heme has been researched along with nadp in 248 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 88 (35.48) | 18.7374 |
| 1990's | 50 (20.16) | 18.2507 |
| 2000's | 63 (25.40) | 29.6817 |
| 2010's | 40 (16.13) | 24.3611 |
| 2020's | 7 (2.82) | 2.80 |
| Authors | Studies |
|---|---|
| Mungikar, AM; Pawar, SS | 1 |
| Piette, LH; Saprin, AN | 1 |
| Ibrahim, NG; Kappas, A; Maines, MD | 1 |
| Denk, H; Eckerstorfer, R; Schenkman, JB; Talcott, RE | 1 |
| Jones, OT; Nasrulhaq-Boyce, A | 1 |
| Badawy, AA | 1 |
| Cavallin-Ståhl, E; Jönsson, GI; Lundh, B | 1 |
| Nason, A; Pan, SS | 1 |
| Guengerich, FP | 1 |
| Downey, RJ; Steiner, FX | 1 |
| Hino, Y; Minakami, S | 1 |
| Awruch, J; Frydman, B; Frydman, RB; Tomaro, ML | 1 |
| Brown, JE; Kupfer, D | 1 |
| Postma, PW; Simoni, RD | 1 |
| Dalvi, RR; HUNTER, AL; Neal, RA | 1 |
| Chavan, AJ; Garcia, RC; Haley, B; Nugent, JH; Rosen, H; Scrace, G; Segal, AW; West, I; Wientjes, F | 1 |
| Beri, R; Chandra, R; Kumar, V | 1 |
| Beale, SI; Rhie, G | 1 |
| Ishimura, Y; Makino, R; Nakamura, Y; Ohtaki, S; Tanaka, T | 1 |
| Hebbel, RP; Repka, T | 1 |
| Kadiiska, M; Stoytchev, T | 1 |
| Arutiunian, AM; Dudchenko, AM; Evstigneeva, RP; Kulish, MA; Luk'ianova, LD; Lysko, AI; Mironov, AF; Zhuravleva, DV | 1 |
| Chaney, SG; Chapman, DE; Hall, IH; Holbrook, DJ; Lee, KH | 1 |
| Cross, AR; Hancock, JT; Henderson, LM; Jones, OT; O'Donnell, VB | 1 |
| Sano, S; Sudo, Y; Yoshinaga, T | 1 |
| Marks, GS; Riddick, DS | 1 |
| Beaune, P; Descatoire, V; Labbe, G; Larrey, D; Letteron, P; Pessayre, D | 1 |
| Gelboin, HV; Marks, GS; Park, SS; Riddick, DS | 1 |
| Grab, LA; Ortiz de Montellano, PR; Swanson, BA | 1 |
| Blázovits, A; Horváth, I; Kittel, A; Marton, A; Végh, M; Venekei, I; Vodnyánszky, L | 1 |
| Köhler, H; Neupert, W; Nicholson, DW | 1 |
| Marks, GS; McCluskey, SA; Racz, WJ | 1 |
| CaJacob, CA; Chan, WK; Ortiz de Montellano, PR; Shephard, E | 1 |
| Horváth, I; Kramer, M; Rusvai, E; Végh, M | 1 |
| Ramasarma, T; Usha Devi, S | 1 |
| Correia, MA; Decker, C; Sugiyama, K; Underwood, M | 1 |
| Barynin, VV; Borisov, VV; Fita, I; Melik-Adamyan, WR; Murthy, MR; Rossmann, MG; Vagin, AA; Vainshtein, BK | 1 |
| Britt, SG; Davies, HW; Pohl, LR | 1 |
| Taketani, S; Tanaka, A; Tokunaga, R | 1 |
| Beale, SI; Weinstein, JD | 1 |
| Aft, RL; Mueller, GC | 1 |
| Ochoa, S; Palomo, C; Sierra, JM; Vicente, O | 1 |
| Marver, HS; Masters, BS; Nelson, EB; Schacter, BA | 1 |
| Kamin, H; Murphy, MJ; Siegel, LM | 2 |
| Kamin, H; Murphy, MJ; Rosenthal, D; Siegel, LM | 1 |
| DeGroot, LJ; Hati, RN | 1 |
| Dalziel, K | 1 |
| Levin, W; Lu, AY; Ryan, D; West, S | 1 |
| Cooper, DY; Rosenthal, O; Schleyer, H | 1 |
| Hildebrandt, AG; Roots, I; Speck, M | 1 |
| Coon, MJ; van der Hoeven, TA | 1 |
| Gayathri, AK; Padmanaban, G | 1 |
| Kikuchi, G; Yoshida, T | 1 |
| Marver, HS; Schmid, R; Tenhunen, R | 3 |
| Kimura, T; Ono, H | 1 |
| Chen, C; Lin, CC | 1 |
| Huennekens, FM; Kajita, A; Kerwar, GK | 1 |
| Nicholas, DJ; Prabhakararao, K | 1 |
| Baron, J; Tephly, TR | 2 |
| Gillette, JR; Greene, FE; Stripp, B | 1 |
| Bryan-Jones, DG; Whittenbury, R | 1 |
| Kumaoka, H; Yoshida, Y | 1 |
| Marver, HS; Ross, ME; Schmid, R; Tenhunen, R | 1 |
| Nebert, DW | 1 |
| Coon, MJ; Heidema, J; Lu, AY; Strobel, HW | 1 |
| Coon, MJ; McKenna, EJ | 1 |
| Marver, HS; Pimstone, NR; Schmid, R; Seitz, PT; Tenhunen, R | 1 |
| Alvares, AP; Kappas, A; Mitani, F; Sassa, S | 1 |
| Engel, P; Marver, HS; Pimstone, NR; Schmid, R; Seitz, PT; Tenhunen, R | 1 |
| Garland, PB; Ragan, CI | 1 |
| Jacobson, M; Kuntzman, R; Levin, W | 1 |
| Tenhunen, R | 1 |
| Cooper, DY; Marver, H; Pimstone, NR; Schmid, R; Tenhunen, R; Trager, WF | 1 |
| Bal, M; Datta, AG; Mahajani, U; Sen, G | 1 |
| Degkwitz, E; Höchli-Kaufmann, L; Luft, D; Staudinger, H | 1 |
| Gray, CH; Nicholson, DC; Tipton, G | 1 |
| Marver, HS; Meyer, UA; Schacter, BA | 1 |
| Bradshaw, JJ; Ivanetich, KM; Ziman, MR | 1 |
| Basile, G; Di Bello, C; Taniuchi, H | 1 |
| Hakim, J; Järvisalo, J; Torres, M | 1 |
| Kikuchi, G; Noguchi, M; Yoshida, T | 1 |
| Kikuchi, G | 1 |
| Moloney, SJ; Prough, RA; Snider, BJ | 1 |
| Beusen, DD; Carrell, HL; Covey, DF; Hood, WF | 1 |
| Fontecave, M; Leclaire, J; Mansuy, D; Momenteau, M | 1 |
| Fujita, H; Ikeda, M; Koizumi, A; Kumai, M; Sadamoto, T; Yamamoto, M | 1 |
| Johnson, EF; Liem, HH; Muller-Eberhard, U | 1 |
| Costa, AK; Ivanetich, KM | 1 |
| Adams, PA; Berman, MC | 1 |
| Adams, C; Adams, PA; Baldwin, DA; Berman, MC | 1 |
| Kunze, KL; Ortiz de Montellano, PR | 1 |
| Baird, MB | 1 |
| Abu-Soud, HM; Stuehr, DJ | 1 |
| Fukuto, JM; Griscavage, JM; Ignarro, LJ; Komori, Y | 1 |
| Abu-Soud, HM; Stuehr, DJ; Yoho, LL | 1 |
| Abu-Soud, HM; Clark, P; Feldman, PL; Stuehr, DJ | 1 |
| Klatt, P; Mayer, B; Schmidt, K; Uray, G | 1 |
| Baek, KJ; Lucas, S; Stuehr, DJ; Thiel, BA | 1 |
| Bolt, EL; Roessner, CA; Scott, AI; Spencer, JB; Warren, MJ; Woodcock, SC | 1 |
| Gonvindaraj, S; Li, H; Poulos, TL | 1 |
| Beaune, PH; Bourdi, M; Pessayre, D; Tinel, M | 1 |
| Porter, TD | 1 |
| Golly, I; Hlavica, P | 1 |
| Burka, LT; Parmar, D | 1 |
| Cho, HJ; Martin, E; Nathan, C; Sassa, S; Xie, QW | 1 |
| Koshkin, V | 1 |
| Abu-Soud, HM; Ghosh, DK; Siddhanta, U; Stuehr, DJ; Wu, C; Zhang, J | 1 |
| Chapman, SK; Coggins, JR; Daff, S; Lindsay, JG; Munro, AW | 1 |
| Andersson, I; Andreoletti, P; Gouet, P; Hajdu, J; Jouve, HM; Nussaume, L; Williams, PA | 1 |
| Feyereisen, R; Murataliev, MB | 1 |
| Abu-Soud, HM; Rousseau, DL; Stuehr, DJ | 1 |
| Berka, V; Chen, PF; Tsai, AL; Wu, KK | 1 |
| Gorren, AC; Mayer, B; Schmidt, K; Schrammel, A | 2 |
| Albores, A; Eldirdiri, NI; Ferrara, R; King, LJ; Manno, M; Tolando, R | 1 |
| Abu-Soud, HM; Blazing, MA; Gachhui, R; George, SE; Ghosha, DK; Mayer, B; Presta, A; Stuehr, DJ | 1 |
| Fan, B; Presta, A; Rousseau, DL; Siddhanta, U; Stuehr, DJ; Wolan, D | 1 |
| Rivera, M; Rodríguez, JC | 1 |
| Chapman, SK; Chumanov, GD; Hanzlik, RP; Munro, AW; Noble, MA; Quaroni, L; Turner, KL | 1 |
| Gross, SS; Ikeda-Saito, M; Liu, Q; Martásek, P; Masters, BS; Migita, CT; Miller, RT; Raman, CS; Roman, LJ; Salerno, JC | 1 |
| Inoue, N; Kamio, H; Kitamura, S; Ohta, S; Tatsumi, K; Terada, A | 1 |
| He, K; Hollenberg, PF; Woolf, TF | 1 |
| Alzari, PM; Betzel, C; Fita, I; Herzog, C; Koller, F; Maté, MJ; Nykyri, LM; Zamocky, M | 1 |
| Bravo, J; Fita, I; Loewen, PC; Mate, MJ; Schneider, T; Switala, J; Wilson, K | 1 |
| Liu, H; Mount, DB; Nasjletti, A; Wang, W | 1 |
| Cross, AR; Curnutte, JT; Erickson, RW | 1 |
| Esumi, H; Hayashi, Y; Hori, H; Iizuka, T; Iwasaki, T; Nishino, T; Ogura, T; Oue, S; Tamura, K | 1 |
| Hodge, K; Hollenberg, PF; Kent, UM; Moreno, RL | 1 |
| Ichikawa, Y; Kawazoe, T; Kosaka, H; Mizoguchi, K; Ohnishi, T; Yoneyama, H | 1 |
| Brody, SS; Gough, SP; Kannangara, CG | 1 |
| Gupte, SA; Phillibert, D; Rupawalla, T; Wolin, MS | 1 |
| Cunningham, O; Gore, MG; Mantle, TJ | 1 |
| Arvai, AS; Bourne, Y; Putnam, CD; Tainer, JA | 1 |
| Gorren, AC; Koesling, D; Mayer, B; Riethmüller, C; Schmidt, K; Schrammel, A; Werner, ER | 1 |
| Abu-Soud, HM; Ichimori, K; Presta, A; Stuehr, DJ | 1 |
| Daff, S; Sagami, I; Sato, Y; Shimizu, T | 1 |
| Adak, S; Stuehr, DJ; Wang, Q | 1 |
| Adak, S; Curran, CM; Santolini, J; Stuehr, DJ | 1 |
| Brien, JF; Graham, CH; Hutchinson, JM; Marks, GS; McLaughlin, BE; Nakatsu, K; Smith, GN | 1 |
| Kikuchi, A; Miyatake, H; Park, SY; Sato, M; Shiro, Y; Sun, D; Yoshida, T | 1 |
| Adak, S; Aulak, KS; Stuehr, DJ | 1 |
| Ghosh, S; Panda, K; Stuehr, DJ | 1 |
| Kitamura, S; Ohta, S; Sugihara, K; Takekawa, K | 1 |
| Dunham, WR; Hollenberg, PF; Kent, UM; Moon, N; Roberts-Kirchhoff, ES | 1 |
| Meade, AL; Santolini, J; Stuehr, DJ | 1 |
| Sagami, I; Sato, Y; Shimizu, T | 1 |
| Adak, S; Aulak, KS; Bilwes, AM; Crane, BR; Getzoff, ED; Hosfield, D; McDonald, JF; Panda, K; Stuehr, DJ; Tainer, JA | 1 |
| Page, AM; Raitt, CE; Ryberg, M; Terry, MJ | 1 |
| Porasuphatana, S; Pou, S; Rosen, GM; Tsai, P | 1 |
| Daff, SN; Fujimoto, N; Rozhkova, EA; Sagami, I; Shimizu, T | 1 |
| Hollenberg, PF; Kent, UM; Lin, HL | 1 |
| Dioum, EM; Gilles-Gonzalez, MA; Gonzalez, G; McKnight, SL; Rutter, J; Tuckerman, JR | 1 |
| Alworth, WL; Blobaum, AL; Hollenberg, PF; Kent, UM | 1 |
| Andreoletti, P; Gagnon, J; Jaquinod, M; Jouve, HM; Sainz, G | 1 |
| Boehning, D; Snyder, SH | 1 |
| Carpena, X; Donald, LJ; Duckworth, HW; Fita, I; Klotz, MG; Loewen, PC; Melik-Adamyan, W; Soriano, M | 1 |
| Ghosh, S; Mukherjee, S; Regulski, M; Sahoo, R; Sengupta, R; Stuehr, DJ; Tully, T | 1 |
| BIOERCK, G; PALEUS, S | 1 |
| NAKAJIMA, H; NAKAJIMA, O; TAKEMURA, T; YAMAOKA, K | 1 |
| GARFINKEL, D | 1 |
| Murray, K; Murray, M | 1 |
| Adak, S; Konas, D; Panda, K; Sharma, M; Stuehr, DJ | 1 |
| Baillie, TA; Kumar, S; Mitra, K; Stearns, RA; Yin, W | 1 |
| Chapman, SK; Cheesman, MR; Fulco, AJ; Gustafsson, MC; Marshall, KR; Munro, AW; Noble, MA; Pessegueiro, A; Roitel, O; von Wachenfeldt, C | 1 |
| Goosen, TC; Hollenberg, PF; Kent, UM; Sridar, C; Williams, JA | 1 |
| Boschero, AC; Carneiro, EM; Ferreira, F; Filiputti, E; Rezende, LF; Stoppiglia, LF | 1 |
| Lad, L; Ortiz de Montellano, PR; Poulos, TL; Wang, J | 1 |
| Mayer, B; Schmidt, K | 1 |
| Furukawa, M; Ikeda-Saito, M; Matsui, T; Tomita, T; Unno, M | 1 |
| Bould, J; Iles, DE; Kemp, PJ; Mason, HS; Peers, C; Riccardi, D; Williams, SE; Wootton, P | 1 |
| Hoshi, T; Lahiri, S | 1 |
| Migita, CT; Sasahara, M; Sato, M; Yoshida, T; Zhang, X | 1 |
| Panda, K; Santolini, J; Stuehr, DJ; Wang, Q; Wang, ZQ; Wei, CC | 1 |
| Garcin, ED; Getzoff, ED; Konas, DW; Panda, K; Sharma, M; Stuehr, DJ; Tiso, M | 1 |
| Brown, KM; Murphy, SE; von Weymarn, LB | 1 |
| Enemark, JH; Feng, C; Ghosh, DK; Holliday, MA; Salerno, JC; Thomas, C; Tollin, G | 1 |
| Hutzler, JM; Locuson, CW; Tracy, TS | 1 |
| Hollenberg, PF; Lin, HL | 1 |
| Beaumont, E; Berka, V; Blanchard-Desce, M; Gautier, C; Gmouh, S; Lambry, JC; Robin, AC; Slama-Schwok, A; Tsai, AL | 1 |
| de Armas, M; Katz, A; Levicán, G; Núñez, H; Orellana, O | 1 |
| Jones, JP; Locuson, CW; Tracy, TS; Wienkers, LC | 1 |
| Altieri, F; Dewilde, S; Hoogewijs, D; Moens, L; Ramser, K; Rivetti di Val Cervo, P; Trandafir, F; Van Doorslaer, S; Vanfleteren, JR | 1 |
| Feyereisen, R; Girvan, HM; Guzov, VM; Munro, AW; Murataliev, M; Noble, MA; Smith, SJ; Smith, WE | 1 |
