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9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.

Abstract:

Biotin synthase catalyzes formation of the thiophane ring through stepwise substitution of a sulfur atom for hydrogen atoms at the C9 and C6 positions of dethiobiotin. Biotin synthase is a radical S-adenosylmethionine (SAM) enzyme that reductively cleaves S-adenosylmethionine, generating 5'-deoxyadenosyl radicals that initially abstract a hydrogen atom from the C9 position of dethiobiotin. We have proposed that the resulting dethiobiotinyl radical is quenched by the μ-sulfide of the nearby [2...

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Publication status:
Published

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Publisher copy:
10.1021/ja3012963

Authors


Fugate, CJ More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Journal:
Journal of the American Chemical Society
Volume:
134
Issue:
22
Pages:
9042-9045
Publication date:
2012-06-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:1db120e1-1ebc-45e2-8a85-6b0b0f23bd66
Source identifiers:
428056
Local pid:
pubs:428056

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