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An allylic ketyl radical intermediate in clostridial amino-acid fermentation

Author

Listed:
  • Jihoe Kim

    (Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität)

  • Daniel J. Darley

    (Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität
    Present address: Department of Pharmacy and Pharmacology, University of Bath, Claverton Down, Bath BA2 7AY, UK.)

  • Wolfgang Buckel

    (Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität)

  • Antonio J. Pierik

    (Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität)

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.

Suggested Citation

  • Jihoe Kim & Daniel J. Darley & Wolfgang Buckel & Antonio J. Pierik, 2008. "An allylic ketyl radical intermediate in clostridial amino-acid fermentation," Nature, Nature, vol. 452(7184), pages 239-242, March.
    • Handle: RePEc:nat:nature:v:452:y:2008:i:7184:d:10.1038_nature06637
    DOI: 10.1038/nature06637
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