| Dombek, KM; Liu, JC; McKnight, SL; Mohler, RE; Synovec, RE; Tu, BP; Young, ET | 1 |
| Aulak, KS; Panda, K; Stuehr, DJ; Tejero, J; Tiso, M | 1 |
| Boer, R; Hesslinger, C; Kenney, CT; Strub, A; Stuehr, DJ; Tiso, M | 1 |
| Bondlela, M; Chen, B; Haines, DC; Hegde, A; Machius, M; Peterson, JA; Tomchick, DR | 1 |
| de Groot, H; Korth, HG; Sicking, W; Sustmann, R | 1 |
| Buldain, G; de Montellano, PO; Evans, JP; Niemevz, F | 1 |
| Cardounel, AJ; Chen, CA; Druhan, LJ; Forbes, SP; Pope, AJ; Zweier, JL | 1 |
| Bluhm, U; Boucher, JL; Buss, U; Clement, B; Friedrich, F; Girreser, U; Heber, D; Lam, T; Lepoivre, M; Rostaie-Gerylow, M; Wolschendorf, U | 1 |
| Hollenberg, PF; Lin, HL; Zhang, H | 1 |
| Gu, Y; Publicover, S; Wang, S | 1 |
| Andreoletti, P; Capeillère-Blandin, C; Gouet, P; Jaquinod, M; Jouve, HM; Mouesca, JM | 1 |
| Fadlalla, M; Haque, MM; Panda, K; Ray, SS; Stuehr, DJ; Wang, ZQ | 1 |
| Agapie, T; Britt, RD; Marletta, MA; Stoll, S; Suseno, S; Woodward, JJ | 1 |
| Appanna, VD; Chénier, D; Hamel, R; Lemire, J; Mailloux, RJ; Singh, R | 1 |
| Stuehr, DJ; Wang, ZQ; Wei, CC | 1 |
| Corcelli, A; Liquori, GE; Lopalco, P; Lorusso, M; Mastrodonato, M; Saponetti, MS; Zaccagnino, P | 1 |
| Bruce, NC; Delenne, M; Flitsch, S; Grogan, G; Hilgarth, EM; Hyde, R; Robin, A; Sabbadin, F; Turner, N | 1 |
| Durra, D; Haque, MM; Stuehr, DJ; Tejero, J | 1 |
| Degregorio, D; Di Nardo, G; Gilardi, G; Sadeghi, SJ; Solinas, SP | 1 |
| Stevenson, DK; Vreman, HJ; Wong, RJ | 1 |
| Qu, HY; Shang, ZL; Tao, ST; Wu, HQ; Wu, J; Wu, JY; Xu, GH; Zhang, SL | 1 |
| Beckerich, JM; Casaregola, S; Hébert, A | 1 |
| Barreca, D; Bellocco, E; De Rosa, MC; Ficarra, S; Galtieri, A; Giardina, B; Laganà, G; Leuzzi, U; Pirolli, D; Russo, A; Tellone, E | 1 |
| Hannibal, L; Somasundaram, R; Stuehr, DJ; Tejero, J; Wilson, A | 1 |
| Blank, O; Davioud-Charvet, E; Elhabiri, M | 1 |
| Nicholls, P | 1 |
| Amunugama, HT; Hollenberg, PF; Zhang, H | 1 |
| Hollenberg, PF; Kenaan, C; Sridar, C | 1 |
| Faut, M; Mazzetti, MB; Paiz, A; San Martín de Viale, LC | 1 |
| Curth, U; Herzog, S; Krausze, J; Kruse, T; Mendel, RR; Pierik, AJ; Ringel, P; van den Heuvel, J | 1 |
| Hollenberg, PF; Kent, UM; Yoshigae, Y | 1 |
| Bayachou, M; Fadlalla, M; Haque, MM; Stuehr, DJ; Tejero, J; Wang, ZQ | 1 |
| Chau, CHT; Kobylarz, MJ; Loutet, SA; Murphy, MEP | 1 |
| Cueno, ME; Imai, K; Ochiai, K; Tamura, M | 1 |
| Chen, X; Dong, W; Fang, Y; Gong, W; Lin, Y; Liu, L; Zhao, A; Zhao, S | 1 |
| Barbero, L; Bojić, M; Dolgos, H; Freisleben, A; Gallemann, D; Guengerich, FP; Riva, S | 1 |
| Gebicka, L; Gebicki, JL; Krych, J | 1 |
| Bolles, AK; Briggs, ED; Fujiwara, R; Furge, LL; Nomeir, AA | 1 |
| Allegra, P; Castrignanò, S; Di Nardo, G; Gilardi, G; Minerdi, D; Rua, F; Sadeghi, SJ | 1 |
| Cueno, ME; Ochiai, K; Tamura, M | 1 |
| Dlakić, M; Kleven, MD; Lawrence, CM | 1 |
| Holden, JK; Hollingsworth, SA; Li, H; Poulos, TL | 1 |
| Jaiswal, D; Mazumdar, S; Parhad, SS; Ray, K | 1 |
| Denkhaus, L; Fisher, K; Hay, S; Lafite, P; Leys, D; Menon, BR; Munro, AW; Ortmayer, M; Rigby, SE; Scrutton, NS; Tralau, T | 1 |
| Chaurasia, AK; Choi, J; Ha, SC; Kim, D; Kim, H; Kim, KK; Kim, T | 1 |
| Delrossi, M; Keul, ND; LaMattina, JW; Lanzilotta, WN; Neelam, AR; Nix, DB; Uy, KG | 1 |
| Bell, SG; Maddigan, NK | 1 |
| Ishimori, K; Onzuka, M; Ozaki, SI; Sekine, Y; Uchida, T | 1 |
| Bocola, M; Davari, MD; Mueller-Dieckmann, J; Panneerselvam, S; Schwaneberg, U; Shehzad, A; Wilmanns, M | 1 |
| Chen, F; Gou, R; Guo, Y; Li, H; Ma, P; Pu, J; Tang, L; Wang, B; Wang, R; Wang, Y; Zheng, B | 1 |
| Balci, S; Goc, G; McPherson, MJ; Pearson, AR; Trinh, CH; Yorke, BA; Yuzugullu Karakus, Y | 1 |
| Förster, F; Granneman, J; Gros, P; Mattevi, A; Oosterheert, W; Rodenburg, RNP; van Bezouwen, LS | 1 |
| Battaile, KP; Benson, DR; Cooper, A; Galeva, N; Gao, P; Lovell, S; Mehzabeen, N; Zhu, H | 1 |
| Gleadle, JM; MacGregor, MN; McNicholas, K | 1 |
| Feng, C; Li, J; Zheng, H | 1 |
| Brimberry, M; Hines, KM; Lanzilotta, WN; Toma, MA | 1 |
| Cortez, N; González, JM; Sartorio, MG | 1 |
| Bhadauria, M; Nirala, SK; Rakshit, S; Sahu, N | 1 |
| Marchese, S; Mascotti, ML; Massari, M; Mattevi, A; Nicoll, CR | 1 |
| Brimberry, M; Corrigan, P; Lanzilotta, WN; Silakov, A | 1 |
| Chen, K; Shen, J; Tsai, AL; Wang, L; Wu, G; Zhou, M | 1 |
8 review(s) available for heme and nadp
| Article | Year |
|---|---|
The functions and regulation of tryptophan pyrrolase.
Topics: Allosteric Regulation; Aminolevulinic Acid; Animals; Dactinomycin; Feedback; Gluconeogenesis; Heme; Kinetics; Kynurenine; Liver; NAD; NADP; Rats; Tryptophan; Tryptophan Oxygenase | 1977 |
The energetics of bacterial active transport.
Topics: Acridines; Adenosine Triphosphatases; Adenosine Triphosphate; Bacteria; Biological Transport, Active; Carrier Proteins; Cell Membrane; Diffusion; Electron Transport; Energy Transfer; Heme; L-Lactate Dehydrogenase; Membrane Potentials; Mutagens; NAD; NADP; Osmotic Pressure; Oxidative Phosphorylation; Protons; Ubiquinone | 1975 |
Inhibitors of NADPH oxidase as guides to its mechanism.
Topics: Binding Sites; Cell Membrane; Cytochrome b Group; Electron Transport; Heme; Humans; NADH, NADPH Oxidoreductases; NADP; NADPH Oxidases; Neutrophils | 1991 |
Kinetics of control enzymes.
Topics: Animals; Cattle; Coenzymes; Enzyme Activation; Enzyme Induction; Enzymes; Fluorescence; Glutamate Dehydrogenase; Heme; Kinetics; Ligands; Models, Chemical; NAD; NADP; Oxidation-Reduction; Protein Binding; Rabbits | 1973 |
[Heme catabolism: its mechanism and regulation].
Topics: Animals; Bile; Bilirubin; Biliverdine; Enzyme Induction; Heme; Heme Oxygenase (Decyclizing); Humans; Iron; Mixed Function Oxygenases; NADP; Rabbits; Rats | 1983 |
CARDIAC HEMATIN COMPOUNDS.
Topics: Adenosine Triphosphate; Citric Acid Cycle; Cytochromes; Heme; Hemin; Hemoglobins; Iron; Metabolism; Muscles; Myocardium; Myoglobin; NAD; NADP; Oxygen | 1963 |
Classical catalase: ancient and modern.
Topics: Biochemistry; Catalase; Electrons; Gene Expression Regulation, Enzymologic; Heme; History, 20th Century; Humans; Hydrogen Bonding; Kinetics; Ligands; Models, Chemical; Molecular Conformation; NADP; Protons | 2012 |
In order for the light to shine so brightly, the darkness must be present-why do cancers fluoresce with 5-aminolaevulinic acid?
Topics: Amino Acid Transport Systems; Aminolevulinic Acid; Brain Neoplasms; Coproporphyrinogens; Ferrochelatase; Fluorescence; Glucose; Heme; Humans; Iron; MicroRNAs; Mitochondria; Mutation; NADP; Neoplasms; Oncogenes; Optical Imaging; Peptide Transporter 1; Photochemotherapy; Protoporphyrins; Skin Neoplasms; Symporters; Tumor Hypoxia; Tumor Microenvironment; Urinary Bladder Neoplasms | 2019 |
240 other study(ies) available for heme and nadp
| Article | Year |
|---|---|
Dioxane-induced changes in mouse liver microsomal mixed function oxidase system.
Topics: Animals; Ascorbic Acid; Cytochrome P-450 Enzyme System; Cytochromes; Dioxanes; Dioxins; Female; Heme; Lipid Metabolism; Liver; Mice; Microsomes, Liver; Mixed Function Oxygenases; NADP; Organ Size; Oxidoreductases; Peroxides; Phenobarbital | 1976 |
Spin trapping and its application in the study of lipid peroxidation and free radical production with liver microsomes.
Topics: Animals; Cyclic N-Oxides; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Lipid Metabolism; Male; Malondialdehyde; Microsomes, Liver; NADP; Nitrosamines; Propyl Gallate; Rats; Solvents; Tromethamine | 1977 |
Solubilization and partial purification of heme oxygenase from rat liver.
Topics: Animals; Cytochrome P-450 Enzyme System; Cytochromes; Heme; Kinetics; Magnesium; Male; Microsomes, Liver; Mixed Function Oxygenases; NAD; NADP; Polyethylene Glycols; Rats; Structure-Activity Relationship; Sulfhydryl Compounds | 1977 |
Alteration of hepatic microsomal enzymes by griseofulvin treatment of mice.
Topics: Animals; Body Weight; Cytochrome P-450 Enzyme System; Cytochromes; Fatty Acid Desaturases; Griseofulvin; Heme; In Vitro Techniques; Lipid Metabolism; Liver; Male; Mice; Microsomes, Liver; Mixed Function Oxygenases; NAD; NADP; Organ Size; Proteins; Time Factors | 1977 |
A possible involvement of protohaem in the induction of nitrate reductase in etiolated barley.
Topics: Darkness; Enzyme Induction; Heme; Hordeum; Kinetics; Light; NAD; NADP; Nitrate Reductases; Plants | 1977 |
A new method for determination of microsomal haem oxygenase (EC 1.14.99.3) based on quantitation of carbon monoxide formation.
Topics: Animals; Carbon Monoxide; Chromatography, Gas; Heme; In Vitro Techniques; Methemalbumin; Methods; Microsomes; Mixed Function Oxygenases; NADP; Rats | 1978 |
Purification and characterization of homogeneous assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase from Neurospora crassa.
Topics: Copper; Heme; Iron; Kinetics; Molybdenum; NADP; Neurospora; Neurospora crassa; Nitrate Reductases; Peptide Fragments; Zinc | 1978 |
Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase.
Topics: Animals; Carbon Monoxide; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Heme; Hemeproteins; Male; Microsomes, Liver; NADP; Oxidation-Reduction; Rats; Spectrophotometry | 1978 |
Further characterization of the reduced nicotinamide adenine dinucleotide phosphate: nitrate oxidoreductase in Aspergillus nidulans.
Topics: Aspergillus nidulans; Chemical Phenomena; Chemistry; Electrophoresis, Polyacrylamide Gel; Heme; Molecular Weight; NADP; Nitrate Reductases | 1979 |
Electron-transport pathway of the NADH-dependent haem oxygenase system of rat liver microsomal fraction induced by cobalt chloride.
Topics: Animals; Biliverdine; Cobalt; Electron Transport; Enzyme Induction; Heme; In Vitro Techniques; Kinetics; Male; Microsomes, Liver; Mixed Function Oxygenases; NAD; NADP; NADPH-Ferrihemoprotein Reductase; Rats | 1979 |
Concerning the specificity of heme oxygenase: the enzymatic oxidation of synthetic hemins.
Topics: Animals; Female; Heme; Microsomes, Liver; Mixed Function Oxygenases; NAD; NADP; Oxidation-Reduction; Rats; Substrate Specificity | 1979 |
Interactions of heme with hepatic microsomal mono-oxygenase. Effect on benzpyrene hydroxylation.
