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Article

Novel haem co-ordination variants of flavocytochrome P450BM3.

The Biochemical journal - 1 Jan 2009

Girvan Hazel M, Toogood Helen S, Littleford Rachael E, Seward Harriet E, Smith W Ewen, Ekanem Idorenyin S, Leys David, Cheesman Myles R, Munro Andrew W

Abstract excerpt

Bacillus megaterium flavocytochrome P450 BM3 is a catalytically self-sufficient fatty acid hydroxylase formed by fusion of soluble NADPH-cytochrome P450 reductase and P450 domains. Selected mutations at residue 264 in the haem (P450) domain of the enzyme lead to novel amino acid sixth (distal) co-ordination ligands to the haem iron. The catalytic, spectroscopic and thermodynamic properties of the A264M, A264Q and...

Topics

Bacterial Proteins
Circular Dichroism
Cytochrome P-450 Enzyme System
Electron Spin Resonance Spectroscopy
Fatty Acids
Glutamine
Heme
Kinetics
Methionine
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

NADPH-Ferrihemoprotein Reductase

Protein Binding

Thermodynamics

Source

Identifiers

PMID: 18721129
DOI: 10.1042/BJ20081133

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Novel haem co-ordination variants of flavocytochrome P450BM3.PMID 18721129Read ↗

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