Novel haem co-ordination variants of flavocytochrome P450 BM3

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Novel haem co-ordination variants of flavocytochrome P450BM3.

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Flavocytochrome P450 BM3 and the origin of CYP102 fusion species.

Flavocytochrome P450 (cytochrome P450) BM3 is an intensively studied model system within the P450 enzyme superfamily, and is a natural fusion of a P450 to its P450 reductase redox partner. The fusion arrangement enables efficient electron transfer within the enzyme and a catalytic efficiency that cannot be matched in P450 systems from higher organisms. P450 BM3's potential for industrially rele...

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Roles of key active-site residues in flavocytochrome P450 BM3.

The effects of mutation of key active-site residues (Arg-47, Tyr-51, Phe-42 and Phe-87) in Bacillus megaterium flavocytochrome P450 BM3 were investigated. Kinetic studies on the oxidation of laurate and arachidonate showed that the side chain of Arg-47 contributes more significantly to stabilization of the fatty acid carboxylate than does that of Tyr-51 (kinetic parameters for oxidation of laur...

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Analysis of the oxidation of short chain alkynes by flavocytochrome P450 BM3.

Bacillus megaterium flavocytochrome P450 BM3 (BM3) is a high activity fatty acid hydroxylase, formed by the fusion of soluble cytochrome P450 and cytochrome P450 reductase modules. Short chain (C6, C8) alkynes were shown to be substrates for BM3, with productive outcomes (i.e. alkyne hydroxylation) dependent on position of the carbon-carbon triple bond in the molecule. Wild-type P450 BM3 cataly...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2008

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj20081133