Topics: Animals; Benzopyrenes; Binding Sites; Cytochrome P-450 Enzyme System; Heme; Hydroxylation; Kinetics; Male; Microsomes, Liver; Mixed Function Oxygenases; NADP; Porphyrins; Protein Binding; Rats | 1975 |
Toxicological implications of the mixed-function oxidase catalyzed metabolism of carbon disulfide.
Topics: Animals; Benzphetamine; Carbon Disulfide; Cytochrome P-450 Enzyme System; Heme; Kinetics; Male; Malondialdehyde; Microsomes, Liver; Mixed Function Oxygenases; NADP; Oxidoreductases; Proadifen; Protein Binding; Rats; Sulfur Oxides; Sulfur Radioisotopes | 1975 |
Cytochrome b-245 is a flavocytochrome containing FAD and the NADPH-binding site of the microbicidal oxidase of phagocytes.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cell Line; Cell Membrane; Chromatography, Affinity; Chromatography, Ion Exchange; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Heme; Humans; Macromolecular Substances; Models, Structural; Molecular Sequence Data; Molecular Weight; NADH, NADPH Oxidoreductases; NADP; NADPH Oxidases; Neutrophils; Oxidation-Reduction; Phagocytosis; Protein Conformation; Rats; Sequence Homology, Nucleic Acid; Superoxides | 1992 |
Metal-metal interaction inhibits the NADP(+)-specific isocitrate dehydrogenase activity in rat brain.
Topics: Animals; Brain; Female; Heme; Isocitrate Dehydrogenase; Metalloporphyrins; Metals; NADP; Protoporphyrins; Rats; Rats, Wistar | 1992 |
Biosynthesis of phycobilins. Ferredoxin-supported nadph-independent heme oxygenase and phycobilin-forming activities from Cyanidium caldarium.
Topics: Cell Fractionation; Ferredoxins; Heme; Heme Oxygenase (Decyclizing); Kinetics; Molecular Structure; NADP; Oxidation-Reduction; Phycobilins; Phycocyanin; Pyrroles; Rhodophyta; Tetrapyrroles | 1992 |
Mechanism of H2O2 production in porcine thyroid cells: evidence for intermediary formation of superoxide anion by NADPH-dependent H2O2-generating machinery.
Topics: Animals; Catalase; Cell Membrane; Cytosol; Egtazic Acid; Erythrocytes; Heme; Horseradish Peroxidase; Hydrogen Peroxide; In Vitro Techniques; Kinetics; NADP; Neutrophils; Oxidation-Reduction; Oxygen Consumption; Superoxide Dismutase; Superoxides; Swine; Thyroid Gland | 1991 |
Hydroxyl radical formation by sickle erythrocyte membranes: role of pathologic iron deposits and cytoplasmic reducing agents.
Topics: Anemia, Sickle Cell; Ascorbic Acid; Deferoxamine; Erythrocyte Membrane; Free Radicals; Glutathione; Heme; Humans; Hydrogen Peroxide; Hydroxides; Hydroxyl Radical; Iron; Kinetics; Lipid Peroxidation; NAD; NADP; Oxidation-Reduction; Reference Values | 1991 |
Effect of continuous treatment with some heavy metal salts upon rat hepatic monooxygenases.
Topics: 5-Aminolevulinate Synthetase; Animals; Behavior, Animal; Body Weight; Cytochrome P-450 Enzyme System; Cytochromes b5; Heme; Lipid Peroxidation; Liver; Male; Metals; Mixed Function Oxygenases; NADP; Rats; Rats, Inbred Strains | 1991 |
[The mechanism of the antioxidant effect of cytochrome C heme nonapeptide].
Topics: Animals; Antioxidants; Catalysis; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochromes c; Drug Interactions; Heme; Lipid Peroxides; Microsomes, Liver; NADP; Peptide Fragments; Rats | 1990 |
In vivo and in vitro effects of helenalin on mouse hepatic microsomal cytochrome P450.
Topics: Animals; Cytochrome P-450 Enzyme System; Heme; Lipid Peroxidation; Male; Mice; Microsomes, Liver; Mixed Function Oxygenases; NADP; Oxygen Consumption; Sesquiterpenes; Sesquiterpenes, Guaiane | 1991 |
Enzymic conversion of alpha-oxyprotohaem IX into biliverdin IX alpha by haem oxygenase.
Topics: Animals; Biliverdine; Cattle; Chromatography, High Pressure Liquid; Heme; Heme Oxygenase (Decyclizing); In Vitro Techniques; Kinetics; NADP; NADPH-Ferrihemoprotein Reductase; Spectrum Analysis; Spleen | 1990 |
Irreversible binding of heme to microsomal protein during inactivation of cytochrome P450 by 4-alkyl analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine.
Topics: Animals; Benzoflavones; beta-Naphthoflavone; Cytochrome P-450 Enzyme System; Dexamethasone; Dicarbethoxydihydrocollidine; Enzyme Induction; Heme; Isoenzymes; Male; Microsomes, Liver; NADP; Phenobarbital; Proteins; Rats; Rats, Inbred Strains | 1990 |
Suicide inactivation of cytochrome P-450 by methoxsalen. Evidence for the covalent binding of a reactive intermediate to the protein moiety.
Topics: Animals; Carbon Monoxide; Carbon Tetrachloride; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Heme; Kinetics; Methoxsalen; Microsomes, Liver; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Precipitin Tests; Protein Binding; Rats; Rats, Inbred Strains; Spectrum Analysis; Ultraviolet Rays | 1989 |
Effects of a series of 4-alkyl analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine on the major inducible cytochrome P-450 isozymes of rat liver.
Topics: Animals; Antibodies, Monoclonal; Benzoflavones; beta-Naphthoflavone; Cytochrome P-450 Enzyme System; Dexamethasone; Dicarbethoxydihydrocollidine; Dihydropyridines; Enzyme Induction; Heme; Isoenzymes; Male; NADP; Phenobarbital; Rats; Rats, Inbred Strains | 1989 |
Cytochrome P-450 inactivation by 3-alkylsydnones. Mechanistic implications of N-alkyl and N-alkenyl heme adduct formation.
Topics: Animals; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Indicators and Reagents; Kinetics; Magnetic Resonance Spectroscopy; Male; Microsomes, Liver; NADP; Oxadiazoles; Oxidation-Reduction; Protein Binding; Protoporphyrins; Rats; Rats, Inbred Strains; Sydnones | 1988 |
Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c.
Topics: Animals; Brain; Cytochrome c Group; Cytochromes c; Heme; Kinetics; Lipid Peroxides; Microsomes; Microsomes, Liver; NAD; NADP; Oxygen Consumption; Peptide Fragments; Rats; Rats, Inbred Strains | 1985 |
Import of cytochrome c into mitochondria. Cytochrome c heme lyase.
Topics: Chromatography, High Pressure Liquid; Cysteine; Cytochrome c Group; Ethylmaleimide; Heme; Hemin; Lyases; Mitochondria; Models, Molecular; NAD; NADP; Neurospora crassa; Peptide Fragments; Protein Conformation; Reticulocytes; Trypsin | 1987 |
Properties of 17- to 19-day-old chick embryo liver microsomes. Induction of cytochrome P-450, effect of storage at low temperature, and resistance to lipid peroxidation.
Topics: Animals; Chick Embryo; Cold Temperature; Cytochrome P-450 Enzyme System; Edetic Acid; Enzyme Induction; Heme; Lipid Peroxides; Malondialdehyde; Microsomes, Liver; NADP; Time Factors; Tissue Preservation | 1986 |
The catalytic site of rat hepatic lauric acid omega-hydroxylase. Protein versus prosthetic heme alkylation in the omega-hydroxylation of acetylenic fatty acids.
Topics: Alkylation; Animals; Binding Sites; Chromatography, High Pressure Liquid; Clofibrate; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System; Fatty Acids, Unsaturated; Heme; Isoenzymes; Liver; Male; Mixed Function Oxygenases; NADP; Rats; Rats, Inbred Strains | 1988 |
Hydroxylation of aniline mediated by heme-bound oxy-radicals in a heme peptide model system.
Topics: Aniline Compounds; Catalase; Dose-Response Relationship, Drug; Free Radicals; Heme; Hydroxylation; Models, Chemical; NADP; Superoxide Dismutase | 1988 |
Hemin-mediated oxidative inactivation of 3-hydroxy-3-methylglutaryl CoA reductase.
Topics: Acyl Coenzyme A; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Heme; Hemin; Hydroxymethylglutaryl CoA Reductases; Hydroxymethylglutaryl-CoA Reductase Inhibitors; NADP; Oxygen | 1987 |
Inactivation of rat hepatic cytochrome P-450 by spironolactone.
Topics: Animals; Cytochrome P-450 Enzyme Inhibitors; Dexamethasone; Drug Synergism; Heme; Male; Microsomes, Liver; NADP; Rats; Rats, Inbred Strains; Spironolactone; Time Factors; Troleandomycin | 1986 |
Comparison of beef liver and Penicillium vitale catalases.
Topics: Amino Acid Sequence; Animals; Biological Evolution; Catalase; Cattle; Clostridium; Crystallography; Flavodoxin; Heme; Liver; Macromolecular Substances; Models, Molecular; NADP; Penicillium; Protein Conformation | 1986 |
Inactivation of cytochrome P-450 by 2-isopropyl-4-pentenamide and other xenobiotics leads to heme-derived protein adducts.
Topics: Acetamides; Allylisopropylacetamide; Animals; Cytochrome P-450 Enzyme Inhibitors; Heme; Male; Microsomes, Liver; NADP; Porphyrins; Protein Binding; Proteins; Rats; Rats, Inbred Strains | 1986 |
Reconstitution of heme-synthesizing activity from ferric ion and porphyrins, and the effect of lead on the activity.
Topics: Animals; Ferric Compounds; Heme; Iron; Lead; Metalloporphyrins; Microsomes, Liver; NADH Dehydrogenase; NADH, NADPH Oxidoreductases; NADP; NADPH-Ferrihemoprotein Reductase; Porphyrins; Rats | 1985 |
Enzymatic conversion of glutamate to delta-aminolevulinate in soluble extracts of the unicellular green alga, Chlorella vulgaris.
Topics: Adenosine Triphosphate; Aminolevulinic Acid; Binding Sites; Catalysis; Chlorella; Glutamates; Heme; Levulinic Acids; NADP; Nucleotides; Solutions; Temperature | 1985 |
Degradation and covalent cross-linking of glutathione reductase by hemin.
Topics: Electrophoresis, Polyacrylamide Gel; Glutathione Reductase; Heme; Hemin; NADP; Oxygen; Yeasts | 1985 |
Studies on the activation of the heme-stabilized translational inhibitor of reticulocyte lysates by oxidized glutathione and NADPH depletion.
Topics: Ammonia; Animals; Dithiothreitol; eIF-2 Kinase; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Eukaryotic Initiation Factor-2; Glucose-6-Phosphate; Glucosephosphates; Glutamate Dehydrogenase; Glutathione; Glutathione Disulfide; Heme; Ketoglutaric Acids; NADP; Peptide Initiation Factors; Protein Biosynthesis; Protein Kinases; Proteins; Rabbits; Reticulocytes | 1985 |
Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system.
Topics: Animals; Cyanides; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport; Female; gamma-Globulins; Heme; Male; Microsomes; Microsomes, Liver; NADP; Oxidoreductases; Oxygenases; Protein Binding; Rabbits; Rats; Spleen; Swine | 1972 |
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups.
Topics: Amino Acids; Ammonium Sulfate; Chemical Precipitation; Chromatography, Gel; Chromatography, Thin Layer; Electron Spin Resonance Spectroscopy; Electrophoresis, Disc; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Immunoelectrophoresis; Iron; Ligands; Molecular Weight; NADH, NADPH Oxidoreductases; NADP; Oxidoreductases; Spectrophotometry; Sulfides; Sulfites; Ultracentrifugation | 1973 |
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. II. Identification of a new class of heme prosthetic group: an iron-tetrahydroporphyrin (isobacteriochlorin type) with eight carboxylic acid groups.
Topics: Carbon Isotopes; Carboxylic Acids; Chromatography, Thin Layer; Copper; Escherichia coli; Heme; Iron; Mass Spectrometry; Metals; NADP; Oxidation-Reduction; Oxidoreductases; Porphyrins; Radioisotopes; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Infrared; Sulfites | 1973 |
Studies on the mechanism of iodination supported by thyroidal NADPH-cytochrome c reductase.
Topics: Animals; Carbon Radioisotopes; Cattle; Coloring Agents; Cytochrome c Group; Depression, Chemical; Ferricyanides; Formates; Guaiacol; Heme; In Vitro Techniques; Iodides; Iodine Radioisotopes; Isoproterenol; NADH, NADPH Oxidoreductases; NADP; Potassium; Pyrogallol; Temperature; Thyroid Gland; Trypsin; Tyrosine; Vitamin K | 1973 |
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme.
Topics: Carbon Monoxide; Enterobacteriaceae; Escherichia coli; Flavoproteins; Heme; Hemeproteins; Iron; Kinetics; Mathematics; NADP; Oscillometry; Oxidation-Reduction; Oxidoreductases; Photolysis; Porphyrins; Spectrophotometry; Structure-Activity Relationship; Sulfites | 1974 |
Preparation of partially purified, lipid-depleted cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase from rat liver microsomes.
Topics: Animals; Cholic Acids; Chromatography, DEAE-Cellulose; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Cytochromes; Detergents; Heme; Male; Methylcholanthrene; Microsomes, Liver; NADP; Phenobarbital; Phospholipids; Rats; Spectrophotometry; Ultrafiltration | 1974 |
The heme protein P-450 in steroid hydroxylation.
Topics: Adrenal Glands; Animals; Binding Sites; Corticosterone; Cyanides; Cytochrome c Group; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Fluorides; Heme; Hemoglobins; Horses; Humans; Iron; Metyrapone; Myocardium; NADP; Pregnenolone; Protein Binding; Species Specificity; Spectrophotometry; Spectrophotometry, Infrared; Spectrophotometry, Ultraviolet; Steroid Hydroxylases | 1973 |
The effects of substrates of mixed function oxidase on ethanol oxidation in rat liver microsomes.
Topics: Acetaldehyde; Aminopyrine; Animals; Azides; Catalase; Cytochrome P-450 Enzyme System; Ethanol; Formaldehyde; Heme; Hydrogen Peroxide; Kinetics; Male; Mathematics; Microsomes, Liver; Morphinans; NADP; Oxidoreductases; Oxygen Consumption; Rats | 1974 |
Preparation and properties of partially purified cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase from rabbit liver microsomes.
Topics: Animals; Binding Sites; Carbon Monoxide; Centrifugation, Density Gradient; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Detergents; Dithionite; Electrophoresis, Disc; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Male; Microsomes, Liver; Mixed Function Oxygenases; Molecular Weight; NADP; Oxidation-Reduction; Phospholipids; Polyethylene Glycols; Protein Binding; Rabbits; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfides | 1974 |
Biochemical effects of 3,5-diethoxycarbonyl-1,4-dihydrocollidine in mouse liver.
Topics: Allylisopropylacetamide; Aniline Compounds; Animals; Carbon Radioisotopes; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Dicarboxylic Acids; Female; Heme; Iron Radioisotopes; Kinetics; Leucine; Lipid Metabolism; Liver; Mice; Microsomes, Liver; Mitochondria, Liver; Mixed Function Oxygenases; NADP; Organ Size; Phenobarbital; Phospholipids; Protein Biosynthesis; Pyridines; Ribonucleases; RNA | 1974 |
Sequence of the reaction of heme catabolism catalyzed by the microsomal heme oxygenase system.
