosynthesis in Aspergillus nidulans.
    Molecular genetics and genomics : MGG, 2001, Volume: 266, Issue:3

    Topics: Amino Acid Sequence; Aspergillus nidulans; Base Sequence; Binding Sites; Blotting, Southern; Carrier Proteins; Catalysis; Chromatography, High Pressure Liquid; Cloning, Molecular; Coenzymes; DNA, Complementary; DNA, Fungal; Enzyme Precursors; Gene Deletion; Gene Expression Regulation; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Mutation; Nitrate Reductase; Nitrate Reductases; Plasmids; Pteridines

2001
Mutational analysis of the gephyrin-related molybdenum cofactor biosynthetic gene cnxE from the lower eukaryote Aspergillus nidulans.
    Genetics, 2002, Volume: 161, Issue:2

    Topics: Amino Acid Sequence; Amino Acid Substitution; Aspergillus nidulans; Carrier Proteins; Chromatography, High Pressure Liquid; Coenzymes; Fungal Proteins; Genetic Complementation Test; Membrane Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on CH-NH Group Donors; Pteridines; Sequence Alignment; Xanthine Dehydrogenase

2002
Evidence for MoeA-dependent formation of the molybdenum cofactor from molybdate and molybdopterin in Escherichia coli.
    Archives of microbiology, 2002, Volume: 178, Issue:6

    Topics: Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; Escherichia coli Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora crassa; Nitrate Reductases; Pteridines; Sulfurtransferases; Xanthine Oxidase

2002
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
    Proceedings of the National Academy of Sciences of the United States of America, 2002, Dec-10, Volume: 99, Issue:25

    Topics: Aldehyde Oxidoreductases; Alphaproteobacteria; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Copper; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitriles; Oxidation-Reduction; Potassium Cyanide; Pteridines; Selenium; Structure-Activity Relationship; Sulfur

2002
Synthesis of a molecular Mo2Fe6S9 cluster with the topology of the PN cluster of nitrogenase by rearrangement of an edge-bridged Mo2Fe6S8 double cubane.
    Journal of the American Chemical Society, 2003, Apr-02, Volume: 125, Issue:13

    Topics: Biomimetic Materials; Coenzymes; Crystallography, X-Ray; Iron; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum; Molybdenum Cofactors; Nitrogenase; Organometallic Compounds; Pteridines; Selenium Compounds; Sulfur

2003
Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency.
    The Journal of biological chemistry, 2003, Jul-11, Volume: 278, Issue:28

    Topics: Amino Acid Sequence; Chromatography; Chromatography, High Pressure Liquid; Circular Dichroism; Cloning, Molecular; Coenzymes; DNA, Complementary; Escherichia coli; Gene Library; Genetic Complementation Test; Humans; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Mutation; Nitrate Reductase; Nitrate Reductases; Protein Binding; Protein Structure, Tertiary; Pteridines; Sequence Homology, Amino Acid; Sulfurtransferases; Time Factors

2003
Multifrequency cw-EPR investigation of the catalytic molybdenum cofactor of polysulfide reductase from Wolinella succinogenes.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2003, Volume: 8, Issue:4

    Topics: Bacterial Proteins; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines; Wolinella

2003
Factors involved in the assembly of a functional molybdopyranopterin center in recombinant Comamonas acidovorans xanthine dehydrogenase.
    European journal of biochemistry, 2003, Volume: 270, Issue:23

    Topics: Amino Acid Sequence; Animals; Binding Sites; Circular Dichroism; Comamonas; Electron Spin Resonance Spectroscopy; Escherichia coli; Genes, Bacterial; Molecular Sequence Data; Molecular Structure; Molybdenum; Protein Subunits; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Xanthine Dehydrogenase

2003
The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor.
    The Journal of biological chemistry, 2004, Apr-16, Volume: 279, Issue:16

    Topics: Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Pteridines; Sulfur

2004
An evaluation by density functional theory of M-M interactions in organometallic clusters with the [Fe(3)MoS(3)](2+) cores.
    Inorganic chemistry, 2004, May-17, Volume: 43, Issue:10

