pteridines has been researched along with molybdenum in 250 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 64 (25.60) | 18.7374 |
1990's | 88 (35.20) | 18.2507 |
2000's | 50 (20.00) | 29.6817 |
2010's | 38 (15.20) | 24.3611 |
2020's | 10 (4.00) | 2.80 |
Authors | Studies |
---|---|
Amy, NK; Rajagopalan, KV | 1 |
Rothery, RA; Sambasivarao, D; Trieber, CA; Weiner, JH | 1 |
Casadesus, J; Flores, A; Garzón, A; Li, J; Stewart, V | 1 |
Boxer, DH; Chippaux, M; Cole, JA; DeMoss, JA; Giordano, G; Gunsalus, RP; Lin, EC; Rajagopalan, KV; Shanmugam, KT; Stewart, V | 1 |
Crawford, NM; Feldmann, KA; LaBrie, ST; Tsay, YF; Wilkinson, JQ | 1 |
Augier, V; Blasco, F; Chippaux, M; Giordano, G; Pommier, J | 1 |
Johnson, JL; Rajagopalan, KV | 4 |
Bray, RC; Burke, JF; Chovnick, A; Doyle, WA; Hughes, RK; Whittle, JR | 1 |
Chaudhury, M; Johnson, JL; Rajagopalan, KV | 1 |
Aguilar, MR; Cárdenas, J; Fernández, E | 1 |
Bennett, B; Bray, RC; Howes, BD; Koppenhöfer, A; Lowe, DJ | 1 |
Baker, KP; Boxer, DH | 1 |
Ferguson, SJ; Jackson, JB; McEwan, AG | 1 |
Bray, RC; Burke, JF; Cock, JM; Doyle, WA; Nicolson, RE; Walters, DE; Wootton, JC | 1 |
Bauder, R; Lingens, F; Tshisuaka, B | 1 |
Barber, MJ; Kay, CJ; Solomonson, LP | 1 |
Basu, SN; Condie, RG; Constantine, G; Desjacques, P; Dorche, C; Gray, RG; Green, A; Vianey-Liaud, C | 1 |
Bastian, NR; Johnson, JL; Rajagopalan, KV | 1 |
Gardlik, S; Rajagopalan, KV | 1 |
Grieve, C; Gurr, SJ; Kinghorn, JR; Ramsden, M; Spence, D; Unkles, SE; Whitehead, MP | 1 |
Dean, D; Hinton, SM | 1 |
Johnson, JL; Mandell, R; Shih, VE; Wuebbens, MM | 2 |
Johnson, JL; Rajagopalan, KV; Wuebbens, MM | 1 |
Boxer, D; Giordano, G; Karibian, D; Santini, CL; Vasishta, A | 1 |
Bray, RC; Deistung, J; Ventom, AM | 1 |
Duch, DS; Nichol, CA; Smith, GK | 1 |
Solomonson, LP; Zeiler, KG | 1 |
Fritz, B; Ninnemann, H; Siefermann-Harms, D | 1 |
Hageman, RV; Rajagopalan, KV | 1 |
Johnson, ME; Rajagopalan, KV | 2 |
Krüger, B; Meyer, O | 1 |
Kasai, Y; Nohno, T; Saito, T | 1 |
Stewart, V | 1 |
Rajagopalan, KV | 3 |
Baldwin, MC; Finnerty, V; Schott, DR | 1 |
Amy, NK; Miller, JB; Scott, DJ | 1 |
Johnson, JL | 1 |
Gheller, SF; Hedman, B; Hodgson, KO; Lough, SM; McDonald, JW; Newton, WE | 1 |
Giordano, G; Pommier, J; Silvestro, A | 1 |
Ishimoto, M; Okubo, N; Yamamoto, I | 1 |
Freyer, G; Hinton, SM | 1 |
Johnson, JL; Kramer, SP; Millington, DS; Rajagopalan, KV; Ribeiro, AA | 1 |
Ferry, JG; May, HD; Schauer, NL | 1 |
Hille, R; Massey, V | 1 |
Bimar, J; Collet, S; Desjacques, P; Divry, P; Lagier, P; Lando, A; Tessonnier, JM; Vianet-Liaud, C | 1 |
Berger, JP; Hervé, F; Soulier, J | 1 |
Hinton, SM; Mortenson, LE | 1 |
Beemer, FA; Cats, BP; Duran, M; Wadman, SK | 1 |
Monnet, JP; Nogues, C; Ogier, H; Roth, A; Saudubray, JM | 1 |
Fukui, S; Ishizuka, M; Kogushi, M; Toraya, T; Ushio, K | 1 |
Bray, RC; Hawkes, TR | 2 |