Topics: Animals; Carbon Monoxide; Cytochrome Reductases; Heme; Hydrogen-Ion Concentration; Microsomes; Microsomes, Liver; NADP; Oxidation-Reduction; Oxygenases; Protein Binding; Spectrophotometry; Spleen; Swine; Thiosulfates; Time Factors | 1974 |
The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.
Topics: Animals; Bilirubin; Heme; Liver; Microsomes; NADP; Oxygen; Rats; Spectrophotometry | 1968 |
Preparation of testis non-heme iron protein and substitution for adrenodoxin by various non-heme iron proteins in steroid 11-beta-hydroxylation.
Topics: Adrenal Glands; Animals; Cellulose; Chemical Phenomena; Chemistry, Physical; Corticosterone; Cytochromes; Electron Spin Resonance Spectroscopy; Euglena; Female; Ferredoxins; Heme; Iron; Liver; Male; NADP; Optical Rotatory Dispersion; Ovary; Oxidoreductases; Plants, Edible; Proteins; Pseudomonas; Spectrophotometry; Swine; Testis; Ultracentrifugation | 1968 |
Mechanism of aliphatic hydroxylation. Tetralin hydroperoxide as an intermediate in the hydroxylation of tetralin in rat-liver homogenate.
Topics: Animals; Azides; Benzoates; Carbon Monoxide; Catalase; Chloromercuribenzoates; Chromatography, Gas; Cytochromes; Heme; Hemoglobins; Hydrogen-Ion Concentration; Iron; Kinetics; Liver; Male; Mercury; Models, Biological; Models, Chemical; NADP; Naphthalenes; Peroxidases; Peroxides; Rats | 1968 |
Multiple forms of methemoglobin reductase.
Topics: Acetone; Chromatography, Ion Exchange; Cytochromes; Drug Stability; Electron Transport; Erythrocytes; Heme; Hot Temperature; Humans; Indophenol; Kinetics; Methemoglobin; Methods; Methylene Blue; NAD; NADP; Nucleotides; Oxidoreductases; Oxygen; Quaternary Ammonium Compounds; Spectrum Analysis; Sulfates; Sulfonic Acids | 1969 |
Sulphite reductase from bakers' yeast: a haemoflavoprotein.
Topics: Benzoates; Carbon Monoxide; Cell-Free System; Chromatography, Gel; Chromatography, Ion Exchange; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Heme; Kinetics; Light; Methods; NADP; Nitrobenzenes; Oxidoreductases; Plant Proteins; Riboflavin; Saccharomyces; Spectrum Analysis; Sulfites; Sulfur Isotopes | 1969 |
The role of heme synthesis during the induction of hepatic microsomal cytochrome P-450 and drug metabolism produced by benzpyrene.
Topics: Acyltransferases; Amino Acids; Animals; Azo Compounds; Benzopyrenes; Carbon Isotopes; Cytochromes; Depression, Chemical; Enzyme Induction; Glycine; Heme; Levulinic Acids; Liver; Male; Microsomes; NADP; Oxidoreductases; Phenobarbital; Rats; Stimulation, Chemical; Time Factors; Transferases; Triazoles | 1969 |
Microsomal heme oxygenase. Characterization of the enzyme.
Topics: Animals; Azides; Benzoates; Bilirubin; Brain; Carbon Monoxide; Cyanides; Depression, Chemical; Detergents; Deuterium; Heme; Hemoglobins; In Vitro Techniques; Kidney; Kinetics; Lipase; Lung; Male; Mercury; Methods; Microsomes; Microsomes, Liver; Myoglobin; NADP; Oxygen Consumption; Oxygenases; Phospholipases; Porphyrins; Rats; Spleen; Time Factors; Trypsin | 1969 |
Disulfiram impairment of drug metabolism by rat liver microsomes.
Topics: Adrenocorticotropic Hormone; Animals; Cytochromes; Disulfiram; Heme; Hexobarbital; In Vitro Techniques; Kinetics; Male; Microsomes, Liver; Morphinans; NADP; Oxidoreductases; Protein Binding; Rats; Sleep; Spectrum Analysis; Thiocarbamates | 1969 |
Haematin-dependent oxidative phosphorylation in Streptococcus faecalis.
Topics: Adenosine Triphosphate; Cytochromes; Enterococcus faecalis; Fructose; Glucose; Heme; Lactates; Manometry; NAD; NADP; Oxidative Phosphorylation; Oxygen Consumption; Spectrum Analysis | 1969 |
Purification of ctochrome b5-ike hemoprotein from anaerobically grown yeast.
Topics: Air; Carbon Monoxide; Culture Media; Cytochromes; Heme; Methods; NAD; NADP; Oxidation-Reduction; Pigments, Biological; Plant Proteins; Saccharomyces; Solubility; Spectrum Analysis; Trypsin | 1969 |
Reduced nicotinamide-adenine dinucleotide phosphate dependent biliverdin reductase: partial purification and characterization.
Topics: Animals; Benzoates; Bilirubin; Brain; Calcium Phosphates; Chemical Precipitation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Copper; Dextrans; Dialysis; Guinea Pigs; Heme; Humans; Kidney; Kinetics; Liver; Mercury; Methods; Muscles; NAD; NADP; Organ Specificity; Oxidoreductases; Oxygenases; Quaternary Ammonium Compounds; Rats; Serum Albumin; Solubility; Spectrophotometry; Spleen; Time Factors; Trypsin | 1970 |
Microsomal cytochromes b5 and P450 during induction of aryl hydrocarbon hydroxylase activity in mammalian cell culture.
Topics: Animals; Benz(a)Anthracenes; Carbon Monoxide; Cricetinae; Culture Techniques; Cycloheximide; Cytochromes; Depression, Chemical; Enzyme Activation; Enzyme Induction; Female; Fetus; Heme; Hydrocarbons; Liver; Maternal-Fetal Exchange; Microsomes; Microsomes, Liver; Mixed Function Oxygenases; NADP; Pigments, Biological; Pregnancy; Protein Biosynthesis; Rats; Spectrophotometry; Stimulation, Chemical; Time Factors | 1970 |
The enzymatic catabolism of hemoglobin: stimulation of microsomal heme oxygenase by hemin.
Topics: Adrenal Glands; Adrenalectomy; Anemia, Hemolytic; Animals; Bilirubin; Bone Marrow; Brain; Cytochromes; Female; Heme; Hemoglobins; Hemolysin Proteins; Kidney; Lung; Methemoglobin; Microsomes; Microsomes, Liver; NADP; Oxygen Consumption; Oxygenases; Phenylhydrazines; Prednisolone; Rats; Spleen; Splenectomy; Zymosan | 1970 |
Effect of 3-amino-1,2,4-triazole on the stimulation of hepatic microsomal heme synthesis and induction of hepatic microsomal oxidases produced by phenobarbital.
Topics: Animals; Azo Compounds; Carbon Isotopes; Cytochromes; Enzyme Induction; Heme; Hydro-Lyases; Iron Isotopes; Levulinic Acids; Male; Microsomes, Liver; Morphinans; NADP; Oxidoreductases; Phenobarbital; Rats; Time Factors; Triazoles | 1969 |
Phosphatidylcholine requirement in the enzymatic reduction of hemoprotein P-450 and in fatty acid, hydrocarbon, and drug hydroxylation.
Topics: Alkanes; Animals; Benzphetamine; Carbon Monoxide; Electron Transport; Fatty Acids; Heme; Kinetics; Microsomes, Liver; Morphinans; NADP; Oxidoreductases; Phosphatidylcholines; Rats; Spectrophotometry | 1970 |
Enzymatic omega-oxidation. IV. Purification and properties of the omega-hydroxylase of Pseudomonas oleovorans.
Topics: Alkanes; Chemical Phenomena; Chemistry; Chromatography; Cyanides; Cyclohexanes; Cytochromes; Detergents; Electron Spin Resonance Spectroscopy; Enzyme Induction; Fatty Acids; Ferredoxins; Flavin-Adenine Dinucleotide; Free Radicals; Glycerides; Heme; Iron; Mercaptoethanol; Microsomes, Liver; Mixed Function Oxygenases; Molecular Weight; NAD; NADP; Oxidoreductases; Oxygen; Pseudomonas; Quinolines; Spectrum Analysis | 1970 |
The enzymatic degradation of hemoglobin to bile pigments by macrophages.
Topics: Albumins; Animals; Bilirubin; Carbon Dioxide; Carbon Isotopes; Female; Heme; Hemoglobins; In Vitro Techniques; Kinetics; Macrophages; Microsomes; NADP; Oxygenases; Peritoneal Cavity; Pulmonary Alveoli; Rabbits; Rats; Spectrophotometry | 1971 |
Preparation and properties of a solubilized form of cytochrome P-450 from chick embryo liver microsomes.
Topics: Acetamides; Allyl Compounds; Animals; Bacillus subtilis; Carbon Monoxide; Cell Fractionation; Chick Embryo; Cytochromes; Depression, Chemical; Detergents; Etiocholanolone; Female; Flavins; Heme; Ketosteroids; Liver; Methods; Methylcholanthrene; Microsomes, Liver; NAD; NADP; Nitrogen; Oxidoreductases; Peptide Hydrolases; Phenobarbital; Pregnanes; Rats; Solubility; Spectrophotometry; Stimulation, Chemical | 1971 |
Inducible heme oxygenase in the kidney: a model for the homeostatic control of hemoglobin catabolism.
Topics: Adaptation, Physiological; Animals; Bilirubin; Bone Marrow; Cycloheximide; Dactinomycin; Disease Models, Animal; Enzyme Induction; Female; Heme; Hemoglobins; Hemoglobinuria; Homeostasis; Injections, Intravenous; Iron Isotopes; Kidney Tubules; Liver; NADP; Oxygenases; Protein Biosynthesis; Puromycin; Rats; RNA; Spleen | 1971 |
Spectroscopic studies of flavoproteins and non-haem iron proteins of submitochondrial particles of Torulopsis utilis modified by iron- and sulphate-limited growth in continuous culture.
Topics: Cycloheximide; Cytochromes; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavoproteins; Glycerolphosphate Dehydrogenase; Heme; Iron; Mitochondria; Mitosporic Fungi; NAD; NADP; Oxidation-Reduction; Oxidoreductases; Proteins; Spectrum Analysis; Succinate Dehydrogenase; Sulfates; Sulfides; Ubiquinone | 1971 |
Incorporation of radioactive- -aminolevulinic acid into microsomal cytochrome P 450 : selective breakdown of the hemoprotein by allylisopropylacetamide and carbon tetrachloride.
Topics: Acetamides; Allyl Compounds; Amides; Amino Acids; Animals; Carbon Monoxide; Carbon Tetrachloride; Cytochromes; Heme; Kinetics; Levulinic Acids; Male; Microsomes, Liver; NADP; Oxidoreductases; Protein Binding; Proteins; Rats; Spectrophotometry; Tritium | 1972 |
Method for microassay of microsomal heme oxygenase activity.
Topics: Amines; Animals; Bilirubin; Biopsy; Carbon Isotopes; Erythrocytes; Glycine; Heme; Humans; Kinetics; Levulinic Acids; Liver; Methods; Microchemistry; Microsomes; NADP; Needles; Oxidoreductases; Oxygenases; Rats; Spectrophotometry; Spleen; Tritium | 1972 |
Enzymatic degradation of heme. Oxygenative cleavage requiring cytochrome P-450.
Topics: Animals; Carbon Monoxide; Cytochromes; Heme; Light; Male; Mass Spectrometry; Microsomes; Microsomes, Liver; NADP; Oxidoreductases; Oxygen; Oxygen Isotopes; Oxygenases; Photochemistry; Radiation Effects; Rats; Spleen; Water | 1972 |
Studies on some aspects of peroxidase from submaxillary gland.
Topics: Animals; Apoproteins; Azides; Chromatography, Gel; Chromatography, Ion Exchange; Cyanides; Enzyme Activation; Flavin-Adenine Dinucleotide; Fluorides; Goats; Heme; Hydrogen-Ion Concentration; Iodoacetates; Kinetics; Molecular Weight; NAD; NADP; Peroxidases; Spectrophotometry; Submandibular Gland; Ultracentrifugation | 1972 |
[Decrease of cytochrome contents and changes in the kinetics of monooxygenase in liver microsomes of guinea pigs at various stages of L-ascorbic acid].
Topics: Acetanilides; Aminopyrine; Animals; Ascorbic Acid; Ascorbic Acid Deficiency; Cytochromes; Female; Guinea Pigs; Heme; Hydroxylation; Kinetics; Male; Microsomes, Liver; NADP; Oxidation-Reduction; Oxygenases | 1972 |
Degradation of haem compounds to bile pigments.
Topics: Aldehydes; Animals; Bile Pigments; Chemical Phenomena; Chemistry; Dicarboxylic Acids; Dogs; Heme; Hemoglobins; Isomerism; Kidney; Liver; Mice; Mononuclear Phagocyte System; NADP; Oxidation-Reduction; Oxidoreductases; Oxygenases; Pyrroles | 1972 |
Hemoprotein catabolism during stimulation of microsomal lipid peroxidation.
Topics: Adenosine Diphosphate; Animals; Blood Proteins; Chlorides; Cytochrome P-450 Enzyme System; Heme; In Vitro Techniques; Iron; Lipid Metabolism; Microsomes, Liver; NADP; Peroxides; Rats; Stimulation, Chemical | 1972 |
1,1,1-Trichloropropene-2,3-oxide: an alternate mechanism for its inhibition of cytochrome P-450.
Topics: Animals; Benzoflavones; beta-Naphthoflavone; Cytochrome P-450 Enzyme Inhibitors; Ethers; Heme; Hydrocarbons, Chlorinated; In Vitro Techniques; Male; Microsomes, Liver; Mixed Function Oxygenases; NADP; Phenobarbital; Rats; Trichloroepoxypropane | 1982 |
Formation of an iso-1-cytochrome c-like species containing a covalently bonded heme group from the apoprotein by a yeast cell-free system in the presence of hemin.
Topics: Apoproteins; Cell-Free System; Cytochrome c Group; Cytochromes c; Heme; Iodine Radioisotopes; NAD; NADP; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1980 |
Effect of carbon disulfide on superoxide anion production by rat liver microsomes.
Topics: Aniline Compounds; Animals; Carbon Disulfide; Cytochrome c Group; Heme; Male; Microsomes, Liver; NAD; NADP; Oxygen; Phenobarbital; Potassium Cyanide; Rats; Superoxides | 1981 |
A stoichiometric study of heme degradation catalyzed by the reconstituted heme oxygenase system with special consideration of the production of hydrogen peroxide during the reaction.
Topics: Animals; Biliverdine; Biotransformation; Catalase; Cattle; Chemical Phenomena; Chemistry; Cytochrome c Group; Heme; Heme Oxygenase (Decyclizing); Hemin; Horses; Hydrogen Peroxide; Mixed Function Oxygenases; NADP; Oxygen Consumption; Swine | 1983 |
The interactions of hydrazine derivatives with rat-hepatic cytochrome P-450.
Topics: Animals; Binding Sites; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Heme; Hydrazines; Imides; In Vitro Techniques; Microsomes, Liver; NADP; Oxidoreductases, N-Demethylating; Porphyrins; Protein Binding; Rats; Structure-Activity Relationship | 1984 |
Hydroperoxides as inactivators of aromatase: 10 beta-hydroperoxy-4-estrene-3,17-dione, crystal structure and inactivation characteristics.
