Báo cáo khoa học: Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding
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The role of coenzyme binding in regulating interflavinelectron transfer in human cytochrome P450 reductase(CPR) has been studied using temperature-jump spectros-copy. Previous studies [Gutierrez, A., Paine, M., Wolf,C.R., Scrutton, N.S., & Roberts, G.C.K.Biochemistry(2002) 41,4626–4637] have shown that the observed rate,1/s, of interflavin electron transfer (FADsq )FMNsq fiFADox)FMNhq) inCPRreduced at the two-electron levelwith NADPH is 55 ± 2 s)1, whereas with dithionite-reduced enzyme the observed rate is 11 ± 0.5 s)1,sug-gesting that NADPH (or NADP+) binding has animportant role in controlling the rate of internal electrontransfer....
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Báo cáo khoa học: Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding
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Báo cáo khoa học: Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding
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