Hageman, RV; Rajagopalan, KV; Wahl, RC | 1 |
Hageman, RV; Kramer, S; Rajagopalan, KV | 1 |
Burns, A; Tennent, DL; Watt, GD | 1 |
Bray, RC; Malthouse, JP; Williams, JW | 1 |
Amy, NK; Miller, JB | 1 |
Coughlan, MP | 1 |
Buxton, RS; Drury, LS | 1 |
Fukui, S; Ishizuka, M; Toraya, T; Ushio, K | 1 |
Brill, WJ; Imperial, J; Shah, VK; Ugalde, RA | 1 |
Goldflam, M; Rowe, JJ | 1 |
Beemer, FA; Berger, R; Cats, BP; Charpentier, C; Duran, M; Johnson, JL; Ogier, H; Rajagopalan, KV; Saudubray, JM; Wadman, SK | 1 |
Campbell, A; del Campillo-Campbell, A | 1 |
Arison, BH; Hainline, BE; Johnson, JL; Rajagopalan, KV | 1 |
Bettenhaussen, CW; Claassen, VP; Fokkens, RH; Nibbering, NM; Oltmann, LF; Pinkse, FA; Stouthamer, AH; van 't Riet, J | 1 |
Meyer, O; Rajagopalan, KV | 1 |
Claassen, VP; Oltmann, LF; Stouthamer, AH; Vader, CE; van 't Riet, J | 1 |
Hainline, BE; Johnson, JL; Rajagopalan, KV | 1 |
Davis, MD; Olson, JS; Palmer, G | 1 |
Charpentier, C; Frezal, J; Kesseler, A; Munnich, A; Ogier, H; Perignon, JL; Saudubray, JM | 1 |
Finnerty, V; Warner, CK | 1 |
Beemer, FA; Duran, M; Johnson, JL; Rajagopalan, KV; Wadman, SK; Waud, WR | 1 |
Amy, NK | 1 |
Bus, S; Claassen, VP; Oltmann, LF; Stouthamer, AH; v 't Riet, J | 1 |
Ishimoto, M; Takagi, M; Tsuchiya, T | 1 |
Brill, WJ; Shah, VK; Shen, SC; Stacey, G; Zhu, J | 1 |
MacGregor, CH; Stewart, V | 1 |
Brinkman, UA; Claassen, VP; Oltmann, LF; Stouthamer, AH; Van't Riet, J | 1 |
Arst, HN; Sealy-Lewis, HM; Tollervey, DW | 1 |
Johnson, JL; Mize, C; Rajagopalan, KV | 1 |
Archer, M; Engh, R; Hof, P; Huber, R; LeGall, J; Moura, I; Moura, JJ; Romão, MJ; Schneider, M | 1 |
Hagen, WR; Hansen, TA; Hensgens, CM | 1 |
Artigas, M; Coll, MJ; Johnson, JL; Naranjo, MA; Pintos-Morell, G; Rajagopalan, KV; Rodes, M; Roge, M | 1 |
Mandel, H; Stroomer, LE; van Cruchten, AG; van Gennip, AH | 1 |
Deppenmeier, U; Gunsalus, RP; Rech, S | 1 |
Bastian, NR; Hilton, J; Kilpatrick, L; Pilato, RS; Rajagopalan, KV; Spiro, TG; Stiefel, EI | 1 |
Heck, IS; Ninnemann, H | 1 |
Krauss, F; Lottspeich, F; Simon, H; Trautwein, T | 1 |
Finnerty, V; Kamdar, KP; Shelton, ME | 1 |
Abeling, NG; Bakker, HD; Overweg-Plandsoen, WC; ten Houten, R; van den Blij, JF; van Gennip, AH; Wanders, RJ | 1 |
Garrett, RM; Hilton, JC; Johnson, JL; Pitterle, DM; Rajagopalan, KV; Wuebbens, MM; Zurick, TR | 1 |
Darwish, IS; Taylor, EC | 1 |
Dubler, E; Fischer, B; Schmalle, H; Viscontini, M | 1 |
Johnson, JL; Rajagopalan, KV; Wadman, SK | 1 |
Finnerty, V; Kamdar, P; Shelton, ME | 1 |
Abeling, NG; Bakker, HD; Barth, PG; Overweg-Plandsoen, WC; Slot, HM; Tamminga, P; Van Gennip, AH | 1 |
Eady, RR; Gangeswaran, R; Lowe, DJ | 1 |
Arnold, GL; Goodman, SI; Greene, CL; Stout, JP | 1 |
Bakker, HD | 1 |
Brinkmann, H; Mendel, RR; Nerlich, A; Schiemann, J; Stallmeyer, B | 1 |
Blasco, F; Buc, J; Cárdenas, ML; Chippaux, M; Cornish-Bowden, A; Giordani, R; Giordano, G; Santini, CL | 1 |
