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Article

Engineering of a functional human NADH-dependent cytochrome P450 system.

Proceedings of the National Academy of Sciences of the United States of America - 2 Jan 2001

Döhr O, Paine M J, Friedberg T, Roberts G C, Wolf C R

Abstract excerpt

A functional human NADH-dependent cytochrome P450 system has been developed by altering the cofactor preference of human NADPH cytochrome P450 reductase (CPR), the redox partner for P450s. This has been achieved by a single amino acid change of the conserved aromatic amino acid Trp-676, which covers the re-side of the FAD isoalloxazine ring in the nicotinamide-binding site. Of the mutations made, the substitution...

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Identifiers

PMID: 11136248
DOI: 10.1073/pnas.98.1.81
PMCID: PMC14548

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