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Science 28 February 1997:
Vol. 275. no. 5304, pp. 1305 - 1308
DOI: 10.1126/science.275.5304.1305
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Reports

Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster

Jeffrey C. Boyington, Vadim N. Gladyshev, * Sergei V. Khangulov, Thressa C. Stadtman, Peter D. Sun dagger

Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alpha beta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer.

J. C. Boyington and P. D. Sun, Structural Biology Section, Laboratory of Molecular Structure, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), 12441 Parklawn Drive, Rockville, MD 20852, USA.
V. N. Gladyshev and T. C. Stadtman, Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, NIH, 9000 Rockville Pike, Bethesda, MD 20892, USA.
S. V. Khangulov, Department of Chemistry, Hoyt Laboratory, Princeton University, Princeton, NJ 08544, USA.
*   Present address: Basic Research Laboratory, National Cancer Institute, NIH, 9000 Rockville Pike, Bethesda, MD 20892, USA.

dagger    To whom correspondence should be addressed.

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