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

عرض إصدارات أخرى (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...

وصف كامل

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Vincent, B, Morellet, N, Fatemi, F, Aigrain, L, Truan, G, Guittet, E, Lescop, E
التنسيق:	Journal article
اللغة:	English
منشور في:	2012

مواد مشابهة

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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منشور في: (2012)

Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.
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منشور في: (2009)

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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Cloning, purification, crystallization and preliminary X-ray analysis of a chimeric NADPH-cytochrome P450 reductase.
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Dynamic control of electron transfers in diflavin reductases.
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Correction: The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength
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Effects of Diminished NADPH:cytochrome P450 Reductase in Human Hepatocytes on Lipid and Bile Acid Homeostasis
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Putidaredoxin binds to the same site on cytochrome P450cam in the open and closed conformation
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