Topics: Androstenedione; Aromatase Inhibitors; Benzene Derivatives; Binding, Competitive; Chemical Phenomena; Chemistry; Estrenes; Female; Heme; Humans; Hydrogen Peroxide; Kinetics; Microsomes; NADP; Oxidoreductases; Placenta; Pregnancy; X-Ray Diffraction | 1984 |
Oxidation of monosubstituted olefins by cytochromes P-450 and heme models: evidence for the formation of aldehydes in addition to epoxides and allylic alcohols.
Topics: 1-Propanol; Aldehydes; Alkenes; Animals; Cytochrome P-450 Enzyme System; Epoxy Compounds; Heme; Iodobenzenes; Male; Microsomes, Liver; NADP; Oxidation-Reduction; Phenyl Ethers; Propanols; Rats; Rats, Inbred Strains; Styrene; Styrenes | 1984 |
Inhibition of delta-aminolevulinate dehydratase in trichloroethylene-exposed rats, and the effects on heme regulation.
Topics: Animals; Bone Marrow; Cytochrome P-450 Enzyme System; Dithiothreitol; Erythrocytes; Heme; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kinetics; Liver; Male; NADP; Porphobilinogen Synthase; Rats; Rats, Inbred Strains; Trichloroethylene; Tryptophan Oxygenase | 1984 |
The effect in vivo and in vitro of allylisopropylacetamide on the content of hepatic microsomal cytochrome P-450 2 of phenobarbital treated rabbits.
Topics: Acetamides; Allylisopropylacetamide; Animals; Chemical Phenomena; Chemistry; Cytochrome P-450 Enzyme System; Heme; In Vitro Techniques; Microsomes, Liver; NADP; Phenobarbital; Rabbits | 1983 |
Vinylidene chloride: its metabolism by hepatic microsomal cytochrome P-450 in vitro.
Topics: Animals; Biotransformation; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Dichloroethylenes; Enzyme Induction; Heme; Hydrocarbons, Chlorinated; Hydrogen Peroxide; In Vitro Techniques; Kinetics; Male; Microsomes, Liver; NADP; Protein Binding; Rats | 1982 |
Hemin-mediated para-hydroxylation of aniline: a potential model for oxygen activation and insertion reactions of mixed function oxidases.
Topics: Aniline Compounds; Animals; Cattle; Cytochrome P-450 Enzyme System; Erythrocytes; Heme; Hemin; Hydrogen-Ion Concentration; Kinetics; Mixed Function Oxygenases; NAD; NADP; Oxidation-Reduction; Oxidoreductases; Oxygen Consumption; Superoxide Dismutase; Thermodynamics | 1982 |
H2O2-and alkyl hydroperoxide-supported para hydroxylation of aniline by alkaline hematin.
Topics: Aniline Compounds; Cytochrome P-450 Enzyme System; Heme; Hemeproteins; Hydrogen Peroxide; Hydroxylation; Kinetics; Models, Biological; NAD; NADP; Oxidation-Reduction; Peroxides | 1982 |
Inactivation of hepatic cytochrome P-450 by allenic substrates.
Topics: Alkadienes; Animals; Cytochrome P-450 Enzyme Inhibitors; Enzyme Induction; Heme; Male; Methylcholanthrene; Microsomes, Liver; NADP; Phenobarbital; Protein Binding; Rats | 1980 |
Microsomal NADPH-dependent lipid peroxidation does not require the presence of intact cytochrome P450.
Topics: Allylisopropylacetamide; Animals; Cytochrome P-450 Enzyme System; Heme; In Vitro Techniques; Lipid Peroxides; Male; Malondialdehyde; Methylcholanthrene; Microsomes, Liver; NADP; Phenobarbital; Pregnenolone Carbonitrile; Rats | 1980 |
Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer.
Topics: Amino Acid Oxidoreductases; Arginine; Calcium; Calmodulin; Enzyme Activation; Heme; Macrophages; NADP; Neurons; Nitric Oxide Synthase; Oxidation-Reduction; Recombinant Proteins | 1993 |
Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group. Role of tetrahydrobiopterin in modulating the inhibitory action of nitric oxide.
Topics: Amino Acid Oxidoreductases; Animals; Arginine; Biopterins; Carbon Monoxide; Cerebellum; Citrulline; Cyanides; Heme; NADP; Neurons; Nitric Oxide; Nitric Oxide Synthase; Oxidants; Oxyhemoglobins; Rats; Sulfhydryl Compounds; Superoxide Dismutase | 1994 |
Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer.
Topics: Amino Acid Oxidoreductases; Animals; Biopterins; Calmodulin; Catalysis; Cells, Cultured; Electron Transport; Flavins; Heme; Humans; NADP; Neurons; Nitric Oxide Synthase; Oxidation-Reduction; Rats | 1994 |
Electron transfer in the nitric-oxide synthases. Characterization of L-arginine analogs that block heme iron reduction.
Topics: Amino Acid Oxidoreductases; Animals; Arginine; Biological Transport; Cells, Cultured; Citrulline; Cloning, Molecular; Electrons; Heme; Humans; Iron; Kinetics; NADP; Neurons; NG-Nitroarginine Methyl Ester; Nitric Oxide Synthase; omega-N-Methylarginine; Oxidation-Reduction; Rats; Thiourea | 1994 |
Multiple catalytic functions of brain nitric oxide synthase. Biochemical characterization, cofactor-requirement, and the role of N omega-hydroxy-L-arginine as an intermediate.
Topics: Amino Acid Oxidoreductases; Animals; Arginine; Biopterins; Brain; Catalysis; Coenzymes; Heme; Hydrolysis; Kinetics; NADP; Nitric Oxide Synthase; Oxidation-Reduction; Substrate Specificity; Swine | 1993 |
Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme.
Topics: Amino Acid Oxidoreductases; Animals; Biopterins; Catalysis; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Macrophages; Mice; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxidoreductases; Substrate Specificity | 1993 |
Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein.
Topics: Amino Acid Sequence; Base Sequence; Catalysis; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Gene Expression; Genes, Bacterial; Heme; Magnetic Resonance Spectroscopy; Methylation; Methyltransferases; Molecular Sequence Data; NADP; Recombinant Proteins; S-Adenosylmethionine; Uroporphyrinogens; Uroporphyrins | 1994 |
Flavin supported fatty acid oxidation by the heme domain of Bacillus megaterium cytochrome P450BM-3.
Topics: Bacillus megaterium; Bacterial Proteins; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Heme; Mixed Function Oxygenases; Myristic Acid; Myristic Acids; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Radioisotope Dilution Technique; Spectrophotometry | 1994 |
Interactions of dihydralazine with cytochromes P4501A: a possible explanation for the appearance of anti-cytochrome P4501A2 autoantibodies.
Topics: Animals; Arylamine N-Acetyltransferase; Autoantibodies; Binding Sites; Biotransformation; Blotting, Western; Carbon Monoxide; Cytochrome P-450 Enzyme System; Dihydralazine; Heme; Iron; Isoenzymes; Light; Male; Microsomes, Liver; NADP; Rats; Rats, Sprague-Dawley | 1994 |
Mutagenesis at a highly conserved phenylalanine in cytochrome P450 2E1 affects heme incorporation and catalytic activity.
Topics: Amino Acid Sequence; Animals; Catalysis; Conserved Sequence; Cytochrome P-450 CYP2E1; Cytochrome P-450 Enzyme System; Escherichia coli; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; Oxidoreductases, N-Demethylating; Phenylalanine; Rabbits; Structure-Activity Relationship | 1994 |
Inactivation of phenobarbital-inducible rabbit-liver microsomal cytochrome P-450 by allylisopropylacetamide: impact on electron transfer.
Topics: Allylisopropylacetamide; Amino Acids; Animals; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Cytochromes b5; Electron Transport; Enzyme Induction; Heme; Microsomes, Liver; NAD; NADP; Phenobarbital; Proteins; Rabbits | 1993 |
Studies on the interaction of furan with hepatic cytochrome P-450.
Topics: Animals; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Furans; Heme; In Vitro Techniques; Liver; Male; Microsomes, Liver; Mixed Function Oxygenases; NADP; Proteins; Rats; Rats, Inbred F344 | 1993 |
Inducible nitric oxide synthase: identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin.
Topics: Amino Acid Sequence; Animals; Binding Sites; Biopterins; Calmodulin; Conserved Sequence; Heme; Mice; Molecular Sequence Data; Mutagenesis; NADP; Nitric Oxide Synthase; Polymerase Chain Reaction; Protein Binding; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid; Structure-Activity Relationship | 1995 |
Aerobic and anaerobic functioning of superoxide-producing cytochrome b-559 reconstituted with phospholipids.
Topics: Aerobiosis; Anaerobiosis; Animals; Cytochrome b Group; Cytochromes; Electron Transport; Flavin-Adenine Dinucleotide; Guinea Pigs; Heme; Kinetics; Macrophages, Peritoneal; NADH, NADPH Oxidoreductases; NADP; NADPH Oxidases; Oxygen; Phospholipids; Photosystem II Protein Complex; Respiratory Burst; Superoxides | 1995 |
Heme iron reduction and catalysis by a nitric oxide synthase heterodimer containing one reductase and two oxygenase domains.
Topics: Animals; Binding Sites; Calmodulin; Catalysis; Cell Line; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Iron; Kinetics; Macromolecular Substances; Macrophages; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxidoreductases; Oxygenases; Spectrophotometry | 1996 |
Probing electron transfer in flavocytochrome P-450 BM3 and its component domains.
Topics: Bacillus megaterium; Bacterial Proteins; Binding Sites; Cloning, Molecular; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Peptide Fragments; Quinones; Recombinant Proteins; Restriction Mapping | 1996 |
Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy.
Topics: Binding Sites; Catalase; Catalysis; Crystallography, X-Ray; Heme; Iron; Microspectrophotometry; Models, Molecular; NADP; Proteus mirabilis | 1996 |
Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain.
Topics: Bacterial Proteins; Carbon Monoxide; Catalysis; Cytochrome c Group; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Electron Transport; Escherichia coli; Fatty Acids; Flavoproteins; Heme; Hydroxylation; Lauric Acids; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Binding; Spectrometry, Fluorescence | 1996 |
Nitric oxide binding to the heme of neuronal nitric-oxide synthase links its activity to changes in oxygen tension.
Topics: Calmodulin; Computer Simulation; Ferric Compounds; Heme; NADP; Neurons; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxygen; Superoxides | 1996 |
Mutation of Glu-361 in human endothelial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers.
Topics: Amino Acid Sequence; Arginine; Binding Sites; Electron Spin Resonance Spectroscopy; Endothelium, Vascular; Glutamates; Heme; Hemeproteins; Humans; Molecular Sequence Data; Molecular Weight; NADP; Nitric Oxide Synthase; Oxidation-Reduction; Structure-Activity Relationship | 1997 |
Thiols and neuronal nitric oxide synthase: complex formation, competitive inhibition, and enzyme stabilization.
Topics: Animals; Arginine; Biopterins; Calmodulin; Cysteine; Dithiothreitol; Enzyme Inhibitors; Enzyme Stability; Flavin-Adenine Dinucleotide; Heme; Mercaptoethanol; NADP; Neurons; Nitric Oxide Synthase; Protein Binding; Rats; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Compounds; Temperature | 1997 |
Reductive activation of 1,1-dichloro-1-fluoroethane (HCFC-141b) by phenobarbital- and pyridine-induced rat liver microsomal cytochrome P450.
Topics: Alkenes; Anaerobiosis; Animals; Biotransformation; Carbon Monoxide; Chlorofluorocarbons; Chlorofluorocarbons, Ethane; Cyclic N-Oxides; Cytochrome P-450 CYP2B1; Cytochrome P-450 CYP2E1; Cytochrome P-450 Enzyme System; Glutathione; Heme; Male; Microsomes, Liver; NADP; Nitrogen Oxides; Oxidation-Reduction; Phenobarbital; Pyridines; Rats; Rats, Wistar | 1996 |
Neuronal nitric-oxide synthase interaction with calmodulin-troponin C chimeras.
Topics: Amino Acid Sequence; Animals; Brain; Calmodulin; Cytochrome c Group; Electron Transport; Enzyme Activation; Flavoproteins; Heme; Kinetics; Molecular Sequence Data; NADP; Neurons; Nitric Oxide; Nitric Oxide Synthase; Rats; Recombinant Fusion Proteins; Sequence Alignment; Troponin C | 1998 |
Effects of pH on the structure and function of neuronal nitric oxide synthase.
Topics: Animals; Arginine; Biopterins; Brain; Citrulline; Dimerization; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; NADP; Nerve Tissue Proteins; Nitric Oxide Synthase; Protein Binding; Protein Conformation; Rats; Spectrophotometry | 1998 |
Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer.
Topics: Arginine; Binding Sites; Catalysis; Dimerization; Electron Transport; Escherichia coli; Flavins; Heme; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Oxidation-Reduction; Point Mutation; Protein Conformation; Spectrophotometry, Atomic; Spectrum Analysis, Raman | 1998 |
Conversion of mitochondrial cytochrome b5 into a species capable of performing the efficient coupled oxidation of heme.
Topics: Cytochromes b5; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Histidine; Magnetic Resonance Spectroscopy; Mass Spectrometry; Methionine; Mitochondria; Mutagenesis, Site-Directed; NADP; Oxidation-Reduction | 1998 |
Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3.
Topics: Arachidonic Acid; Bacterial Proteins; Binding Sites; Catalysis; Circular Dichroism; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Enzyme Inhibitors; Fatty Acids; Heme; Imidazoles; Kinetics; Lauric Acids; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Substrate Specificity | 1998 |
The C331A mutant of neuronal nitric-oxide synthase is defective in arginine binding.
Topics: Animals; Arginine; Biopterins; Calmodulin; Carbon Monoxide; Catalytic Domain; Conserved Sequence; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Mutation; NADP; Neurons; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Rats; Recombinant Proteins; Spectrophotometry; Structure-Activity Relationship | 1998 |
Quinone-dependent tertiary amine N-oxide reduction in rat blood.
Topics: Animals; Antidepressive Agents, Tricyclic; Heme; Imipramine; In Vitro Techniques; Liver; Male; NAD(P)H Dehydrogenase (Quinone); NADP; Oxidation-Reduction; Rats; Rats, Wistar; Time Factors | 1998 |
Mechanism-based inactivation of cytochrome P-450-3A4 by mifepristone (RU486).
Topics: Abortifacient Agents, Steroidal; Animals; Apoenzymes; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Heme; Humans; Kinetics; Male; Mifepristone; Mixed Function Oxygenases; NADP; Rats; Rats, Inbred F344; Sodium Dodecyl Sulfate; Spectrum Analysis; Testosterone | 1999 |
Structure of catalase-A from Saccharomyces cerevisiae.
Topics: Alanine; Binding Sites; Catalase; Crystallography, X-Ray; Heme; Models, Molecular; Mutagenesis, Site-Directed; NADP; Protein Conformation; Saccharomyces cerevisiae; Valine | 1999 |
Structure of catalase HPII from Escherichia coli at 1.9 A resolution.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalase; Crystallography, X-Ray; Escherichia coli; Heme; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; NADP; Protein Conformation; Water | 1999 |
Carbon monoxide stimulates the apical 70-pS K+ channel of the rat thick ascending limb.
