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Portland Press, Biochemical Society Transactions, 3(31), p. 497-501, 2003

DOI: 10.1042/bst0310497

Portland Press, Biochemical Society Transactions, 1(29), p. A9-A9, 2001

DOI: 10.1042/bst029a009b

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Electron transfer in human cytochrome P450 reductase.

Journal article published in 2001 by A. Gutierrez, A. Grunau, Mark Paine ORCID, Aw W. Munro, Cr R. Wolf, Gck C. K. Roberts, Ns S. Scrutton, Grunau A Paine M Munro AW Wolf CR Roberts GC Scrutton Ns Gutierrez A.
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.