    Topics: Catechols; Chlorides; Cluster Analysis; Cobalt; Crystallography, X-Ray; Electrons; Iron; Ligands; Models, Molecular; Molybdenum; Nitrogenase; Organometallic Compounds; Oxidation-Reduction; Pteridines; Pyridines; Sulfur

2004
Biological chemistry: the making of Moco.
    Nature, 2004, Aug-12, Volume: 430, Issue:7001

    Topics: Adenosine Monophosphate; Animals; Binding Sites; Carrier Proteins; Coenzymes; Copper; Crystallography, X-Ray; Membrane Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Plant Proteins; Plants; Protein Binding; Protein Structure, Tertiary; Pteridines

2004
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism.
    Nature, 2004, Aug-12, Volume: 430, Issue:7001

    Topics: Adenosine Monophosphate; Arabidopsis Proteins; Binding Sites; Calnexin; Coenzymes; Copper; Crystallization; Crystallography, X-Ray; Magnesium; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Plant Proteins; Plants; Protein Binding; Protein Structure, Tertiary; Pteridines; Sulfur

2004
Geometrical control of the active site electronic structure of pyranopterin enzymes by metal-dithiolate folding: aldehyde oxidase.
    Journal of the American Chemical Society, 2004, Sep-29, Volume: 126, Issue:38

    Topics: Aldehyde Oxidase; Binding Sites; Coenzymes; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Protein Folding; Pteridines; Structure-Activity Relationship; Sulfur Compounds

2004
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
    The Journal of biological chemistry, 2005, Feb-11, Volume: 280, Issue:6

    Topics: Aldehyde Oxidase; Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Cysteine; Cytosol; Fluorescent Dyes; Genetic Vectors; Iron-Sulfur Proteins; Kinetics; Lyases; Lysine; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Naphthalenesulfonates; Pichia; Plant Proteins; Protein Binding; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Selenocysteine; Spectrophotometry; Substrate Specificity; Sulfides; Sulfurtransferases; Xanthine Dehydrogenase

2005
In vitro molybdenum ligation to molybdopterin using purified components.
    The Journal of biological chemistry, 2005, Mar-04, Volume: 280, Issue:9

    Topics: Adenosine Triphosphate; Biochemistry; Coenzymes; Dose-Response Relationship, Drug; Escherichia coli; Escherichia coli Proteins; Humans; Magnesium; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Pteridines; Pterins; Sulfates; Sulfur; Sulfurtransferases; Time Factors; Tungsten

2005
Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres.
    The Biochemical journal, 2005, Jun-01, Volume: 388, Issue:Pt 2

    Topics: Animals; Cattle; Coenzymes; Female; Humans; Iron; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Pteridines; Spectrum Analysis; Sulfur; Xanthine Dehydrogenase

2005
Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity.
    Biochemistry, 2005, May-10, Volume: 44, Issue:18

    Topics: Amino Acid Sequence; Bacterial Proteins; Catalysis; Cloning, Molecular; Coenzymes; Cytochrome c Group; Electrochemistry; Flavoproteins; Heme; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Oxidoreductases; Paracoccus pantotrophus; Protein Structure, Tertiary; Pteridines; Spectrophotometry, Ultraviolet

2005
Molybdenum. Monograph.
    Alternative medicine review : a journal of clinical therapeutic, 2006, Volume: 11, Issue:2

    Topics: Animals; Coenzymes; Drug Hypersensitivity; Hepatolenticular Degeneration; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neoplasms; Pteridines; Sulfites

2006
A novel thermostable sulfite oxidase from Thermus thermophilus: characterization of the enzyme, gene cloning and expression in Escherichia coli.
    Extremophiles : life under extreme conditions, 2006, Volume: 10, Issue:6

    Topics: Amino Acid Sequence; Bacterial Proteins; Cloning, Molecular; Coenzymes; Electrophoresis, Polyacrylamide Gel; Enzyme Stability; Escherichia coli; Ferricyanides; Hydrogen-Ion Concentration; Kinetics; Metalloproteins; Molecular Sequence Data; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Periplasm; Protein Conformation; Pteridines; Recombinant Proteins; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Sulfite Oxidase; Sulfites; Temperature; Thermus thermophilus

