O
Ortwin Meyer
Researcher at University of Bayreuth
Publications - 63
Citations - 4013
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 receiving 3724 citations. Previous affiliations of Ortwin Meyer include Max Planck Society.
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Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster
TL;DR: This structure represents the prototype for Ni-containing CO dehydrogenases from anaerobic bacteria and archaea and contains five metal clusters of which clusters B, B′, and a subunit-bridging, surface-exposed cluster D are cubane-type [4Fe-4S] clusters.
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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.
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Biology of Aerobic Carbon Monoxide-Oxidizing Bacteria
Ortwin Meyer,Hans G. Schlegel +1 more
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Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans.
TL;DR: Two monofunctional NiFeS carbon monoxide (CO) dehydrogenases, designated CODH I andCODH II, were purified to homogeneity from the anaerobic CO-utilizing eubacterium Carboxydothermus hydrogenoformans and it is proposed that CODh I is involved in energy generation and that C ODH II serves in anabolic functions.