Hedderich, R; Hochheimer, A; Schmitz, RA; Thauer, RK | 1 |
Edmondson, DE; Xiang, Q | 1 |
Hille, R; Kim, JH; Knaut, H; Ryan, MG | 1 |
Kroneck, PM; Reichenbecher, W; Rüdiger, A; Schink, B | 1 |
Stiefel, EI | 1 |
Bray, RC; Chovnick, A; Doyle, WA; Whittle, JR | 1 |
Hanlon, SP; Holt, RA; McEwan, AG; Solomon, PS; Toh, TH | 1 |
Brandsch, R; Menéndez, C; Siebert, D | 1 |
Johnson, JL; Joshi, MS; Rajagopalan, KV | 1 |
Bellini, C; Bertola, A; Bonioli, E; Caruso, U; DiStefano, A; Dorche, C; Fantasia, AR; Minniti, G; Palmieri, A | 1 |
Eshed, Y; Fluhr, R; Ori, N; Paran, I; Pinto, P; Zamir, D | 1 |
Amaya, Y; Hosoya, T; Ichida, K; Kamatani, N; Nishino, T; Sakai, O | 1 |
Hanson, GR; Lane, I; McEwan, AG; Solomon, PS | 1 |
Kisker, C; Rees, DC; Schindelin, H | 1 |
Boxer, DH; Heck, IS; Kanan, GJ; Kinghorn, JR; Millar, LJ; Smith, J; Unkles, SE | 1 |
Archangeli, LL; Finnerty, V; Kamdar, KP; Primus, JP; Shelton, ME; Wittle, AE | 1 |
Bray, RC; Eisenthal, R; Godber, B; Harrison, R; Sanders, S | 1 |
Böttcher, B; Brandsch, R; Igloi, G; Menéndez, C; Nick, P; Otto, A; Schubach, B | 1 |
Hasona, A; Ray, RM; Shanmugam, KT | 1 |
Asso, M; Bertrand, P; Blasco, F; Giordano, G; Guigliarelli, B; Magalon, A; Rothery, RA | 1 |
Blasco, F; Dos Santos, JP; Frixon, C; Giordano, G; Guigliarelli, B; Magalon, A; Santini, CL | 1 |
Ishibashi, S; Matsuishi, T; Nakashima, M; Satoi, M | 1 |
Huber, R; Knäblein, J; Moura, JJ; Romão, MJ | 1 |
Enemark, JH; McMaster, J | 1 |
Bacher, A; Blanchard, S; Boyle, P; Eisenreich, W; Götze, E; O'Brien, J; Richter, G; Rieder, C; Simon, H | 1 |
Fernández, E; Igeño, MI; Mendel, R; Schwarz, G; Witte, CP | 1 |
Hänzelmann, P; Meyer, O | 1 |
Betz, H; Feng, G; Kirsch, J; Kuhse, J; Nichol, MC; Sanes, JR; Tintrup, H | 1 |
Couillault, C; Dos Santos, JP; Giordano, G; Iobbi-Nivol, C; Méjean, V | 1 |
Froehner, SC | 1 |
Christensen, E; Dorche, C; Kurlemann, G; Reiss, J; Zabot, MT | 1 |
Baas, D; Kisker, C; Kroneck, PM; Meckenstock, RU; Rétey, J; Schindelin, H | 1 |
Hoffmann, GF; Micheli, V; Pérignon, JL; Simmonds, HA; van Gennip, AH | 1 |
Maxwell, S; Waring, WS | 1 |
Confort-Gouny, S; Cozzone, PJ; Salvan, AM; Vion-Dury, J | 1 |
Hilton, JC; Rajagopalan, KV; Temple, CA | 1 |
Anemüller, S; Hansen, T; Kardinahl, S; Petersen, A; Schäfer, G; Schmidt, CL | 1 |
Klipp, W; Leimkühler, S | 2 |
Cole, JA; Potter, L; Thomas, G | 1 |
Hanson, GR; Lane, I; McEwan, AG; Palmer, T; Shaw, AL; Solomon, PS | 1 |
Götz, F; Lindgren, PE; Neubauer, H; Pantel, I | 1 |
Angermüller, S; Klipp, W; Leimkühler, S; Mendel, RR; Schwarz, G | 1 |
Fujiwara, T; Sakurai, T; Yoshimatsu, K | 1 |
Reiss, J | 1 |
Kishikawa, M; Nakanishi, T; Shimizu, A; Yoshino, M | 1 |
Kuper, J; Mendel, RR; Palmer, T; Schwarz, G | 1 |
Behrens, A; Fryxelius, J; Lorber, C; Nordlander, E; Thapper, A | 1 |
