The closed and compact domain organization of the 70-kDa human cytochrome P450 reductase in its oxidized state as revealed by NMR

The closed and compact domain organization of the 70-kDa human cytochrome P450 reductase in its oxidized state as revealed by NMR

Ցույց տալ այլ տարբերակներ (1)

The NADPH cytochrome P450 reductase (CPR), a diflavin enzyme, catalyzes the electron transfer (ET) from NADPH to the substrate P450. The crystal structures of mammalian and yeast CPRs show a compact organization for the two domains containing FMN (flavin mononucleotide) and FAD (flavin adenine dinuc...

Ամբողջական նկարագրություն

Մատենագիտական մանրամասներ
Հիմնական հեղինակներ:	Vincent, B, Morellet, N, Fatemi, F, Aigrain, L, Truan, G, Guittet, E, Lescop, E
Ձևաչափ:	Journal article
Լեզու:	English
Հրապարակվել է:	2012

Նմանատիպ նյութեր

The closed and compact domain organization of the 70-kDa human cytochrome P450 reductase in its oxidized state as revealed by NMR.
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Հրապարակվել է: (2012)

Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.
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Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase.
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Dynamic control of electron transfers in diflavin reductases.
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Cytochrome P450 monooxygenases.
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The Cytochrome P450 Homepage
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