Transient-State Reduction and Steady-State Kinetic Studies of Menaquinol Oxidase from Bacillus subtilis, Cytochrome aa3-600 nm. Spectroscopic Characterization of the Steady-State Species
Author:
Affiliation:
1. Department of Biochemistry, Queen's University, Kingston, Ontario K7L 3N6, Canada
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi011116q
Reference35 articles.
1. Evolution of the Cytochrome c Oxidase Proton Pump
2. CYTOCHROME C OXIDASE: Structure and Spectroscopy
3. X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
4. Bacillus subtilis expresses two kinds of haem-A-containing terminal oxidases
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1. Structure of the cytochromeaa3-600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site;Proceedings of the National Academy of Sciences;2019-12-30
2. Exposure of Bacillus subtilis to silver inhibits activity of cytochrome c oxidase in vivo via interaction with SCO, the CuA assembly protein;Metallomics;2018
3. Plasticity in the High Affinity Menaquinone Binding Site of the Cytochrome aa3-600 Menaquinol Oxidase from Bacillus subtilis;Biochemistry;2015-08-06
4. Resolving protein-semiquinone interactions by two-dimensional ESEEM spectroscopy;Electron Paramagnetic Resonance;2012
5. The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2010-12
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