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Lookup NU author(s): Emeritus Professor Bernard Golding
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Dearomatizing benzoyl-coenzyme A reductases (BCR) from facultatively anaerobic bacteria are key enzymes in the anaerobic degradation of aromatic compounds. They catalyze the ATP-dependent reduction of benzoyl-CoA (BCoA) to cyclohexa-1,5-diene-1-carboxyl-CoA (dienoyl-CoA). A Birch reduction mechanism involving alternate electron transfer and protonation steps has been proposed for BCR. In this work we reacted BCoA in H2O and D2O, and d(5)-BCoA in H2O with BCR and the second enzyme of the pathway, dienoyl-CoA hydratase (DCH). The 1,4 hydration product formed from the dienoyl-CoA, 6-hydroxycyclohex-1-ene-1-carbonyl-CoA, was analyzed by several NMR techniques. The results obtained indicate that BCR stereoselectively forms the trans-dienoyl-CoA product, and DCH stereoselectively catalyzes a trans-1,4 water addition. Moreover, unexpected proton exchanges at C-2 and C-6 were observed. They indicate that a free
Author(s): Thiele B, Rieder O, Golding BT, Müller M, Boll M
Publication type: Article
Publication status: Published
Journal: Journal of the American Chemical Society
Year: 2008
Volume: 130
Issue: 43
Pages: 14050-14051
ISSN (print): 0002-7863
ISSN (electronic): 1943-2984
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/ja805091w
DOI: 10.1021/ja805091w
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