Dunn, RL; Kozmin, SG; Pavlov, YI; Schaaper, RM | 1 |
Demontis, S; Garattini, E; Kurosaki, M; Marini, M; Salmona, M; Saltini, G; Terao, M | 1 |
Adams, B; Bailey, S; Bennett, B; Bray, RC; Smith, AT | 1 |
Anderson, LA; Boxer, DH; Leubke, T; Lubke, T; McNairn, E; Pau, RN | 1 |
Christensen, E; Gross-Hardt, S; Mendel, RR; Reiss, J; Schmidt, P; Schwarz, G | 1 |
Donahue, JP; Holm, RH; Lim, BS | 1 |
Kisker, C; Rajagopalan, KV; Schindelin, H | 1 |
Heck, IS; Kana'n, GJ; Kinghorn, JR; Millar, LJ; Sloan, J; Unkles, SE | 1 |
Heck, IS; Kanan, G; Kinghorn, JR; Millar, LJ; Schrag, JD; Sloan, J; Unkles, SE | 1 |
Hille, R | 1 |
Hänsch, R; Mendel, RR | 1 |
Brandsch, R; Sandu, C | 1 |
Dobbek, H; Gremer, L; Huber, R; Kiefersauer, R; Meyer, O | 1 |
Holm, RH; Zhang, Y | 1 |
Araujo, JA; Freuer, A; Leimkuhler, S; Mendel, RR; Rajagopalan, KV | 1 |
Atabay, Y; Klimmek, O; Kröger, A; Lyubenova, S; MacMillan, F; Prisner, T | 1 |
Edmondson, DE; Hubálek, F; Ivanov, NV; Trani, M | 1 |
Fischer, B; Mendel, RR; Nimtz, M; Otte, T; Santamaria-Araujo, JA; Schwarz, G; Wray, V | 1 |
Ahlrichs, R; Coucouvanis, D; Han, J; Nava, P | 1 |
Hunter, WN | 1 |
Hecht, HJ; Kuper, J; Llamas, A; Mendel, RR; Schwarz, G | 1 |
Enemark, JH; Joshi, HK | 1 |
Bittner, F; Heidenreich, T; Mendel, RR; Wollers, S | 1 |
Nichols, JD; Rajagopalan, KV | 1 |
Yoshida, M | 1 |
Bray, RC; Eisenthal, R; Godber, BL; Harrison, R; Lowe, DJ; Mendel, RR; Schwarz, G | 1 |
Bardischewsky, F; Friedrich, CG; Hellwig, P; Kostka, S; Quentmeier, A; Rother, D | 1 |
Bittner, F; Mendel, RR | 1 |
Cannio, R; D'Errico, G; Di Salle, A; La Cara, F; Rossi, M | 1 |
Choi, EY; Hemann, C; Hille, R; Ilich, P; Stockert, AL | 1 |
Ataya, FS; Fernandez, E; Fischer, K; Galvan, A; Kuper, J; Llamas, A; Mendel, RR; Schrader, N; Schwarz, G; Tejada-Jimenez, M | 1 |
Nichols, JD; Rajagopalan, KV; Schindelin, H; Xiang, S | 1 |
Mendel, RR | 3 |
Marquet, A; Mendel, RR; Smith, AG; Warren, MJ | 1 |
Morozkina, EV; Zvyagilskaya, RA | 1 |
Barrick, JE; Breaker, RR; Moy, RH; Regulski, EE; Ruzzo, WL; Weinberg, Z; Yao, Z | 1 |
Gladyshev, VN; Zhang, Y | 1 |
Moquin, K; Rothery, RA; Weiner, JH; Workun, GJ | 1 |
Nishino, T; Okamoto, K | 1 |
Aznar, CP; Britt, RD; Curatti, L; Hernandez, JA; Perova, Z; Rubio, LM | 1 |
Leimkühler, S; Neumann, M | 1 |
Cao, H; Hille, R; Pauff, JM | 1 |
Fingrut, DR; Li, W; Maxwell, DP | 1 |
Ryde, U; Schulzke, C; Starke, K | 1 |
Enemark, JH; Johnson-Winters, K; Tollin, G | 1 |
Chi, JC; Fischer, K; Krizowski, S; Lambeck, I; Mehlmer, N; Mueller, S; Schwarz, G; Teige, M | 1 |
Davis, AC; Enemark, JH; Johnson-Winters, K; Nordstrom, AR; Tollin, G | 1 |
Fernández, E; Galván, A; Llamas, A; Tejada-Jiménez, M | 1 |
Shi, T; Xie, J | 1 |
Astashkin, AV; Bittner, F; Enemark, JH; Klein, EL; Mendel, RR; Rajapakshe, A; Reichmann, D | 1 |
Kruse, T; Mendel, RR | 1 |
Burgmayer, SJ; Fu, Y; Williams, BR; Yap, GP | 1 |
