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Mechanism of Enzymatic Birch Reduction: Stereochemical Course and Exchange Reactions of Benzoyl-CoA Reductase

Lookup NU author(s): Professor Bernard Golding

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Abstract

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


Publication metadata

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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