JB Accepts, published online ahead of print on 6 November 2009

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J. Bacteriol. doi:10.1128/JB.01125-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Identification and Characterization of a Novel Member of the Radical AdoMet Enzyme Superfamily and Implications for the Biosynthesis of the Hmd Hydrogenase Active Site Cofactor

Shawn E. McGlynn, Eric S. Boyd, Eric M. Shepard, Rachel Lange, Robin Gerlach, Joan B. Broderick, and John W. Peters^*

Department of Chemistry and Biochemistry and Astrobiology Biogeocatalysis Research Center, Department of Chemical and Biological Engineering, Montana State University, Bozeman, Montana 59717

^* To whom correspondence should be addressed. Email: john.peters{at}chemistry.montana.edu.

The genetic context, phylogeny, and biochemistry of a gene flanking the H₂-forming methylene-H₄MPT hydrogenase gene (hmdA), designated here as hmdB, indicate that it is a new member of the radical S-adenosylmethionine enzyme superfamily. In contrast to the characteristic CX_3-4CX₂C motif defining this family, HmdB contains a unique CX₅CX₂C motif.