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Journal article

Selective aliphatic carbon-hydrogen bond activation of protected alcohol substrates by cytochrome P450 enzymes.

Abstract:

Protected cyclohexanol and cyclohex-2-enol substrates, containing benzyl ether and benzoate ester moieties, were designed to fit into the active site of the Tyr96Ala mutant of cytochrome P450cam. The protected cyclohexanol substrates were efficiently and selectively hydroxylated by the mutant enzyme at the trans C-H bond of C-4 on the cyclohexyl ring. The selectivity of oxidation of the benzoate ester protected cyclohexanol could be altered by making alternative amino acid substitutions in th...

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Publication status:
Published

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Publisher copy:
10.1039/c3ob42417k

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
Publisher:
Royal Society of Chemistry
Journal:
Organic and biomolecular chemistry More from this journal
Volume:
12
Issue:
15
Pages:
2479-2488
Publication date:
2014-04-01
DOI:
EISSN:
1477-0539
ISSN:
1477-0520
Language:
English
Keywords:
Pubs id:
pubs:459685
UUID:
uuid:1b5652b4-29d8-4c7b-adf6-6c8c1a3cc388
Local pid:
pubs:459685
Source identifiers:
459685
Deposit date:
2014-06-16

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