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- W2144572696 abstract "Enzymes that catalyze the terminal hydroxylation of alkanes could be used to produce more valuable chemicals from hydrocarbons. Cytochrome P450 BM3 from Bacillus megaterium hydroxylates medium-chain fatty acids at subterminal positions at high rates. To engineer BM3 for terminal alkane hydroxylation, we performed saturation mutagenesis at selected active-site residues of a BM3 variant that hydroxylates alkanes. Recombination of beneficial mutations generated a library of BM3 mutants that hydroxylate linear alkanes with a wide range of regioselectivities. Mutant 77-9H exhibits 52% selectivity for the terminal position of octane. This regioselectivity is octane-specific and does not transfer to other substrates, including shorter and longer hydrocarbons or fatty acids. These results show that BM3 can be readily molded for regioselective oxidation." @default.
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- W2144572696 date "2006-04-01" @default.
- W2144572696 modified "2023-10-18" @default.
- W2144572696 title "Engineering Cytochrome P450 BM3 for Terminal Alkane Hydroxylation" @default.
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- W2144572696 doi "https://doi.org/10.1002/adsc.200505465" @default.
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