2006
Resonance Raman studies of xanthine oxidase: The reduced enzyme-product complex with violapterin.
    The journal of physical chemistry. B, 2005, Feb-24, Volume: 109, Issue:7

    Topics: Binding Sites; Coenzymes; Deuterium Oxide; Metalloproteins; Models, Chemical; Models, Molecular; Molecular Conformation; Molybdenum; Molybdenum Cofactors; Oxygen; Pteridines; Solvents; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Substrate Specificity; Water; Xanthine Oxidase

2005
Function and structure of the molybdenum cofactor carrier protein from Chlamydomonas reinhardtii.
    The Journal of biological chemistry, 2006, Oct-06, Volume: 281, Issue:40

    Topics: Amino Acid Sequence; Animals; Carrier Proteins; Chlamydomonas reinhardtii; Coenzymes; Computer Simulation; Crystallography, X-Ray; Metalloproteins; Models, Molecular; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Protein Binding; Pteridines; Structure-Activity Relationship; Tungsten

2006
Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft.
    Biochemistry, 2007, Jan-09, Volume: 46, Issue:1

    Topics: Binding Sites; Coenzymes; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Mutation; Protein Structure, Tertiary; Pteridines; Sulfurtransferases

2007
A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism.
    Molecular microbiology, 2008, Volume: 68, Issue:4

    Topics: 5' Untranslated Regions; Base Sequence; Coenzymes; Computational Biology; Conserved Sequence; Escherichia coli; Gene Expression Regulation, Bacterial; Ligands; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; Operon; Organometallic Compounds; Phylogeny; Pteridines; Pterins; RNA, Bacterial

2008
Molybdoproteomes and evolution of molybdenum utilization.
    Journal of molecular biology, 2008, Jun-13, Volume: 379, Issue:4

    Topics: Archaea; Bacteria; Coenzymes; Eukaryotic Cells; Evolution, Molecular; Ion Transport; Metalloproteins; Models, Biological; Molybdenum; Molybdenum Cofactors; Phylogeny; Proteome; Pteridines

2008
[Structure and mechanism of molybdenum hydroxylase].
    Seikagaku. The Journal of Japanese Biochemical Society, 2008, Volume: 80, Issue:6

    Topics: Animals; Catalysis; Coenzymes; Crystallization; Humans; Hydroxylation; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Xanthine Dehydrogenase

2008
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor.
    Proceedings of the National Academy of Sciences of the United States of America, 2008, Aug-19, Volume: 105, Issue:33

    Topics: Azotobacter vinelandii; Bacterial Proteins; Biological Transport; Coenzymes; Iron; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogen Fixation; Nitrogenase; Protein Binding; Pteridines; Transcription Factors

2008
Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli.
    The FEBS journal, 2008, Volume: 275, Issue:22

    Topics: Binding Sites; Coenzymes; Escherichia coli; Humans; Iron-Sulfur Proteins; Metalloproteins; Metals, Heavy; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines; Rhodobacter sphaeroides; Sulfite Oxidase; Sulfurtransferases; Tungsten Compounds

2008
Substrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase: CRYSTAL STRUCTURES IN COMPLEX WITH XANTHINE AND LUMAZINE.
    The Journal of biological chemistry, 2009, Mar-27, Volume: 284, Issue:13

    Topics: Animals; Bacterial Proteins; Catalysis; Catalytic Domain; Cattle; Crystallography, X-Ray; Female; Milk; Molybdenum; Protein Structure, Tertiary; Pteridines; Rhodobacter capsulatus; Xanthine; Xanthine Oxidase

2009
Characterization of a mutant of Chlamydomonas reinhardtii deficient in the molybdenum cofactor.
    Physiologia plantarum, 2009, Volume: 136, Issue:3

    Topics: Algal Proteins; Animals; Chlamydomonas reinhardtii; Coenzymes; Genetic Complementation Test; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Insertional; Mutation; Nitrate Reductase; Nitrogen; Phenotype; Pteridines; RNA, Algal

2009
Which functional groups of the molybdopterin ligand should be considered when modeling the active sites of the molybdenum and tungsten cofactors? A density functional theory study.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009, Volume: 14, Issue:7

