Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/75465
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Type: Journal article
Title: Selective oxidative demethylation of veratric acid to vanillic acid by CYP199A4 from Rhodopseudomonas palustris HaA2
Author: Bell, S.
Tan, A.
Johnson, E.
Wong, L.
Citation: Molecular BioSystems, 2010; 6(1):206-214
Publisher: Royal Society of Chemistry
Issue Date: 2010
ISSN: 1742-2051
1742-2051
Statement of
Responsibility: 
Stephen G. Bell, Adrian B. H. Tan, Eachan O. D. Johnson and Luet-Lok Wong
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 expression systems when compared to the equivalent proteins in the closely related CYP199A2-Pux-PuR Class I system from R. palustris CGA009. HaPuR and HaPux can also replace PuR and Pux in supporting the CYP199A2 enzyme turnover with high activity. Whole-cell in vivo substrate oxidation systems for CYP199A4 and CYP199A2 with HaPux and HaPuR as the electron transfer proteins have been constructed. These E. coli systems were capable of selectively demethylating veratric acid at the para position to produce vanillic acid at rates of up to 15.3 microM (g-cdw)(-1) min(-1) and yields of up to 1.2 g L(-1).
Keywords: Rhodopseudomonas; Escherichia coli; Vanillic Acid; Mixed Function Oxygenases; Bacterial Proteins; Ferredoxins; Methylation; Kinetics
Rights: Copyright status unknown
RMID: 0020121277
DOI: 10.1039/B913487E
Appears in Collections:Chemistry publications

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