Topics: Animals; Biliverdine; Carbon Monoxide; Enzyme Inhibitors; Female; Gene Expression Regulation, Enzymologic; Heme; Heme Oxygenase (Decyclizing); Kidney; Lysine; Male; NADP; Patch-Clamp Techniques; Porphyrins; Potassium Channels; Rats; Rats, Sprague-Dawley; RNA | 1999 |
Simultaneous presence of p47(phox) and flavocytochrome b-245 are required for the activation of NADPH oxidase by anionic amphiphiles. Evidence for an intermediate state of oxidase activation.
Topics: Anions; Arachidonic Acid; Cytochrome b Group; Electron Transport; Enzyme Activation; Flavins; Flavoproteins; Heme; Kinetics; NADH, NADPH Oxidoreductases; NADP; NADPH Oxidases; Phosphoproteins; Sodium Dodecyl Sulfate; Superoxides; Surface-Active Agents; Tetrazolium Salts | 1999 |
Characterization of mouse nNOS2, a natural variant of neuronal nitric-oxide synthase produced in the central nervous system by selective alternative splicing.
Topics: Alternative Splicing; Amino Acid Sequence; Animals; Central Nervous System; Heme; Mice; Models, Molecular; Molecular Sequence Data; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Recombinant Proteins; Sequence Alignment; Sequence Deletion; Spectrophotometry, Ultraviolet | 1999 |
Inactivation of cytochrome P450 2E1 by benzyl isothiocyanate.
Topics: Cytochrome P-450 CYP2E1; Cytochromes b5; Enzyme Inhibitors; Heme; Isothiocyanates; Kinetics; NADP; Protein Binding | 1999 |
Reaction of neuronal nitric oxide synthase with the nitric oxide spin-trapping agent, iron complexed with N-dithiocarboxysarcosine.
Topics: Animals; Arginine; Citrulline; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Inhibitors; Ferric Compounds; Heme; In Vitro Techniques; Iron; Mice; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxygen Consumption; Spin Labels; Swine; Thiocarbamates | 1999 |
Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Binding Sites; Conserved Sequence; Heme; Hordeum; Models, Molecular; Molecular Sequence Data; NADP; Protein Folding; Protein Structure, Secondary; Sequence Homology, Amino Acid | 1999 |
NADPH and heme redox modulate pulmonary artery relaxation and guanylate cyclase activation by NO.
Topics: Animals; Cattle; Colforsin; Cyclic GMP; Electron Transport; Enzyme Activation; Enzyme Inhibitors; Ferricyanides; Flavoproteins; Glutathione; Guanylate Cyclase; Heme; In Vitro Techniques; NADH, NADPH Oxidoreductases; NADP; Nitric Oxide; Oxadiazoles; Oxidation-Reduction; Penicillamine; Pentose Phosphate Pathway; Pulmonary Artery; Quinoxalines; Reactive Oxygen Species; Sulfhydryl Compounds | 1999 |
Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B).
Topics: Aerobiosis; Biliverdine; Flavins; FMN Reductase; Heme; Humans; Kinetics; Models, Chemical; NADH, NADPH Oxidoreductases; NADP; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Stereoisomerism; Substrate Specificity | 2000 |
Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.
Topics: Amino Acid Sequence; Amitrole; Binding Sites; Catalase; Catalysis; Crystallization; Crystallography, X-Ray; Cyanides; Electrons; Enzyme Inhibitors; Heme; Humans; Hydrogen Bonding; Hydrogen Peroxide; Models, Chemical; Models, Molecular; Molecular Sequence Data; NADP; Protein Conformation; Substrate Specificity; Tyrosine; Water | 2000 |
Nitric oxide-induced autoinhibition of neuronal nitric oxide synthase in the presence of the autoxidation-resistant pteridine 5-methyltetrahydrobiopterin.
Topics: Animals; Arginine; Biopterins; Catalase; Catalysis; Cattle; Citrulline; Dimerization; Free Radical Scavengers; Guanylate Cyclase; Heme; Hydrogen Peroxide; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidants; Pteridines; Rats; Superoxide Dismutase; Superoxides | 2000 |
Electron transfer, oxygen binding, and nitric oxide feedback inhibition in endothelial nitric-oxide synthase.
Topics: Animals; Calmodulin; Cattle; Cloning, Molecular; Electron Transport; Escherichia coli; Feedback; Heme; Kinetics; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Oxygen; Protein Binding; Recombinant Proteins; Spectrophotometry; Substrate Specificity | 2000 |
Aromatic residues and neighboring Arg414 in the (6R)-5,6,7, 8-tetrahydro-L-biopterin binding site of full-length neuronal nitric-oxide synthase are crucial in catalysis and heme reduction with NADPH.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Binding Sites; Biopterins; Catalysis; Dimerization; Drosophila; Glutamine; Heme; Humans; Hydrogen Bonding; Leucine; Mice; Models, Molecular; Molecular Sequence Data; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Rats; Spectrophotometry, Atomic; Structure-Activity Relationship; Tryptophan | 2000 |
Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism.
Topics: Arginine; Biopterins; Catalysis; Citrulline; Heme; Hydrogen Peroxide; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction | 2000 |
A kinetic simulation model that describes catalysis and regulation in nitric-oxide synthase.
Topics: Amino Acid Substitution; Binding Sites; Catalysis; Citrulline; Cloning, Molecular; Escherichia coli; Heme; Kinetics; Models, Chemical; Models, Theoretical; Mutagenesis, Site-Directed; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Recombinant Proteins | 2001 |
Heme oxygenase activity in term human placenta.
Topics: Amnion; Carbon Monoxide; Chorion; Chorionic Villi; Decidua; Female; Heme; Heme Oxygenase (Decyclizing); Humans; Microsomes; NADP; Placenta; Pregnancy | 2000 |
Crystal structure of rat biliverdin reductase.
Topics: Amino Acid Sequence; Animals; Biliverdine; Binding Sites; Crystallography, X-Ray; Heme; Kinetics; Models, Molecular; Molecular Sequence Data; NAD; NADP; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Protein Structure, Tertiary; Rats; Sequence Alignment; Zinc | 2001 |
Chimeras of nitric-oxide synthase types I and III establish fundamental correlates between heme reduction, heme-NO complex formation, and catalytic activity.
Topics: Animals; Catalysis; Catalytic Domain; Flavins; Heme; Kinetics; Macromolecular Substances; Models, Chemical; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type III; Oxidation-Reduction; Recombinant Fusion Proteins | 2001 |
Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer.
Topics: Animals; Arginine; Calmodulin; Dimerization; Electron Transport; Escherichia coli; Heme; Iron; Models, Biological; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Point Mutation; Protein Subunits; Rats; Transfection | 2001 |
Non-enzymatic reduction of aliphatic tertiary amine N-oxides mediated by the haem moiety of cytochrome P450.
Topics: Amines; Animals; Catalysis; Cyclic N-Oxides; Cytochrome P-450 Enzyme System; Flavins; Heme; Imipramine; In Vitro Techniques; Male; Microsomes, Liver; NADP; Niacinamide; Oxidation-Reduction; Oxidoreductases; Rats; Rats, Sprague-Dawley; Strychnine | 2001 |
Spectral studies of tert-butyl isothiocyanate-inactivated P450 2E1.
Topics: Animals; Binding Sites; Carbon Monoxide; Chromatography, Liquid; Cytochrome P-450 CYP2E1; Cytochrome P-450 CYP2E1 Inhibitors; Dithionite; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Inhibitors; Fomepizole; Heme; Iodobenzenes; Isothiocyanates; NADP; Pyrazoles; Rabbits; Rats; Spectrometry, Mass, Electrospray Ionization | 2001 |
Differences in three kinetic parameters underpin the unique catalytic profiles of nitric-oxide synthases I, II, and III.
Topics: Heme; Kinetics; Models, Chemical; NADP; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Nitric Oxide Synthase Type III; Oxidation-Reduction | 2001 |
Critical role of the neuronal nitric-oxide synthase heme proximal side residue, Arg418, in catalysis and electron transfer.
Topics: Amino Acid Sequence; Animals; Arginine; Binding Sites; Catalysis; Electron Transport; Heme; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Rats; Spectrophotometry | 2001 |
Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans.
Topics: Amino Acid Sequence; Animals; Arginine; Biopterins; Catalysis; Citrulline; Cloning, Molecular; Dimerization; Dithiothreitol; Dose-Response Relationship, Drug; Electrons; Heme; Hydrogen Peroxide; Kinetics; Ligands; Models, Chemical; Models, Molecular; Molecular Sequence Data; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Thermus; Time Factors; Zinc | 2002 |
Altered etioplast development in phytochrome chromophore-deficient mutants.
Topics: Arabidopsis; Darkness; Heme; Hypocotyl; Microscopy, Electron; Mutation; NADP; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Phytochrome; Pisum sativum; Plants, Genetically Modified; Plastids; Protochlorophyllide; Pyrroles; Signal Transduction; Solanum lycopersicum; Tetrapyrroles | 2001 |
Perferryl complex of nitric oxide synthase: role in secondary free radical formation.
Topics: Arginine; Binding Sites; Carbon Radioisotopes; Citrulline; Electron Spin Resonance Spectroscopy; Ethanol; Free Radicals; Heme; Humans; Iron; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Potassium Compounds; Recombinant Proteins; Sodium Cyanide; Spin Trapping; Sulfates | 2002 |
Interactions between the isolated oxygenase and reductase domains of neuronal nitric-oxide synthase: assessing the role of calmodulin.
Topics: Animals; Binding Sites; Calmodulin; Catalysis; Cytochrome c Group; DNA, Complementary; Heme; Kinetics; NADP; NADPH-Ferrihemoprotein Reductase; Neurons; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidoreductases; Oxygen; Oxygenases; Plasmids; Protein Binding; Protein Structure, Tertiary; Rats; Spectrometry, Fluorescence; Time Factors | 2002 |
Mechanism-based inactivation of cytochrome P450 3A4 by 17 alpha-ethynylestradiol: evidence for heme destruction and covalent binding to protein.
Topics: Apoproteins; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Escherichia coli; Ethinyl Estradiol; Gas Chromatography-Mass Spectrometry; Heme; Mixed Function Oxygenases; NADP; Oxidation-Reduction; Protein Binding; Solubility; Spectrometry, Mass, Electrospray Ionization | 2002 |
NPAS2: a gas-responsive transcription factor.
Topics: Animals; ARNTL Transcription Factors; Basic Helix-Loop-Helix Transcription Factors; Carbon Monoxide; Circadian Rhythm; Dimerization; DNA; Helix-Loop-Helix Motifs; Heme; Ligands; Myoglobin; NADP; Nerve Tissue Proteins; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Spectrophotometry, Ultraviolet; Transcription Factors | 2002 |
Mechanism-based inactivation of cytochromes P450 2E1 and 2E1 T303A by tert-butyl acetylenes: characterization of reactive intermediate adducts to the heme and apoprotein.
Topics: Acetylene; Alkylation; Amino Acid Substitution; Animals; Apoproteins; Carbon Monoxide; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP2E1; Cytochrome P-450 CYP2E1 Inhibitors; Dose-Response Relationship, Drug; Enzyme Activation; Enzyme Inhibitors; Heme; Hydroxylation; Kinetics; NADP; Rabbits; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Substrate Specificity | 2002 |
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.
Topics: Acetates; Anions; Arginine; Binding Sites; Catalase; Catalysis; Crystallography, X-Ray; Heme; Hydrogen Bonding; Iron; Models, Molecular; NADP; Protein Conformation; Proteus mirabilis; Protoporphyrins; Recombinant Proteins; Spectrum Analysis; Sulfates | 2003 |
Circadian rhythms. Carbon monoxide and clocks.
Topics: Animals; ARNTL Transcription Factors; Autonomic Nervous System; Basic Helix-Loop-Helix Transcription Factors; Behavior, Animal; Brain; Carbon Monoxide; Circadian Rhythm; CLOCK Proteins; Diffusion; Dimerization; DNA; Helix-Loop-Helix Motifs; Heme; Heme Oxygenase (Decyclizing); Mice; Models, Genetic; NAD; NADP; Nerve Tissue Proteins; Neurons; Neurotransmitter Agents; Oxidation-Reduction; Protein Structure, Tertiary; Synaptic Transmission; Trans-Activators; Transcription Factors; Transcription, Genetic | 2002 |
Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution.
Topics: Binding Sites; Catalase; Heme; Models, Molecular; Molecular Weight; NADP; Nuclear Magnetic Resonance, Biomolecular; Protein Subunits; Pseudomonas; Sensitivity and Specificity; Solvents; Water | 2003 |
Characterization of Drosophila nitric oxide synthase: a biochemical study.
Topics: Animals; Arginine; Biopterins; Dose-Response Relationship, Drug; Drosophila; Electrons; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Hydrogen Peroxide; Hydrolysis; NADP; Nitrates; Nitric Oxide; Nitric Oxide Synthase; Nitrites; Open Reading Frames; Protein Structure, Tertiary; Spectrophotometry; Time Factors; Trypsin; Ultraviolet Rays; Urea | 2003 |
STUDIES ON HEME ALPHA-METHENYL OXYGENASE. I. THE ENZYMATIC CONVERSION OF PYRIDINE-HEMICHROMOGEN AND HEMOGLOBIN-HAPTOGLOBIN INTO A POSSIBLE PRECURSOR OF BILIVERDIN.
Topics: Animals; Bile Pigments; Biliverdine; Cattle; Chelating Agents; Chromatography; Guinea Pigs; Haptoglobins; Heme; Heme Oxygenase (Decyclizing); Hemoglobins; Liver; NADP; Oxygenases; Polarography; Pyridines; Research; Spectrophotometry; Sulfhydryl Compounds | 1963 |
A COMPARATIVE STUDY OF ELECTRON TRANSPORT IN MICROSOMES.
Topics: Adipose Tissue; Adrenal Glands; Animals; Brain; Cell Biology; Cytochromes; Electron Transport; Electron Transport Complex IV; Flavins; Gonads; Heme; Kidney; Lipids; Liver; Lung; Metabolism; Microsomes; Mucous Membrane; Muscles; NAD; NADP; Pancreas; Research; Spleen; Thymus Gland; Vertebrates | 1963 |
Mechanism-based inhibition of CYP activities in rat liver by fluoxetine and structurally similar alkylamines.
Topics: Adrenergic Uptake Inhibitors; Amines; Animals; Aryl Hydrocarbon Hydroxylases; Binding Sites; Cytochrome P450 Family 2; Desipramine; Diffusion; Dose-Response Relationship, Drug; Enzyme Inhibitors; Fluoxetine; Heme; Hydroxylation; Inhibitory Concentration 50; Kinetics; Liver; Male; Microsomes, Liver; Models, Chemical; NADP; Nortriptyline; Oxygen; Protein Binding; Rats; Rats, Wistar; Selective Serotonin Reuptake Inhibitors; Steroid 16-alpha-Hydroxylase; Steroids; Time Factors | 2003 |
A conserved aspartate (Asp-1393) regulates NADPH reduction of neuronal nitric-oxide synthase: implications for catalysis.
Topics: Amino Acid Substitution; Animals; Aspartic Acid; Catalysis; Conserved Sequence; Electron Transport; Flavins; Heme; Kinetics; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Binding; Rats; Spectrometry, Fluorescence | 2004 |
Conversion of the 2,2,6,6-tetramethylpiperidine moiety to a 2,2-dimethylpyrrolidine by cytochrome P450: evidence for a mechanism involving nitroxide radicals and heme iron.