    Topics: Catalysis; Catalytic Domain; Coenzymes; Computational Biology; Ligands; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Pteridines; Pterins; Tungsten

2009
Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase.
    Biochemistry, 2010, Sep-21, Volume: 49, Issue:37

    Topics: 14-3-3 Proteins; Arabidopsis; Catalysis; Coenzymes; Eukaryota; Heme; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; NAD; Nitrate Reductase; Nitrate Reductase (NADH); Nitrate Reductases; Oxidation-Reduction; Phosphorylation; Protein Kinases; Pteridines

2010
Effects of large-scale amino acid substitution in the polypeptide tether connecting the heme and molybdenum domains on catalysis in human sulfite oxidase.
    Metallomics : integrated biometal science, 2010, Volume: 2, Issue:11

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Biocatalysis; Chickens; Coenzymes; Heme; Humans; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Peptides; Pteridines; Sulfite Oxidase

2010
Structural studies of the molybdenum center of mitochondrial amidoxime reducing component (mARC) by pulsed EPR spectroscopy and 17O-labeling.
    Biochemistry, 2011, Oct-18, Volume: 50, Issue:41

    Topics: Biochemistry; Buffers; Catalytic Domain; Coenzymes; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Humans; Ligands; Metalloproteins; Mitochondria; Mitochondrial Proteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxygen Isotopes; Protein Binding; Pteridines

2011
Structure and reversible pyran formation in molybdenum pyranopterin dithiolene models of the molybdenum cofactor.
    Journal of the American Chemical Society, 2012, Dec-05, Volume: 134, Issue:48

    Topics: Coenzymes; Crystallography, X-Ray; Cyclization; Ligands; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Pteridines; Pterins

2012
Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin.
    The Biochemical journal, 2013, Feb-15, Volume: 450, Issue:1

    Topics: Alternative Splicing; Apoproteins; Carrier Proteins; Coenzymes; Membrane Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Protein Processing, Post-Translational; Protein Structure, Tertiary; Pteridines; Recombinant Proteins

2013
Biochemical characterization of molybdenum cofactor-free nitrate reductase from Neurospora crassa.
    The Journal of biological chemistry, 2013, May-17, Volume: 288, Issue:20

    Topics: Amino Acid Sequence; Cloning, Molecular; Coenzymes; Dimerization; Electron Spin Resonance Spectroscopy; Heme; Metalloproteins; Models, Molecular; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; NADP; Neurospora crassa; Nitrate Reductase; Nitrite Reductases; Oxidation-Reduction; Protein Binding; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Ultracentrifugation

2013
Identification of a bis-molybdopterin intermediate in molybdenum cofactor biosynthesis in Escherichia coli.
    The Journal of biological chemistry, 2013, Oct-11, Volume: 288, Issue:41

    Topics: Coenzymes; Escherichia coli; Escherichia coli Proteins; Guanosine Monophosphate; Humans; Metalloproteins; Molecular Chaperones; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Phosphates; Protein Binding; Pteridines; Sulfurtransferases; X-Ray Absorption Spectroscopy

2013
Effect of exchange of the cysteine molybdenum ligand with selenocysteine on the structure and function of the active site in human sulfite oxidase.
    Biochemistry, 2013, Nov-19, Volume: 52, Issue:46

    Topics: Catalytic Domain; Coenzymes; Cysteine; Electron Spin Resonance Spectroscopy; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Metalloproteins; Molybdenum; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Selenocysteine; X-Ray Absorption Spectroscopy

2013
Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion.
    Biochimica et biophysica acta, 2014, Volume: 1837, Issue:2

    Topics: Coenzymes; Electrochemical Techniques; Electron Spin Resonance Spectroscopy; Enzyme Activation; Ions; Iron-Sulfur Proteins; Kinetics; Ligands; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Oxidation-Reduction; Periplasm; Pteridines; Pterins; Rhodobacter sphaeroides; Spin Labels; Temperature

2014
Biochemical, stabilization and crystallization studies on a molecular chaperone (PaoD) involved in the maturation of molybdoenzymes.
    PloS one, 2014, Volume: 9, Issue:1

