An allylic ketyl radical intermediate in clostridial amino-acid fermentation

Jihoe Kim, Daniel J. Darley, Wolfgang Buckel and Antonio J. Pierik ()
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Jihoe Kim: Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität
Daniel J. Darley: Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität
Wolfgang Buckel: Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität
Antonio J. Pierik: Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität

Nature, 2008, vol. 452, issue 7184, 239-242

Abstract: C. difficile's radical solution In the human gut the bacterium Clostridium difficile, a common cause of hospital acquired infection worldwide, utilizes L-leucine as both oxidant and reductant. The fermentation involves a chemically demanding dehydration, catalysed by an iron–sulphur cluster-containing dehydratase, and thought to involve ketyl radicals. This suspicion has been confirmed with the identification of a product-related allylic ketyl radical bound to the dehydratase. The radical enzymes described previously require radical generators such as coenzyme B12, S-adenosylmethionine or oxygen. Such assistance is not necessary for the C. difficile 2-hydroxyacyl-CoA dehydratase, making this enzyme unprecedented in biochemistry. Similar enzymes might be found in other bacteria growing anaerobically.

Date: 2008
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DOI: 10.1038/nature06637

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