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Arch Biochem Biophys. 2011 Mar 1;507(1):86-94. doi: 10.1016/j.abb.2010.08.011. Epub 2010 Aug 19.

Structural control of cytochrome P450-catalyzed ω-hydroxylation.

Author information

1
Department of Pharmaceutical Chemistry, University of California-San Francisco, CA 94158-2517, United States.

Abstract

The regiospecific or preferential ω-hydroxylation of hydrocarbon chains is thermodynamically disfavored because the ease of C-H bond hydroxylation depends on the bond strength, and the primary C-H bond of a terminal methyl group is stronger than the secondary or tertiary C-H bond adjacent to it. The hydroxylation reaction will therefore occur primarily at the adjacent secondary or tertiary C-H bond unless the protein structure specifically enforces primary C-H bond oxidation. Here we review the classes of enzymes that catalyze ω-hydroxylation and our current understanding of the structural features that promote the ω-hydroxylation of unbranched and methyl-branched hydrocarbon chains. The evidence indicates that steric constraints are used to favor reaction at the ω-site rather than at the more reactive (ω-1)-site.

PMID:
20727847
PMCID:
PMC2997901
DOI:
10.1016/j.abb.2010.08.011
[Indexed for MEDLINE]
Free PMC Article

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