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Gerhard Buse

Researcher at RWTH Aachen University

Publications -  79
Citations -  3702

Gerhard Buse is an academic researcher from RWTH Aachen University. The author has contributed to research in topics: Cytochrome c oxidase & Cytochrome c. The author has an hindex of 33, co-authored 79 publications receiving 3648 citations. Previous affiliations of Gerhard Buse include Max Planck Society.

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Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus

TL;DR: The crystal structure of the ba3‐cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 Å resolution and the discovery of a novel subunit IIa is led to the identification of sequence motifs and residues that seem to be indispensable for the function of the haem copper oxidases.
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A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

TL;DR: Simulations of the EPR spectra indicated that Cu-Cu interaction, in a mixed-valence [Cu(1.5) ... Cu(1/2)], S = 1/2 site is consistent with, if not proof of, the unusual spectral features observed for N2OR and COX.
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Inhibition of cytochrome c oxidase function by dicyclohexylcarbodiimide.

TL;DR: Dicyclohexylcarbodiimide reacted with beef heart cytochrome c oxidase in inhibit the proton-pumping function of this enzyme and to a lesser extent to inhibit electron transfer.
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Cytochrome c oxidase is three-copper, two-heme-A protein

TL;DR: Metal contents of preparations of procaryotic and eucaryotic cytochrome c oxidases have been determined by inductively coupled plasma atomic emission spectroscopy and shown to be stoichiometrically related to the protein contents.
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The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: Evolutionary implications

TL;DR: The findings support the hypothesis of a common phylogeny of aerobic respiration and bacterial denitrification, which was proposed on the basis of structural similarities between the Pseudomonas stutzeri NO reductase and the cbb(3) terminal oxidases, by suggesting a mechanism consistent with the stoichiometry of the overall reaction.