Belaidi, AA; Schwarz, G | 1 |
Curth, U; Herzog, S; Krausze, J; Kruse, T; Mendel, RR; Pierik, AJ; Ringel, P; van den Heuvel, J | 1 |
Gast, K; Haumann, M; Horn, S; Kaufmann, P; Leidel, N; Leimkühler, S; Reschke, S; Schulzke, C; Sigfridsson, KG | 1 |
Cotelesage, JJ; George, GN; Pushie, MJ | 1 |
Haumann, M; Hille, R; Leimkühler, S; Niks, D; Rajagopalan, KV; Reschke, S; Sigfridsson, KG; Wilson, H | 1 |
Arnoux, P; Bertrand, P; Biaso, F; Burlat, B; Etienne, E; Fourmond, V; Grosse, S; Guigliarelli, B; Jacques, JG; Léger, C; Pignol, D; Sabaty, M | 1 |
Cabrita, EJ; Leimkühler, S; Otrelo-Cardoso, AR; Rodrigues, D; Romão, MJ; Santos-Silva, T; Schwuchow, V | 1 |
Azarov, I; Basu, P; Gauthier, MC; Gladwin, MT; Merchant, BA; Ragireddy, V; Sparacino-Watkins, CE; Sun, B; Tejero, J; Thomas, J; Wang, J | 1 |
Alexander, MM; Boysen, V; Kruse, T; Mendel, RR; Probst, C; Ringel, P; Wirsing, L | 1 |
Leimkühler, S; Mendel, RR | 1 |
Leimkühler, S; Yokoyama, K | 1 |
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, Y | 1 |
Li, J; Ryde, U | 1 |
Clement, B; Havemeyer, A; Ott, G | 1 |
Basu, P; Burgmayer, SJ | 1 |
Magalon, A; Mendel, RR | 1 |
Kasaragod, VB; Schindelin, H | 1 |
Ali, K; Hoffmann, MC; Masepohl, B; Narberhaus, F; Robrahn, L; Sonnenschein, M; Strauss, D | 1 |
Agresta, AM; Bittner, F; Di Silvestre, D; Donnini, S; Gehl, C; Mauri, P; Murgia, I; Vigani, G | 1 |
Duffus, BR; Iobbi-Nivol, C; Jänsch, L; Kaufmann, P; Leimkühler, S; Mitrova, B; Nimtz, M; Teutloff, C; Wollenberger, U | 1 |
Caldararu, O; Cioloboc, D; Feldt, M; Mata, RA; Nordlander, E; Ryde, U; Starke, K; van Severen, MC | 1 |
Blankenfeldt, W; Hercher, TW; Kirk, ML; Krausze, J; Kruse, T; Mendel, RR; Zwerschke, D | 1 |
Novotny, JA; Peterson, CA | 1 |
Bittner, F; Clement, B; Ginsel, C; Havemeyer, A; Kubitza, C; Scheidig, AJ | 1 |
Calatrava, V; Chamizo-Ampudia, A; Fernandez, E; Galvan, A; Llamas, A; Tejada-Jimenez, M | 1 |
Dau, H; Duffus, BR; Haumann, M; Leimkühler, S; Mebs, S; Reschke, S; Schrapers, P; Teutloff, C | 1 |
Martínez-Espinosa, RM; Miralles-Robledillo, JM; Pire, C; Torregrosa-Crespo, J | 1 |
Iobbi-Nivol, C; Leimkühler, S; Méjean, V; Zupok, A | 1 |
Blankenfeldt, W; Hercher, TW; Hoffmeister, S; Krausze, J; Kruse, T; Lindel, T; Mendel, RR; Zwerschke, D | 1 |
Leimkühler, S | 2 |
Mayr, SJ; Mendel, RR; Schwarz, G | 1 |
DeBeer, S; Decamps, L; Van Stappen, C | 1 |
Giles, LJ; Hercher, TW; Kc, K; Kirk, ML; Krausze, J; Kruse, T; Mendel, RR; Probst, C; Rees, DC; Richers, CP; Spatzal, T; Yang, J | 1 |
Enemark, JH | 1 |
Fettig, RR; Mendel, RR; Oliphant, KD; Snoozy, J; Warnhoff, K | 1 |
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, JN | 1 |
Hassan, AH; Iacobucci, C; Ihling, C; Kastritis, PL; Kruse, T; Sinz, A | 1 |
42 review(s) available for pteridines and molybdenum
Article | Year |
---|---|
Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli.