    Topics: Chromatography, Gel; Coenzymes; Crystallization; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Ionic Liquids; Magnetic Resonance Spectroscopy; Metalloproteins; Molecular Chaperones; Molecular Structure; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Protein Binding; Protein Multimerization; Protein Stability; Pteridines; Tungsten

2014
Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2.
    The Journal of biological chemistry, 2014, Apr-11, Volume: 289, Issue:15

    Topics: Amino Acid Sequence; Coenzymes; Cytochrome Reductases; Cytochromes b5; Electron Transport; HEK293 Cells; Humans; Hydrogen-Ion Concentration; Kinetics; Metalloproteins; Mitochondria; Mitochondrial Proteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Nitric Oxide; Nitric Oxide Synthase; Nitrite Reductases; Nitrites; Oxidoreductases; Oxygen; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Xanthine Oxidase

2014
Genetic characterization of the Neurospora crassa molybdenum cofactor biosynthesis.
    Fungal genetics and biology : FG & B, 2014, Volume: 66

    Topics: Aspergillus nidulans; Coenzymes; Fungal Proteins; Gene Knockout Techniques; Genes, Fungal; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Neurospora crassa; Pteridines

2014
The biosynthesis of the molybdenum cofactors.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015, Volume: 20, Issue:2

    Topics: Archaea; Bacteria; Catalysis; Coenzymes; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nucleotides; Organophosphorus Compounds; Oxidation-Reduction; Oxidoreductases; Pteridines; Pterins

2015
Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide.
    Antioxidants & redox signaling, 2015, Aug-01, Volume: 23, Issue:4

    Topics: Coenzymes; Electron Transport; Fibroblasts; Heme; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitric Oxide; Nitrites; Oxidation-Reduction; Protein Structure, Tertiary; Pteridines; Signal Transduction; Sulfite Oxidase

2015
Comparison of the active-site design of molybdenum oxo-transfer enzymes by quantum mechanical calculations.
    Inorganic chemistry, 2014, Nov-17, Volume: 53, Issue:22

    Topics: Binding Sites; Catalysis; Coenzymes; Computational Biology; Coordination Complexes; Kinetics; Ligands; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Oxygen; Pteridines; Quantum Theory; Sulfite Oxidase; Thermodynamics; Xanthine Oxidase

2014
Recent developments in the study of molybdoenzyme models.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015, Volume: 20, Issue:2

    Topics: Binding Sites; Catalytic Domain; Coenzymes; Iron-Sulfur Proteins; Ligands; Molecular Structure; Molybdenum; Pteridines; Pterins

2015
Structural Framework for Metal Incorporation during Molybdenum Cofactor Biosynthesis.
    Structure (London, England : 1993), 2016, 05-03, Volume: 24, Issue:5

    Topics: Adenosine Diphosphate; Adenosine Monophosphate; Binding Sites; Carrier Proteins; Coenzymes; Humans; Membrane Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Protein Binding; Pteridines

2016
Molybdate uptake by Agrobacterium tumefaciens correlates with the cellular molybdenum cofactor status.
    Molecular microbiology, 2016, Volume: 101, Issue:5

    Topics: Agrobacterium tumefaciens; Amino Acid Sequence; Base Sequence; Coenzymes; Escherichia coli; Escherichia coli Proteins; Inverted Repeat Sequences; Metalloproteins; Molybdenum; Molybdenum Cofactors; Operon; Promoter Regions, Genetic; Pteridines; Transcription Factors

2016
Molybdenum and iron mutually impact their homeostasis in cucumber (Cucumis sativus) plants.
    The New phytologist, 2017, Volume: 213, Issue:3

    Topics: Cluster Analysis; Coenzymes; Cucumis sativus; Formate Dehydrogenases; Homeostasis; Iron; Metabolome; Metalloproteins; Mitochondria; Mitochondrial Proteins; Models, Biological; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Plant Leaves; Plant Roots; Proteome; Pteridines

2017
Modulating the Molybdenum Coordination Sphere of Escherichia coli Trimethylamine N-Oxide Reductase.
    Biochemistry, 2018, 02-20, Volume: 57, Issue:7

