Resonance Raman Characterization of the Ammonia-Generated Oxo Intermediate of Cytochrome c Oxidase from Paracoccus denitrificans
Author:
Affiliation:
1. Technische Universität Berlin, Institut fuer Chemie, Strasse des 17. Juni 135, 10623 Berlin, Germany
2. Max Planck Institut für Biophysik, Abteilung Molekulare Membranbiologie, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi400535m
Reference26 articles.
1. Cytochrome c oxidase: exciting progress and remaining mysteries
2. Energy Transduction: Proton Transfer Through the Respiratory Complexes
3. Active site intermediates in the reduction of O2 by cytochrome oxidase, and their derivatives
4. Formation and reduction of a ‘peroxy’ intermediate of cytochrome c oxidase by hydrogen peroxide
5. The Interaction of Cytochrome Oxidase with Hydrogen Peroxide: The Relationship of Compounds P and F
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2. Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy;Frontiers in Molecular Biosciences;2022-06-13
3. Quantification of Local Electric Field Changes at the Active Site of Cytochrome c Oxidase by Fourier Transform Infrared Spectroelectrochemical Titrations;Frontiers in Chemistry;2021-04-27
4. A Resonance Raman Marker Band Characterizes the Slow and Fast Form of Cytochrome c Oxidase;Journal of the American Chemical Society;2021-02-09
5. In Escherichia coli Ammonia Inhibits Cytochrome bo3 But Activates Cytochrome bd-I;Antioxidants;2020-12-25
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