The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.

doi:10.1042/bj3030423

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Article

The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.

The Biochemical journal - 15 Oct 1994

Munro A W, Malarkey K, McKnight J, Thomson A J, Kelly S M, Price N C, Lindsay J G, Coggins J R, Miles J S

Abstract excerpt

The 'Covalent Switching' hypothesis suggests that a strongly conserved tryptophan residue acts as a mediator of electron-transfer flow between redox partners in cytochrome P-450 systems [Baldwin, Morris and Richards (1991) Proc. R. Soc. London B 245, 43-51]. We have investigated the effect of alteration of the conserved tryptophan (Trp-97) in cytochrome P-450 BM3 (P-450 102) from Bacillus megaterium. Replacement...

Topics

Alanine
Bacillus megaterium
Bacterial Proteins
Base Sequence
Catalysis
Circular Dichroism
Cytochrome P-450 Enzyme System
DNA Primers
Electron Spin Resonance Spectroscopy
Electron Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Escherichia coli

Heme

Mixed Function Oxygenases

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

NADPH-Ferrihemoprotein Reductase

Phenylalanine

Source

Open in PubMed Open full text

Identifiers

PMID: 7980400
DOI: 10.1042/bj3030423
PMCID: PMC1137344

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7980400-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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