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Journal Article

Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1).

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Cryle,  Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Cryle, M., & De Voss, J. J. (2004). Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chemical Communications, 7(1), 86-87. doi:10.1039/b311652b.


Cite as: https://hdl.handle.net/21.11116/0000-0001-EE4B-0
Abstract
Cytochrome p450(BioI)(CYP107H1) is believed to supply pimelic acid equivalents for biotin biosynthesis in Bacillus subtilis: we report here that the mechanistic pathway adopted by this multifunctional p450 for the in-chain cleavage of fatty acids is via consecutive formation of alcohol and threo-diol intermediates, with the likely absolute configuration of the intermediates also reported.