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J. Biol. Chem., Vol. 279, Issue 48, 50391-50400, November 26, 2004

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Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase^*

Lodovica Loschi, Stephen J. Brokx, Tanya L. Hills, Glen Zhang, Michela G. Bertero¶, Andrew L. Lovering||, Joel H. Weiner**, and Natalie C. J. Strynadka, Canadian Institutes of Health Research Scientist and Howard Hughes Medical Institute International Scholar

From the Department of Biochemistry, University of British Columbia, Vancouver British Columbia V6T 1Z3 and Canadian Institutes of Health Research Membrane Protein Research Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

By using a bioinformatics screen of the Escherichia coli genome for potential molybdenum-containing enzymes, we have identified a novel oxidoreductase conserved in the majority of Gram-negative bacteria. The identified operon encodes for a proposed heterodimer, YedYZ in Escherichia coli, consisting of a soluble catalytic subunit termed YedY, which is likely anchored to the membrane by a heme-containing trans-membrane subunit termed YedZ. YedY is uniquely characterized by the presence of one molybdenum molybdopterin not conjugated by an additional nucleotide, and it represents the only molybdoenzyme isolated from E. coli characterized by the presence of this cofactor form. We have further characterized the catalytic subunit YedY in both the molybdenum- and tungsten-substituted forms by using crystallographic analysis. YedY is very distinct in overall architecture from all known bacterial reductases but does show some similarity with the catalytic domain of the eukaryotic chicken liver sulfite oxidase. However, the strictly conserved residues involved in the metal coordination sphere and in the substrate binding pocket of YedY are strikingly different from that of chicken liver sulfite oxidase, suggesting a catalytic activity more in keeping with a reductase than that of a sulfite oxidase. Preliminary kinetic analysis of YedY with a variety of substrates supports our proposal that YedY and its many orthologues may represent a new type of membrane-associated bacterial reductase.

Received for publication, August 4, 2004 , and in revised form, August 30, 2004.

The atomic coordinates and structure factors (codes 1XDQ and 1XDY) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the National Institutes of Health, the Canadian Institutes of Health Research, and the Howard Hughes Medical Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Canadian Institutes of Health Research fellow.

^|| Michael Smith Foundation for Health Research postdoctoral fellow.

^** Hold the Canada Research Chair in Membrane Biochemistry.

To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of British Columbia, 2146 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada. Tel.: 604-822-0789; Fax: 604-822-5227; E-mail: natalie{at}byron.biochem.ubc.ca.

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