Electron transfer in human cytochrome P450 reductase

Author:

Gutierrez A.1,Grunau A.1,Paine M.2,Munro A.W.1,Wolf C.R.2,Roberts G.C.K.13,Scrutton N.S.1

Affiliation:

1. Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, U.K.

2. Biomedical Research Centre, University of Dundee, Ninewells Hospital and Medical School, Dundee DD1 9SY, U.K.

3. Biological NMR Centre, University of Leicester, University Road, Leicester LE1 7RH, U.K.

Abstract

Cytochrome P450 reductase (CPR) is a diflavin enzyme responsible for electron donation to mammalian cytochrome P450 enzymes in the endoplasmic reticulum. Dissection of the enzyme into functional domains and studies by site-directed mutagenesis have enabled detailed characterization of the mechanism of electron transfer using stopped-flow and equilibrium-perturbation methods, and redox potentiometry. These studies and the mechanism of electron transfer in CPR are reported herein.

Publisher

Portland Press Ltd.

Subject

Biochemistry

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