Topics: Aerobiosis; Anaerobiosis; Carbon Monoxide; Cyclic N-Oxides; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Deferoxamine; Free Radicals; Heme; Hemin; Humans; Iron; Iron Chelating Agents; Microsomes, Liver; NADP; Nitrogen Oxides; Oxygen Isotopes; Piperidones; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Triacetoneamine-N-Oxyl | 2004 |
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Topics: Bacillus megaterium; Bacillus subtilis; Bacterial Proteins; Carbon Monoxide; Cloning, Molecular; Coenzymes; Cytochrome P-450 Enzyme System; Fatty Acids; Flavoproteins; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Heme; Hydroxylation; Kinetics; Mixed Function Oxygenases; Myristic Acid; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Binding; Sequence Alignment; Sequence Homology, Amino Acid; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2004 |
Silybin inactivates cytochromes P450 3A4 and 2C9 and inhibits major hepatic glucuronosyltransferases.
Topics: Aryl Hydrocarbon Hydroxylases; Cytochrome P-450 CYP2C9; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Glucuronosyltransferase; Heme; Kinetics; NADP; Plant Extracts; Recombinant Proteins; Silybin; Silymarin; Testosterone | 2004 |
Characterization of the peroxidase system at low H2O2 concentrations in isolated neonatal rat islets.
Topics: Animals; Animals, Newborn; Catalase; Catalytic Domain; Cell Nucleus; Cells, Cultured; Copper; Cytoplasm; Dose-Response Relationship, Drug; Heme; Hydrogen Peroxide; Ions; Iron; Islets of Langerhans; Kinetics; Magnesium; Models, Chemical; NADP; Oxidation-Reduction; Oxidative Stress; Oxygen; Peroxidase; Rats; Sulfhydryl Compounds; Superoxides; Time Factors | 2004 |
Regiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant.
Topics: Ascorbic Acid; Biliverdine; Binding Sites; Catalysis; Chromatography, High Pressure Liquid; Crystallography, X-Ray; Electrons; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen Bonding; Models, Chemical; Mutation; NADP; Oxygen; Protein Binding; Protein Conformation; Spectrophotometry; Superoxide Dismutase; Ultraviolet Rays | 2005 |
Consumption of nitric oxide by endothelial cells: evidence for the involvement of a NAD(P)H-, flavin- and heme-dependent dioxygenase reaction.
Topics: Animals; Dioxygenases; Endothelium, Vascular; Flavins; Heme; NADP; Nitric Oxide; Subcellular Fractions; Swine | 2004 |
Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.
Topics: Aspartic Acid; Binding Sites; Catalysis; Corynebacterium diphtheriae; Crystallography, X-Ray; Escherichia coli; Heme; Heme Oxygenase (Decyclizing); Hydrogen Peroxide; Iron; Models, Chemical; Mutagenesis, Site-Directed; Mutation; NADP; NADPH-Ferrihemoprotein Reductase; Oxygen; Plasmids; Spectrophotometry; Spectrum Analysis, Raman; Ultraviolet Rays; Water | 2005 |
Hemoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel.
Topics: Animals; Carbon Monoxide; Carotid Body; Cell Hypoxia; Cell Line; Heme; Heme Oxygenase (Decyclizing); Humans; Immunoprecipitation; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits; Large-Conductance Calcium-Activated Potassium Channels; Membrane Potentials; NADP; Oxygen; Patch-Clamp Techniques; Potassium Channels, Calcium-Activated; Rats; RNA Interference; RNA, Small Interfering; Transfection | 2004 |
Cell biology. Oxygen sensing: it's a gas!
Topics: Animals; Carbon Monoxide; Carotid Body; Cell Hypoxia; Cell Membrane; Cells, Cultured; Heme; Heme Oxygenase (Decyclizing); Hemeproteins; Large-Conductance Calcium-Activated Potassium Channels; Membrane Potentials; Mitochondria; NADP; NADPH Oxidases; Oxidation-Reduction; Oxygen; Potassium Channels, Calcium-Activated; Proteomics; RNA, Small Interfering; Signal Transduction | 2004 |
Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase. Properties of the heme and enzyme complex.
Topics: Amino Acid Sequence; Ascorbic Acid; Bacterial Proteins; Biliverdine; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Hemin; Hydrogen Peroxide; Molecular Sequence Data; NADP; Sequence Alignment; Spectrophotometry; Synechocystis | 2005 |
A tryptophan that modulates tetrahydrobiopterin-dependent electron transfer in nitric oxide synthase regulates enzyme catalysis by additional mechanisms.
Topics: Animals; Arginine; Biopterins; Catalysis; Dimerization; Electron Transport; Enzyme Stability; Ferrous Compounds; Heme; Hydroxylation; Isoenzymes; Kinetics; Mice; Mutagenesis, Site-Directed; NADP; Nerve Tissue Proteins; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Binding; Rats; Spectrophotometry; Tryptophan | 2005 |
C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Base Sequence; Calmodulin; DNA, Complementary; Electron Transport; Heme; Humans; In Vitro Techniques; Kinetics; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Conformation; Protein Structure, Tertiary; Rats; Recombinant Proteins; Sequence Homology, Amino Acid | 2005 |
Inactivation of CYP2A6 and CYP2A13 during nicotine metabolism.
Topics: Animals; Aryl Hydrocarbon Hydroxylases; Carbon Monoxide; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP2A6; Escherichia coli; Half-Life; Heme; Humans; Kinetics; Mixed Function Oxygenases; NADP; Nicotine; Nicotinic Agonists; Rats; Substrate Specificity | 2006 |
Direct measurement by laser flash photolysis of intramolecular electron transfer in a two-domain construct of murine inducible nitric oxide synthase.
Topics: Animals; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Mice; NADP; Nitric Oxide Synthase Type II; Oxidation-Reduction; Photolysis; Protein Structure, Tertiary | 2006 |
Visible spectra of type II cytochrome P450-drug complexes: evidence that "incomplete" heme coordination is common.
Topics: Aniline Compounds; Aryl Hydrocarbon Hydroxylases; Benzodioxoles; Binding Sites; Cytochrome P-450 CYP2C9; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Enzyme Inhibitors; Fluconazole; Heme; Humans; Imidazoles; Itraconazole; Kinetics; Ligands; Light; Models, Chemical; Molecular Structure; NADP; Nonlinear Dynamics; Protein Binding; Pyrimidines; Recombinant Proteins; Reference Standards; Regression Analysis; Spectrum Analysis; Sulfaphenazole; Triazoles | 2007 |
The inactivation of cytochrome P450 3A5 by 17alpha-ethynylestradiol is cytochrome b5-dependent: metabolic activation of the ethynyl moiety leads to the formation of glutathione conjugates, a heme adduct, and covalent binding to the apoprotein.
Topics: Apoproteins; Biotransformation; Chemical Phenomena; Chemistry, Physical; Chromatography, High Pressure Liquid; Chromatography, Liquid; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme Inhibitors; Cytochromes b5; Endopeptidases; Enzyme Inhibitors; Ethinyl Estradiol; Glutathione; Heme; Humans; Mass Spectrometry; NADP; Spectrometry, Mass, Electrospray Ionization | 2007 |
Synchronous photoinitiation of endothelial NO synthase activity by a nanotrigger targeted at its NADPH site.
Topics: Binding Sites; Binding, Competitive; Flavins; Heme; Kinetics; NADP; Nanoparticles; Nitric Oxide Synthase Type III; Oxidation-Reduction; Photochemistry | 2007 |
Regulation of a glutamyl-tRNA synthetase by the heme status.
Topics: Acidithiobacillus; Aldehyde Oxidoreductases; Blotting, Western; DNA Primers; Feedback, Physiological; Gene Expression Regulation, Bacterial; Glutamate-tRNA Ligase; Heme; Hemin; NADP; Recombinant Proteins; Spectrophotometry | 2007 |
CYP2C9 protein interactions with cytochrome b(5): effects on the coupling of catalysis.
Topics: Allosteric Regulation; Animals; Aryl Hydrocarbon Hydroxylases; Catalysis; Cytochrome P-450 CYP2C9; Cytochromes b5; Diclofenac; Flurbiprofen; Heme; Humans; Hydrogen Peroxide; Kinetics; Models, Biological; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation; Rats; Recombinant Proteins; Warfarin; Water | 2007 |
Neuroglobin and cytoglobin as potential enzyme or substrate.
Topics: Animals; Catalase; Disulfides; Enzymes; Globins; Heme; Humans; Iron; NAD; NADP; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Peroxidase; Spectrophotometry; Spectrum Analysis, Raman; Substrate Specificity; Superoxide Dismutase; Thioredoxin-Disulfide Reductase | 2007 |
Analysis of the interactions of cytochrome b5 with flavocytochrome P450 BM3 and its domains.
Topics: Animals; Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Cytochromes b5; Electron Transport; Flavin-Adenine Dinucleotide; Flavins; Heme; Houseflies; Kinetics; Lauric Acids; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation; Spectrophotometry, Ultraviolet; Substrate Specificity | 2007 |
Cyclic changes in metabolic state during the life of a yeast cell.
Topics: Acetyl Coenzyme A; Gene Expression Regulation, Fungal; Genes, Fungal; Heme; NADP; Saccharomyces cerevisiae; Sulfur; Time Factors | 2007 |
Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail.
Topics: Amino Acid Sequence; Animals; Computer Simulation; Cytochrome Reductases; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Molecular Sequence Data; Mutation; NADP; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Rats | 2007 |
BYK191023 (2-[2-(4-methoxy-pyridin-2-yl)-ethyl]-3h-imidazo[4,5-b]pyridine) is an NADPH- and time-dependent irreversible inhibitor of inducible nitric-oxide synthase.
Topics: Anaerobiosis; Animals; Carbon Monoxide; Cell Line; Chromatography, Gel; Chromatography, High Pressure Liquid; Dimerization; Enzyme Activation; Enzyme Inhibitors; Heme; Humans; Imidazoles; Iron; Kinetics; Mice; NADP; Nitric Oxide; Nitric Oxide Synthase Type II; Oxidation-Reduction; Oxygen; Pyridines; Time Factors; Tritium | 2008 |
Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel.
Topics: Bacterial Proteins; Crystallization; Crystallography, X-Ray; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Enzyme Inhibitors; Fatty Acids; Heme; Imidazoles; Leucine; Mixed Function Oxygenases; Models, Molecular; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation | 2008 |
On the functional role of a water molecule in clade 3 catalases: a proposal for the mechanism by which NADPH prevents the formation of compound II.
Topics: Catalase; Crystallography, X-Ray; Ferric Compounds; Heme; Models, Molecular; NADP; Quantum Theory; Structure-Activity Relationship; Thermodynamics | 2008 |
Isoporphyrin intermediate in heme oxygenase catalysis. Oxidation of alpha-meso-phenylheme.
Topics: Biliverdine; Carbon Monoxide; Catalysis; Chromatography, High Pressure Liquid; Heme; Heme Oxygenase-1; Humans; Hydrogen Peroxide; Iron; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Spectrometry, Mass, Electrospray Ionization; Superoxides | 2008 |
Regulation of eNOS-derived superoxide by endogenous methylarginines.
Topics: Arginine; Biopterins; Electron Spin Resonance Spectroscopy; Heme; Humans; NADP; Nitric Oxide Synthase Type III; omega-N-Methylarginine; Superoxides | 2008 |
Synthesis and evaluation of pyrido[1,2-a]pyrimidines as inhibitors of nitric oxide synthases.
Topics: Animals; Cell Line; Drug Evaluation, Preclinical; Enzyme Inhibitors; Ethylenediamines; Gene Expression Regulation, Enzymologic; Heme; Humans; Isoenzymes; Macrophages; Mice; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Pyrimidines; Radioactivity; Rats; Structure-Activity Relationship; Substrate Specificity; Sulfanilamides | 2009 |
Metabolic activation of mifepristone [RU486; 17beta-hydroxy-11beta-(4-dimethylaminophenyl)-17alpha-(1-propynyl)-estra-4,9-dien-3-one] by mammalian cytochromes P450 and the mechanism-based inactivation of human CYP2B6.
Topics: Animals; Apoproteins; Aryl Hydrocarbon Hydroxylases; Biotransformation; Chromatography, High Pressure Liquid; Crystallization; Cytochrome P-450 CYP2B6; Cytochrome P-450 Enzyme System; Dexamethasone; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Glutathione; Heme; Hormone Antagonists; Humans; In Vitro Techniques; Isoenzymes; Microsomes, Liver; Mifepristone; NADP; Oxidoreductases, N-Demethylating; Phenobarbital; Rats; Spectrometry, Mass, Electrospray Ionization; Substrate Specificity; Tandem Mass Spectrometry | 2009 |
An oxygen-sensitive mechanism in regulation of epithelial sodium channel.
Topics: Animals; Epithelial Sodium Channels; Heme; Heme Oxygenase (Decyclizing); Mice; NADP; Oxygen; Patch-Clamp Techniques | 2009 |
Verdoheme formation in Proteus mirabilis catalase.
Topics: Biliverdine; Catalase; Crystallography, X-Ray; Edetic Acid; Heme; Kinetics; Metals; Mutant Proteins; NADP; Oxidation-Reduction; Peracetic Acid; Protein Structure, Secondary; Proteus mirabilis; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Static Electricity | 2009 |
Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex.
Topics: Binding Sites; Calmodulin; Catalysis; Ferrous Compounds; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Mutant Proteins; NADP; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Oxygen; Point Mutation; Temperature; Time Factors | 2009 |
NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Electron Spin Resonance Spectroscopy; Electron Transport; Electrophoresis, Polyacrylamide Gel; Heme; Kinetics; Models, Chemical; Molecular Sequence Data; Myxococcales; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxygen; Protein Binding; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Substrate Specificity | 2009 |
An ATP and oxalate generating variant tricarboxylic acid cycle counters aluminum toxicity in Pseudomonas fluorescens.
Topics: Adenosine Triphosphate; Aldehyde Oxidoreductases; Aluminum; Citric Acid Cycle; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation, Enzymologic; Heme; Isocitrate Lyase; Models, Biological; NADP; Oxalates; Oxygen; Pseudomonas fluorescens | 2009 |
How does a valine residue that modulates heme-NO binding kinetics in inducible NO synthase regulate enzyme catalysis?
Topics: Animals; Bacillus subtilis; Binding Sites; Catalysis; Computer Simulation; Heme; Isoenzymes; Mice; Molecular Structure; Mutagenesis, Site-Directed; NADP; Nitrates; Nitric Oxide; Nitric Oxide Synthase Type II; Nitrites; Oxidation-Reduction; Superoxides; Valine | 2010 |
Mitochondria isolated in nearly isotonic KCl buffer: focus on cardiolipin and organelle morphology.
Topics: Animals; Buffers; Cardiolipins; Cell Respiration; Chromatography, Thin Layer; Cytochrome Reductases; Heme; Isotonic Solutions; Lipids; Mitochondria, Liver; NADP; Organelle Shape; Oxygen Consumption; Potassium Chloride; Rats; Spectrometry, Mass, Electrospray Ionization | 2010 |
LICRED: a versatile drop-in vector for rapid generation of redox-self-sufficient cytochrome P450s.
Topics: Cytochrome P-450 Enzyme System; Electron Transport; Enzymes; Genetic Vectors; Heme; Kinetics; NADP; Oxidation-Reduction; Protein Structure, Tertiary; Recombinant Fusion Proteins | 2010 |
A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism.
