A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters

Tyler L. Grove, Jessica H. Ahlum, Priya Sharma, Carsten Krebs, Squire J. Booker

Research output: Contribution to journalArticle

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BtrN catalyzes the two-electron oxidation of the C3 secondary alcohol of 2-deoxy-scyllo-inosamine to the corresponding ketone and is a member of a subclass of radical S-adenosylmethionine (SAM) enzymes called radical SAM (RS) dehydrogenases. Like all RS enzymes, BtrN contains a [4Fe-4S] cluster that delivers an electron to SAM, inducing its cleavage to the common intermediate in RS reactions, the 5′-deoxyadenosyl 5′-radical. In this work, we show that BtrN contains an additional [4Fe-4S] cluster, thought to bind in contact with the substrate to facilitate loss of the second electron in the two-electron oxidation.

Original languageEnglish (US)
Pages (from-to)3783-3785
Number of pages3
Issue number18
Publication statusPublished - May 11 2010


All Science Journal Classification (ASJC) codes

  • Biochemistry

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