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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Complete nucleotide sequence of the circular megaplasmid pHCG3 of Oligotropha carboxidovorans: function in the chemolithoautotrophic utilization of CO, H2 and CO2
TL;DR: Sequence comparisons of pHCG3-encoded genes suggest that major genetic exchange between O. carboxidovorans and the proteobacteria has occurred, and a putative system of global regulation of plasmid replication in O.carboxidotrophy has occurred.
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The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.
Ortwin Meyer,Lothar Gremer,Reinhold Ferner,Marion Ferner,Holger Dobbek,Manuel Gnida,Wolfram Meyer-Klaucke,Robert Huber +7 more
TL;DR: CO dehydrogenase is a selenium-containing molybdo-iron-sulfur-flavoenzyme, which has been crystallized and structurally characterized in its oxidized state from the aerobic CO utilizing bacteria Oligotropha carboxidovorans and Hydrogenophaga pseudoflava.
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Chemolithoautotrophic assimilation of dinitrogen by Streptomyces thermoautotrophicus UBT1: identification of an unusual N2-fixing system.
TL;DR: The N2-fixing system of S. thermoautotrophicus exhibited several properties not apparent in the diazotrophic bacteria studied so far, since it was incapable of reducing acetylene to ethylene or ethane and resistant to inhibition by acetylene or Ethylene, CO, CO or CO2, or H2.
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Isolation and characterization of a second molybdopterin dinucleotide: molybdopterin cytosine dinucleotide.
TL;DR: The fact that molybdoenzyme CO dehydrogenase pterin cytosine dinucleotide and molybdopterin guanine din nucleotide contain molyBDopterin in their structure shows that the pterIn moiety, with its unique dithiolene-containing sidechain, is a structural element which is common to the organic portion of themolybdenum cofactors of many molyBdoenzymes.
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Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria
TL;DR: The N-terminal sequences of CO dehydrogenase structural genes were found to be conserved among carboxydotrophic bacteria of distinct taxonomic position, independent of the presence of plasmids.