Topics: Animals; Binding Sites; Calmodulin; Catalysis; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Mutagenesis, Site-Directed; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Protein Structure, Tertiary; Rats | 2010 |
Understanding uncoupling in the multiredox centre P450 3A4-BMR model system.
Topics: Bacterial Proteins; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Electron Transport; Heme; Humans; Hydrogen-Ion Concentration; Models, Biological; NADP; NADPH-Ferrihemoprotein Reductase; Osmolar Concentration; Oxidation-Reduction; Oxidoreductases; Phosphates; Potassium Compounds; Recombinant Proteins | 2011 |
Quantitating carbon monoxide production from heme by vascular plant preparations in vitro.
Topics: Carbon Monoxide; Chloroplasts; Chromatography, Gas; Heme; NADP; Oxygen; Plant Structures; Plants; Solanum tuberosum; Spinacia oleracea | 2011 |
Reciprocal regulation of Ca²+-activated outward K+ channels of Pyrus pyrifolia pollen by heme and carbon monoxide.
Topics: Carbon Monoxide; Germination; Heme; Ion Channel Gating; NADP; Pollen; Pollen Tube; Potassium Channels, Calcium-Activated; Protoplasts; Pyrus | 2011 |
Biodiversity in sulfur metabolism in hemiascomycetous yeasts.
Topics: Amino Acids, Sulfur; Biodiversity; Cysteine; Genetic Variation; Glucosephosphate Dehydrogenase; Glutathione; Heme; Homocysteine; Methionine; NADP; Phylogeny; Sequence Alignment; Sequence Analysis, Protein; Sulfur; Yeasts | 2011 |
Caffeine inhibits erythrocyte membrane derangement by antioxidant activity and by blocking caspase 3 activation.
Topics: Anion Exchange Protein 1, Erythrocyte; Binding Sites; Biological Transport; Caffeine; Caspase 3; Erythrocyte Membrane; Erythrocytes; Heme; Hemoglobins; Humans; Hydroxyl Radical; Kinetics; Models, Molecular; NADP; Oxidation-Reduction; Oxygen; Pentose Phosphate Pathway; Protein Binding; Protein Conformation; Thermodynamics | 2012 |
Influence of heme-thiolate in shaping the catalytic properties of a bacterial nitric-oxide synthase.
Topics: Amino Acid Substitution; Bacillus subtilis; Bacterial Proteins; Catalysis; Heme; Hydroxylation; Mutation, Missense; NADP; Nitric Oxide Synthase; Oxidation-Reduction | 2011 |
Interactions of the antimalarial drug methylene blue with methemoglobin and heme targets in Plasmodium falciparum: a physico-biochemical study.
Topics: Animals; Antimalarials; Dimerization; Glutathione Reductase; Heme; Humans; Hydrogen-Ion Concentration; Methemoglobin; Methylene Blue; Molecular Structure; NADP; Oxidation-Reduction; Plasmodium falciparum; Proteolysis | 2012 |
Mechanism-based inactivation of cytochrome P450 2B6 by methadone through destruction of prosthetic heme.
Topics: Analgesics, Opioid; Aryl Hydrocarbon Hydroxylases; Biotransformation; Carbon Monoxide; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP2B6; Dose-Response Relationship, Drug; Enzyme Inhibitors; Heme; Humans; Kinetics; Methadone; NADP; Oxidoreductases, N-Demethylating; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet | 2012 |
Inhibition of bupropion metabolism by selegiline: mechanism-based inactivation of human CYP2B6 and characterization of glutathione and peptide adducts.
Topics: Amino Acid Sequence; Antidepressive Agents, Second-Generation; Antiparkinson Agents; Aryl Hydrocarbon Hydroxylases; Bupropion; Chromatography, Liquid; Cytochrome P-450 CYP2B6; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Drug Interactions; Escherichia coli; Glutathione; Heme; Humans; Hydroxylation; Molecular Sequence Data; NADP; Oxidoreductases, N-Demethylating; Peptides; Selegiline; Tandem Mass Spectrometry | 2012 |
Alterations of the redox state, pentose pathway and glutathione metabolism in an acute porphyria model. Their impact on heme pathway.
Topics: Allylisopropylacetamide; Animals; Disease Models, Animal; Glucose; Glucosephosphate Dehydrogenase; Glutathione; Glutathione Disulfide; Glutathione Peroxidase; Glutathione Reductase; Glutathione Transferase; Heme; Liver; NADP; Oxidation-Reduction; Oxidative Stress; Pentose Phosphate Pathway; Porphyria, Acute Intermittent; Pyridines; Rats; Reactive Oxygen Species | 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 |
Role of the highly conserved threonine in cytochrome P450 2E1: prevention of H2O2-induced inactivation during electron transfer.
Topics: Antioxidants; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP2E1; Cytochrome P-450 CYP2E1 Inhibitors; Electron Transport; Electrophoresis, Polyacrylamide Gel; Heme; Hydrogen Peroxide; Mutation; NADP | 2013 |
Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.
Topics: Animals; Arginine; Binding Sites; Biocatalysis; Computer Simulation; Ferrous Compounds; Heme; Kinetics; Models, Chemical; NADP; Neurons; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Oxygen; Protein Binding; Rats; Temperature; Thermodynamics | 2013 |
IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus.
Topics: Bacterial Proteins; Flavoproteins; Heme; Hydrogen Peroxide; Iron; Mixed Function Oxygenases; NADP; Oxidants; Oxygenases; Staphylococcus aureus | 2013 |
Butyric acid-induced rat jugular blood cytosolic oxidative stress is associated with SIRT1 decrease.
Topics: Animals; Butyric Acid; Cytosol; Gingiva; Heme; Jugular Veins; NAD; NADP; Oxidative Stress; Rats; Sirtuin 1 | 2014 |
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Binding Sites; Crystallography, X-Ray; Glutamates; Glutamic Acid; Heme; Models, Molecular; Molecular Sequence Data; Multiprotein Complexes; NADP; Protein Interaction Domains and Motifs; Recombinant Proteins; RNA-Binding Proteins; Sequence Homology, Amino Acid; Static Electricity | 2014 |
Time- and NADPH-dependent inhibition of cytochrome P450 3A4 by the cyclopentapeptide cilengitide: significance of the guanidine group and accompanying spectral changes.
Topics: Adult; Cytochrome P-450 CYP3A; Enzyme Inhibitors; Female; Guanidine; Heme; Humans; Male; Microsomes, Liver; NADP; Oxidation-Reduction; Snake Venoms | 2014 |
Flavonoid-induced conversion of catalase to its inactive form--Compound II.
Topics: Animals; Catalase; Catalysis; Cattle; Flavonoids; Heme; Humans; Hydrogen Peroxide; Models, Molecular; NADP; Oxidants; Oxidation-Reduction | 2014 |
Mechanism-based inactivation of human cytochrome P450 3A4 by two piperazine-containing compounds.
Topics: Cytochrome P-450 CYP2D6; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme Inhibitors; Heme; Humans; Imidazoles; Mass Spectrometry; NADP; Piperazine; Piperazines; Pyridines; Pyrimidines | 2014 |
CYP116B5: a new class VII catalytically self-sufficient cytochrome P450 from Acinetobacter radioresistens that enables growth on alkanes.
Topics: Acinetobacter; Alkanes; Amino Acid Sequence; Binding Sites; Biocatalysis; Biological Evolution; Cytochrome P-450 Enzyme System; Escherichia coli; Evolution, Molecular; Gene Transfer, Horizontal; Heme; Italy; Molecular Sequence Data; NADP; Oxidation-Reduction; Phylogeny; Recombinant Proteins; Rhodococcus; Sequence Alignment; Soil Microbiology | 2015 |
Middle-aged rats orally supplemented with gel-encapsulated catechin favorably increases blood cytosolic NADPH levels.
Topics: Age Factors; Animals; Antioxidants; Catalase; Catechin; Cytosol; Fatty Acids; Glutathione Reductase; Heme; Hydrogen Peroxide; Male; NADP; Rats; Rats, Sprague-Dawley; Sirtuin 1 | 2015 |
Characterization of a single b-type heme, FAD, and metal binding sites in the transmembrane domain of six-transmembrane epithelial antigen of the prostate (STEAP) family proteins.
Topics: Antigens, Neoplasm; Copper; Flavin-Adenine Dinucleotide; HEK293 Cells; Heme; Humans; Iron; NADP; Protein Multimerization; Protein Structure, Tertiary | 2015 |
Elucidating nitric oxide synthase domain interactions by molecular dynamics.
Topics: Calmodulin; Electron Transport; Flavin Mononucleotide; Heme; Humans; Molecular Dynamics Simulation; NADP; Nitric Oxide; Nitric Oxide Synthase Type II; Oxidation-Reduction; Protein Interaction Domains and Motifs | 2016 |
The protein inhibitor of nNOS (PIN/DLC1/LC8) binding does not inhibit the NADPH-dependent heme reduction in nNOS, a key step in NO synthesis.
Topics: Calmodulin; Cytoplasmic Dyneins; Electron Transport; Enzyme Inhibitors; Heme; Humans; In Vitro Techniques; Kinetics; NADP; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Binding; Recombinant Proteins | 2016 |
An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.
Topics: Binding Sites; Coenzymes; Crystallography, X-Ray; Dimethylamines; Flavin Mononucleotide; Heme; Iron-Sulfur Proteins; Models, Molecular; NADP; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Oxygen; Protein Domains; Protein Subunits; Pseudomonas mendocina; Tetrahydrofolates | 2016 |
Structural and functional study of ChuY from Escherichia coli strain CFT073.
Topics: Animals; Biliverdine; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; FMN Reductase; Gene Deletion; Genomics; HEK293 Cells; Heme; Hemin; Homeostasis; Humans; Iron; Mice; NADP; Oxidoreductases Acting on CH-CH Group Donors; Porphyrins; Protein Conformation; Protein Structure, Secondary; RAW 264.7 Cells; Virulence | 2017 |
Anaerobic Heme Degradation: ChuY Is an Anaerobilin Reductase That Exhibits Kinetic Cooperativity.
Topics: Apoenzymes; Biocatalysis; Deuterium; Dimerization; Escherichia coli O157; Escherichia coli Proteins; Heme; Hydrolysis; Models, Molecular; Molecular Structure; Molecular Weight; NADP; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Protein Conformation; Protein Interaction Domains and Motifs; Recombinant Proteins; Structural Homology, Protein; Substrate Specificity; Tetrapyrroles | 2017 |
The self-sufficient CYP102 family enzyme, Krac9955, from Ktedonobacter racemifer DSM44963 acts as an alkyl- and alkyloxy-benzoic acid hydroxylase.
Topics: Bacterial Proteins; Carbon; Chloroflexi; Cytochrome P-450 Enzyme System; Electron Transport; Escherichia coli; Fatty Acids; Heme; Hydroxylation; Kinetics; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen; Oxygenases; Protein Domains; Substrate Specificity | 2017 |
HmuS from Yersinia pseudotuberculosis is a non-canonical heme-degrading enzyme to acquire iron from heme.
Topics: Ferredoxin-NADP Reductase; Heme; Iron; NADP; Spectrum Analysis, Raman; Structure-Activity Relationship; Yersinia pseudotuberculosis | 2017 |
Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.
Topics: Bacillus megaterium; Bacterial Proteins; Catalytic Domain; Cloning, Molecular; Cobalt; Coenzymes; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electrons; Escherichia coli; Gene Expression; Heme; Models, Molecular; NADP; NADPH-Ferrihemoprotein Reductase; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Recombinant Proteins; Substrate Specificity; Zinc | 2018 |
The FNR modules contribute to control nitric oxide synthase catalysis revealed by chimera enzymes.
Topics: Animals; Biocatalysis; Cytochromes c; Ferredoxin-NADP Reductase; Ferricyanides; Flavins; Heme; Kinetics; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxygenases; Rats; Recombinant Fusion Proteins; Spectrum Analysis; Time Factors | 2017 |
Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase.
Topics: Amitrole; Binding Sites; Catalase; Catalytic Domain; Crystallography, X-Ray; Fungal Proteins; Fungi; Heme; NADP; Oxidoreductases | 2018 |
Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
Topics: Binding Sites; Biocatalysis; Cryoelectron Microscopy; Electrons; Flavin-Adenine Dinucleotide; Heme; Humans; Iron; Membrane Proteins; NADP; NADPH Oxidases; Oxidation-Reduction; Oxidoreductases; Protein Domains; Substrate Specificity | 2018 |
Crystal structures of the naturally fused CS and cytochrome b
Topics: Carrier Proteins; Catalytic Domain; Crystallization; Cytochrome-B(5) Reductase; Cytochromes b5; Heme; Humans; Hydrogen Bonding; Kinetics; Membrane Proteins; Models, Molecular; Multiprotein Complexes; NAD; NADP; Oxidation-Reduction; Phosphate-Binding Proteins; Protein Conformation, beta-Strand; Protein Domains; Recombinant Proteins | 2019 |
Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.
Topics: Animals; Aspartic Acid; Binding Sites; Cloning, Molecular; Electrons; Escherichia coli; Ficoll; Flavin Mononucleotide; Gene Expression; Genetic Vectors; Heme; HSP90 Heat-Shock Proteins; Humans; Lysine; Molecular Docking Simulation; Mutation; NADP; Nitric Oxide Synthase Type I; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Rats; Recombinant Proteins; Static Electricity | 2020 |
HutW from
Topics: Anaerobiosis; Bacterial Outer Membrane Proteins; Gene Expression Regulation, Bacterial; Heme; Methyltransferases; NADP; Protein Conformation; S-Adenosylmethionine; Tetrapyrroles; Vibrio cholerae | 2021 |
Structure and functional properties of the cold-adapted catalase from Acinetobacter sp. Ver3 native to the Atacama plateau in northern Argentina.
Topics: Acclimatization; Acinetobacter; Argentina; Bacterial Proteins; Binding Sites; Catalase; Cold Temperature; Crystallography, X-Ray; Enzyme Stability; Heme; Models, Molecular; NADP; Protein Conformation | 2021 |
Protective activity of purpurin against d-galactosamine and lipopolysaccharide-induced hepatorenal injury by upregulation of heme oxygenase-1 in the RBC degradation cycle.
Topics: Animals; Anthraquinones; Antioxidants; Biliverdine; Catalase; Cholesterol; Cytochrome P-450 CYP2E1; Female; Ferritins; Food Additives; Galactosamine; Glutathione; Glutathione Peroxidase; Glutathione Reductase; Heme; Heme Oxygenase-1; Hemosiderin; Inflammation; Lipopolysaccharides; Liver; NADP; Rats; Superoxide Dismutase; Transferases; Triglycerides; Up-Regulation | 2022 |
Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency.
Topics: Animals; Calcium; Eukaryota; Flavin-Adenine Dinucleotide; Heme; NADP; NADPH Oxidase 1; NADPH Oxidase 4; NADPH Oxidases; Oxygen; Phylogeny; Reactive Oxygen Species | 2022 |
Evidence for Porphyrin-Mediated Electron Transfer in the Radical SAM Enzyme HutW.
Topics: Electrons; Heme; Humans; Iron; Iron-Sulfur Proteins; NADP; Porphyrins; S-Adenosylmethionine | 2023 |
Mechanism of stepwise electron transfer in six-transmembrane epithelial antigen of the prostate (STEAP) 1 and 2.
Topics: Antigens, Neoplasm; Cryoelectron Microscopy; Electrons; Heme; Humans; Male; NADP; Oxidoreductases; Prostate | 2023 |