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Vitali Svetlitchnyi

Researcher at University of Bayreuth

Publications -  8
Citations -  1203

Vitali Svetlitchnyi is an academic researcher from University of Bayreuth. The author has contributed to research in topics: Carboxydothermus hydrogenoformans & Carbon monoxide dehydrogenase. The author has an hindex of 6, co-authored 6 publications receiving 1078 citations.

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Journal ArticleDOI

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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A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans

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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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.
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Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

TL;DR: It is suggested that the C-terminal domain of the large subunit is the mobile element that allows the necessary interaction of CoFeSPCh with the active site of ACSCh and the methyltetrahydrofolate carrying MeTr.
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Carbon Monoxide Induced Decomposition of the Active Site [Ni-4Fe-5S] Cluster of CO Dehydrogenase

TL;DR: The CO oxidation activity of CODHII(Ch) is determined under different conditions of crystallization, prepared crystals of the enzyme in the presence of dithiothreitol or dithionite as reducing agents under an atmosphere of N(2) or CO, and solved the corresponding structures.