NDLI: Analysis of the oxidation of short chain alkynes by flavocytochrome P450 BM3

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Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis

Circular dichroism spectra of cytochrome c oxidase

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Metallomics Vol - 3 Issue - 3

Metallomics Vol - 3 Issue - 2

Metallomics Vol -2

Metallomics Vol -1

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

Content Provider	Royal Society of Chemistry (RSC)
Author	Holt, Robert A. Rigby, Stuart R. Dunford, Adrian J. Munro, Andrew W. Waltham, Timothy N. Girvan, Hazel M. Butler, Christopher F.
Copyright Year	2011
Abstract	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 catalyses ω-3 hydroxylation of both 1-hexyne and 1-octyne, but is suicidally inactivated in NADPH-dependent turnover with non-terminal alkynes. A F87G mutant of P450 BM3 also undergoes turnover-dependent heme destruction with the terminal alkynes, pointing to a key role for Phe87 in controlling regioselectivity of alkyne oxidation. The terminal alkynes access the BM3 heme active site led by the acetylene functional group, since hydroxylated products are not observed near the opposite end of the molecules. For both 1-hexyne and 1-octyne, the predominant enantiomeric product formed (up to ∼90%) is the (S)-(−)-1-alkyn-3-ol form. Wild-type P450 BM3 is shown to be an effective oxidase catalyst of terminal alkynes, with strict regioselectivity of oxidation and potential biotechnological applications. The absence of measurable octanoic or hexanoic acid products from oxidation of the relevant 1-alkynes is also consistent with previous studies suggesting that removal of the phenyl group in the F87G mutant does not lead to significant levels of ω-oxidation of alkyl chain substrates.
Starting Page	369
Ending Page	378
Page Count	10
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	3
Issue Number	4
Journal	Metallomics
DOI	10.1039/c1mt00004g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Hydroxylation Regioselectivity Cytochrome P450 Active site Oxidase Octyne Phenyl group Cytochrome P450 reductase Acetylene Hexyne Carboxylic acid Alkyl Fatty acid Bacillus Triple bond Catalysis Mutation Alkyne Functional group
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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