Oliver Maneg
Goethe University Frankfurt
9 Papers
243 Citations
Oliver Maneg is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Thermus thermophilus & Cytochrome C1. The author has an hindex of 7, co-authored 8 publications. Previous affiliations of Oliver Maneg include Aventis Pharma.
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Papers
Interaction of cytochrome c with cytochrome oxidase: two different docking scenarios.
TL;DR: Recent results obtained from bacterial cytochrome c oxidases from both Paracoccus denitrificans, in which the primary electrostatic encounter most closely matches the mitochondrial situation, and the Thermus thermophilus ba(3) oxidase in which docking and electron transfer is predominantly based on hydrophobic interactions.
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The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach
Lucia Muresanu,Primoz Pristovsek,Frank Löhr,Oliver Maneg,Marco D. Mukrasch,Heinz Rüterjans,Bernd Ludwig,Christian Lücke +7 more
TL;DR: The chemical shift analysis performed for both redox states provided a topological description of the contact surface on each partner molecule, suggesting that alterations of the electron distribution in the porphyrin ring due to formation of the protein-protein complex are apparently sensed even beyond the heme propionate groups.
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Different Interaction Modes of Two Cytochrome-c Oxidase Soluble CuA Fragments with Their Substrates
TL;DR: The results indicate that the soluble CuA domains are excellent models for the initial electron transfer processes in cytochrome-c oxidase, and particularly in Thermus thermophilus and P. denitrificans.
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Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Hans Wienk,Oliver Maneg,Christian Lücke,Primoz Pristovsek,Frank Löhr,Bernd Ludwig,Heinz Rüterjans +6 more
TL;DR: The detected contact areas on the cytochrome c(552) surface were comparable under both fully reduced and fully oxidized conditions, suggesting that the respective chemical shift changes represent biologically relevant protein-protein interactions.
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A four-subunit cytochrome bc(1) complex complements the respiratory chain of Thermus thermophilus.
Daniela Mooser,Oliver Maneg,Oliver Maneg,Carsten Corvey,Thomas Steiner,Francesco Malatesta,Michael Karas,Tewfik Soulimane,Bernd Ludwig +8 more
TL;DR: In this article, it was shown that four consecutive genes encoding cytochrome bc(1) subunits are organized in an operon-like structure termed fbcCXFB.
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