Ortwin Meyer
University of Bayreuth
63 Papers
767 Citations
Ortwin Meyer is an academic researcher from University of Bayreuth. The author has contributed to research in topics: Carbon monoxide dehydrogenase & Oligotropha carboxidovorans. The author has an hindex of 33, co-authored 63 publications. Previous affiliations of Ortwin Meyer include Max Planck Society.
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Papers
Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
TL;DR: The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor.
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A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans
Vitali Svetlitchnyi,Holger Dobbek,Wolfram Meyer-Klaucke,Thomas Meins,Bärbel Thiele,Piero Römer,Robert Huber,Ortwin Meyer +7 more
TL;DR: The functional cluster A of ACS(Ch) contains a Ni-Ni-[4Fe-4S] site, in which the positions proximal and distal to the cubane are occupied by Ni ions, which is apparent from a positive correlation of the Ni contents and negative correlations of the Cu or Zn contents with the acetyl-CoA/CO exchange activities of different preparations of monomeric ACS.
289
Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.
TL;DR: 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.
247
N2 Fixation by Streptomyces thermoautotrophicus Involves a Molybdenum-Dinitrogenase and a Manganese-Superoxide Oxidoreductase That Couple N2Reduction to the Oxidation of Superoxide Produced from O2by a Molybdenum-CO Dehydrogenase
TL;DR: Among the most striking properties of the S. thermoautotrophicus nitrogenase system are the dependence on O2 and O·̄2, the complete insensitivity of all components involved toward O 2 and H2O2,The inability to reduce ethine or ethene, and a low MgATP requirement.
198
A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.
TL;DR: The structurally characterized molybdoenzyme carbon monoxide dehydrogenase (CODH) catalyzes the oxidation of CO to CO2 in the aerobic bacterium Oligotropha carboxidovorans and demonstrates that Se is coordinated by two C atoms at 1.94-1.95 A distance, interpreted as a replacement of the S in methionine residues.
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