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.
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.
Topics: Amino Acid Sequence; Coenzymes; Enzymes; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Pteridines; Sequence Alignment | 1991 |
Biogenesis of molybdenum cofactors.
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.
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.
Topics: Anaerobiosis; Coenzymes; Enterobacteriaceae; Formates; Hydrogen; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Nitrates; Nitrites; Pteridines | 1988 |
Molybdopterin--problems and perspectives.
Topics: Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Structure-Activity Relationship | 1988 |
Molybdenum in nitrogenase.
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.
Topics: Animals; Bacteria; Coenzymes; Metalloproteins; Molecular Conformation; Molecular Structure; Molybdenum; Molybdenum Cofactors; Nucleotides; Oxidoreductases; Pteridines; Pterins | 1993 |
Molybdenum-cofactor-containing enzymes: structure and mechanism.
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.
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.
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].
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.
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.
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.
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.
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.
Topics: Amino Acid Sequence; Coenzymes; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Protein Conformation; Pteridines; Tungsten | 2001 |
Molybdenum and tungsten in biology.
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.
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].
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.
Topics: Aldehyde Oxidase; Cell Biology; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Pteridines; Xanthine Dehydrogenase | 2006 |
Biology of the molybdenum cofactor.
Topics: Apoenzymes; Arabidopsis; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrite Reductases; Pteridines; Sulfite Oxidase | 2007 |
Metal and cofactor insertion.
Topics: Coenzymes; Copper; Iron; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Pteridines | 2007 |
Nitrate reductases: structure, functions, and effect of stress factors.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organophosphorus Compounds; Pteridines; Pterins | 2020 |
Molybdenum cofactor biology, evolution and deficiency.
Topics: Coenzymes; Eukaryota; Gene Fusion; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Substrate Specificity | 2021 |
Metal-Containing Formate Dehydrogenases, a Personal View.
Topics: Catalytic Domain; Coenzymes; Formate Dehydrogenases; Metalloproteins; Molybdenum; Oxidation-Reduction; Pteridines | 2023 |
208 other study(ies) available for pteridines and molybdenum
Article | Year |
---|---|
Characterization of molybdenum cofactor from Escherichia coli.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
Topics: Chromatography, Affinity; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Neurospora; Neurospora crassa; Nitrate Reductases; Pteridines | 1985 |
Assay and detection of the molybdenum cofactor.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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].
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].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Amino Acid Sequence; Binding Sites; Catalysis; Catalytic Domain; Coenzymes; Eukaryota; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Protein Conformation; Pteridines; Sequence Homology | 2018 |
Molybdenum.
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.
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.
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.
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.
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.
Topics: Adenosine Monophosphate; Arabidopsis; Arabidopsis Proteins; Coenzymes; Crystallography, X-Ray; Models, Chemical; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Pteridines | 2021 |
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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.
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.
Topics: Arabidopsis; Homeostasis; Membrane Transport Proteins; Molybdenum; Pteridines | 2023 |
The structural principles underlying molybdenum insertase complex assembly.
Topics: Arabidopsis; Arabidopsis Proteins; Calnexin; Coenzymes; Metalloproteins; Molybdenum; Pteridines | 2023 |