    Topics: Coenzymes; Cytochrome P-450 Enzyme System; Escherichia coli; Escherichia coli Proteins; Guanine Nucleotides; Humans; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Oxidoreductases, N-Demethylating; Pteridines; Pterins; Sulfides

2018
QM/MM study of the reaction mechanism of sulfite oxidase.
    Scientific reports, 2018, 03-16, Volume: 8, Issue:1

    Topics: Animals; Chickens; Coenzymes; Hydrogen Bonding; Mechanical Phenomena; Metalloproteins; Models, Molecular; Molecular Dynamics Simulation; Molybdenum; Molybdenum Cofactors; Pteridines; Quantum Theory; Sulfite Oxidase; Sulfites

2018
The functional principle of eukaryotic molybdenum insertases.
    The Biochemical journal, 2018, 05-24, Volume: 475, Issue:10

    Topics: Amino Acid Sequence; Binding Sites; Catalysis; Catalytic Domain; Coenzymes; Eukaryota; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Protein Conformation; Pteridines; Sequence Homology

2018
Molybdenum.
    Advances in nutrition (Bethesda, Md.), 2018, 05-01, Volume: 9, Issue:3

    Topics: Animals; Coenzymes; Cytochromes b5; Diet; Humans; Liver; Metalloproteins; Mitochondria; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines; Trace Elements

2018
Crystal structure of human mARC1 reveals its exceptional position among eukaryotic molybdenum enzymes.
    Proceedings of the National Academy of Sciences of the United States of America, 2018, 11-20, Volume: 115, Issue:47

    Topics: Catalysis; Coenzymes; Crystallography, X-Ray; Eukaryotic Cells; Humans; Metalloproteins; Mitochondria; Mitochondrial Proteins; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Protein Structure, Tertiary; Pteridines

2018
Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in Escherichia coli.
    Biochemistry, 2019, 04-30, Volume: 58, Issue:17

    Topics: Coenzymes; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Ferredoxins; Guanine Nucleotides; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Oxidation-Reduction; Oxidoreductases; Pteridines; Pterins

2019
Insights into the Cnx1E catalyzed MPT-AMP hydrolysis.
    Bioscience reports, 2020, 01-31, Volume: 40, Issue:1

    Topics: Adenosine Monophosphate; Amino Acid Sequence; Amino Acids; Arabidopsis; Arabidopsis Proteins; Catalysis; Catalytic Domain; Coenzymes; Hydrolysis; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organophosphorus Compounds; Pteridines; Pterins

2020
Preparation and spectroscopic characterization of lyophilized Mo nitrogenase.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2021, Volume: 26, Issue:1

    Topics: Acetylene; Biocatalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Enzyme Assays; Freeze Drying; Iron; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Pteridines; X-Ray Absorption Spectroscopy

2021
Mechanism of molybdate insertion into pterin-based molybdenum cofactors.
    Nature chemistry, 2021, Volume: 13, Issue:8

    Topics: Adenosine Monophosphate; Arabidopsis; Arabidopsis Proteins; Coenzymes; Crystallography, X-Ray; Models, Chemical; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines

2021
{Moco}
    Journal of inorganic biochemistry, 2022, Volume: 231

    Topics: Coenzymes; Electron Spin Resonance Spectroscopy; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Sulfite Oxidase

2022
Obtaining the necessary molybdenum cofactor for sulfite oxidase activity in the nematode Caenorhabditis elegans surprisingly involves a dietary source.
    The Journal of biological chemistry, 2023, Volume: 299, Issue:1

    Topics: Animals; Caenorhabditis elegans; Diet; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Sulfite Oxidase

2023
Moonlighting Arabidopsis molybdate transporter 2 family and GSH-complex formation facilitate molybdenum homeostasis.
    Communications biology, 2023, 08-02, Volume: 6, Issue:1

    Topics: Arabidopsis; Homeostasis; Membrane Transport Proteins; Molybdenum; Pteridines

2023
The structural principles underlying molybdenum insertase complex assembly.
    Protein science : a publication of the Protein Society, 2023, Volume: 32, Issue:9

    Topics: Arabidopsis; Arabidopsis Proteins; Calnexin; Coenzymes; Metalloproteins; Molybdenum; Pteridines

2023