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Selective oxidative demethylation of veratric acid to vanillic acid by CYP199A4 from Rhodopseudomonas palustris HaA2.

Abstract:

CYP199A4 (RPB3613) from Rhodopseudomonas palustris HaA2 is a heme monooxygenase that catalyzes the hydroxylation of para-substituted benzoic acids. Monooxygenase activity of CYP199A4 can be reconstituted in a Class I electron transfer chain with an associated [2Fe-2S] ferredoxin, HaPux, (RPB3614) and the flavin-dependent reductase, HaPuR, (RPB3656) that is not associated with a CYP gene. CYP199A4 and the ferredoxin HaPux are produced in greater quantities using recombinant Escherichia coli ex...

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Publication status:
Published

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Publisher copy:
10.1039/b913487e

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Molecular bioSystems
Volume:
6
Issue:
1
Pages:
206-214
Publication date:
2010-01-05
DOI:
EISSN:
1742-2051
ISSN:
1742-206X
URN:
uuid:de89f850-e7f0-4a56-abe9-912623267280
Source identifiers:
35029
Local pid:
pubs:35029

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