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Article

Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes.

The Journal of biological chemistry - 6 May 2005

Neeli Rajasekhar, Roitel Olivier, Scrutton Nigel S, Munro Andrew W

Abstract excerpt

Flavocytochrome P450 BM3 is a member of the diflavin reductase enzyme family. Members include cytochrome P450 reductase, nitric-oxide synthase, methionine synthase reductase, and novel oxidoreductase 1. These enzymes show a strong preference for NADPH over NADH as reducing coenzyme. An aromatic residue stacks over the FAD isoalloxazine ring in each enzyme, and in some cases it is important in controlling coenzyme...

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Identifiers

PMID: 15710617
DOI: 10.1074/jbc.M413826200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes.PMID 15710617Read ↗

Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer.Semantic proximity Read ↗

The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3.Semantic proximity Read ↗

Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.Semantic proximity Read ↗

Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.Semantic proximity Read ↗

The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase.Semantic proximity Read ↗

Flavocytochrome P450 BM3 mutant A264E undergoes substrate-dependent formation of a novel heme iron ligand set.Semantic proximity Read ↗

Novel haem co-ordination variants of flavocytochrome P450BM3.Semantic proximity Read ↗

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Structure, electronic properties and catalytic behaviour of an activity-enhancing CYP102A1 (P450(BM3)) variant.Semantic proximity Read ↗

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.Semantic proximity Read ↗

Key mutations alter the cytochrome P450 BM3 conformational landscape and remove inherent substrate bias.Semantic proximity Read ↗

Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3.Semantic proximity Read ↗

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