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Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8884-9.

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.

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  • 1Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, D-82152 Martinsried, Germany. dobbek@biochem.mpg.de

Abstract

CO dehydrogenase from the aerobic bacterium Oligotropha carboxidovorans catalyzes the oxidation of CO with H(2)O, yielding CO(2), two electrons, and two H(+). Its crystal structure in the air-oxidized form has been determined to 2.2 A. The active site of the enzyme, which contains molybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotide and S-selanylcysteine, delivers the electrons to an intramolecular electron transport chain composed of two types of [2Fe-2S] clusters and flavin-adenine dinucleotide. CO dehydrogenase is composed of an 88.7-kDa molybdoprotein (L), a 30. 2-kDa flavoprotein (M), and a 17.8-kDa iron-sulfur protein (S). It is organized as a dimer of LMS heterotrimers and resembles xanthine dehydrogenase/oxidase in many, but not all, aspects. A mechanism based on a structure with the bound suicide-substrate cyanide is suggested and displays the necessity of S-selanylcysteine for the catalyzed reaction.

PMID:
10430865
[PubMed - indexed for MEDLINE]
PMCID:
PMC17702
Free PMC Article
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