Role of active site loop in coenzyme binding and flavin reduction in cytochrome P450 reductase

Archives of Biochemistry and Biophysics

Volumn 606, Issue , 2016, Pages 111-119

  Mothersole, Robert G ^a   Meints, Carla E ^a   Louder, Alex ^a   Wolthers, Kirsten R ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Cytochrome P450 reductase; Flavin enzymology; Stopped flow spectroscopy

Indexed keywords

CYTOCHROME C3; CYTOCHROME P450 REDUCTASE; METHIONINE SYNTHASE REDUCTASE; QUERCETIN; ALANINE; ARGININE; ASPARTIC ACID; CYTOCHROME C; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN BINDING; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; RIBOFLAVIN DERIVATIVE; TRYPTOPHAN;

AMINO ACID COMPOSITION; ARTICLE; COENZYME; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME STABILITY; FLOW MEASUREMENT; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; MICHAELIS CONSTANT; NONHUMAN; NUCLEOTIDE SEQUENCE; OBSERVED RATE CONSTANT; PRIORITY JOURNAL; REDUCTION; SITE DIRECTED MUTAGENESIS; STEADY STATE; SUBSTRATE CONCENTRATION; ULTRAVIOLET SPECTROPHOTOMETRY; ARABIDOPSIS; BACILLUS MEGATERIUM; CATALYSIS; CHEMISTRY; HYDROGEN BOND; KINETICS; MUTATION; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE; STATIC ELECTRICITY;

ALANINE; ARABIDOPSIS; ARGININE; ASPARTIC ACID; BACILLUS MEGATERIUM; CATALYSIS; CATALYTIC DOMAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYTOCHROMES C; FLAVINS; HUMANS; HYDROGEN BONDING; KINETICS; MUTAGENESIS, SITE-DIRECTED; MUTATION; NADP; NADPH-FERRIHEMOPROTEIN REDUCTASE; PROTEIN BINDING; PROTEIN DOMAINS; SACCHAROMYCES CEREVISIAE; STATIC ELECTRICITY; TRYPTOPHAN;

EID: 84979686884     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2016.07.018     Document Type: Article

References (29)

1. [1] Enoch, H.G., Strittmatter, P., J. Biol. Chem. 254 (1979), 8976–8981.
2. [2] Ono, T., Bloch, K., J. Biol. Chem. 250 (1975), 1571–1579.
3. [3] Schacter, B.A., Nelson, E.B., Marver, H.S., Masters, B.S., J. Biol. Chem. 247 (1972), 3601–3607.
4. [4] Guengerich, F.P., Chem. Res. Toxicol. 14 (2001), 611–650.
5. [5] Isin, E.M., Guengerich, F.P., Biochim. Biophys. Acta 1770 (2007), 314–329.
6. [6] Vermilion, J.L., Ballou, D.P., Massey, V., Coon, M.J., J. Biol. Chem. 256 (1981), 266–277.
7. [7] Oprian, D.D., Coon, M.J., J. Biol. Chem. 257 (1982), 8935–8944.
8. [8] Vermilion, J.L., Coon, M.J., J. Biol. Chem. 253 (1978), 8812–8819.
9. [9] Aigrain, L., Fatemi, F., Frances, O., Lescop, E., Truan, G., Int. J. Mol. Sci. 13 (2012), 15012–15041.
10. [10] Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S., Kim, J.J., Proc. Natl. Acad. Sci. U. S. A. 94 (1997), 8411–8416.
11. [11] Hamdane, D., Xia, C., Im, S.C., Zhang, H., Kim, J.J., Waskell, L., J. Biol. Chem. 284 (2009), 11374–11384.
12. [12] Aigrain, L., Pompon, D., Morera, S., Truan, G., EMBO Rep. 10 (2009), 742–747.
13. [13] Xia, C., Hamdane, D., Shen, A.L., Choi, V., Kasper, C.B., Pearl, N.M., Zhang, H., Im, S.C., Waskell, L., Kim, J.J., J. Biol. Chem. 286 (2011), 16246–16260.
14. [14] Hubbard, P.A., Shen, A.L., Paschke, R., Kasper, C.B., Kim, J.J., J. Biol. Chem. 276 (2001), 29163–29170.
15. [15] Roitel, O., Scrutton, N.S., Munro, A.W., Biochemistry 42 (2003), 10809–10821.
16. [16] Viola, R.E., Cook, P.F., Cleland, W.W., Anal. Biochem. 96 (1979), 334–340.
17. [17] Olteanu, H., Banerjee, R., J. Biol. Chem. 276 (2001), 35558–35563.
18. [18] Meints, C.E., Simtchouk, S., Wolthers, K.R., Febs J. 280 (2013), 1460–1474.
19. [19] Simtchouk, S., Eng, J.L., Meints, C.E., Makins, C., Wolthers, K.R., Febs J. 280 (2013), 6627–6642.
20. [20] Lian, L.Y., Widdowson, P., McLaughlin, L.A., Paine, M.J., PLoS One, 6, 2011, e20574.
21. [21] Sem, D.S., Kasper, C.B., Biochemistry 34 (1995), 12768–12774.
22. [22] Shen, A.L., Porter, T.D., Wilson, T.E., Kasper, C.B., J. Biol. Chem. 264 (1989), 7584–7589.
23. [23] Brenner, S., Hay, S., Munro, A.W., Scrutton, N.S., Febs J. 275 (2008), 4540–4557.
24. [24] Sem, D.S., Kasper, C.B., Biochemistry 32 (1993), 11548–11558.
25. [25] Wolthers, K.R., Lou, X., Toogood, H.S., Leys, D., Scrutton, N.S., Biochemistry 46 (2007), 11833–11844.
26. [26] Joyce, M.G., Ekanem, I.S., Roitel, O., Dunford, A.J., Neeli, R., Girvan, H.M., Baker, G.J., Curtis, R.A., Munro, A.W., Leys, D., Febs J. 279 (2012), 1694–1706.
27. [27] Wolthers, K.R., Scrutton, N.S., Biochemistry 43 (2004), 490–500.
28. [28] Finn, R.D., Basran, J., Roitel, O., Wolf, C.R., Munro, A.W., Paine, M.J., Scrutton, N.S., Eur. J. Biochem. 270 (2003), 1164–1175.
29. [29] Gutierrez, A., Paine, M., Wolf, C.R., Scrutton, N.S., Roberts, G.C., Biochemistry 41 (2002), 4626–4637.