Identification of the Nitrogen Donor Hydrogen Bonded with the Semiquinone at the QH Site of the Cytochrome bo3 from Escherichia coli-Reference-Cited by-同舟云学术

Identification of the Nitrogen Donor Hydrogen Bonded with the Semiquinone at the QH Site of the Cytochrome bo3 from Escherichia coli

Published:2008-11-05 Issue:47 Volume:130 Page:15768-15769
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lin Myat T.¹,Samoilova Rimma I.¹,Gennis Robert B.¹,Dikanov Sergei A.¹

Affiliation:

1. Departments of Biophysics and Computational Biology, Biochemistry, and Veterinary Clinical Medicine, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801, and Institute of Chemical Kinetics and Combustion, Russian Academy of Sciences, Novosibirsk 630090, Russia

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja805906a

Reference14 articles.

1. Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers

2. Identification of the Residues Involved in Stabilization of the Semiquinone Radical in the High-Affinity Ubiquinone Binding Site in Cytochrome bo3 from Escherichia coli by Site-Directed Mutagenesis and EPR Spectroscopy

3. Direct Evidence for the Protonation of Aspartate-75, Proposed To Be at a Quinol Binding Site, upon Reduction of Cytochrome bo3 from Escherichia coli

4. Vibrational Modes of Ubiquinone in Cytochrome bo3 from Escherichia coli Identified by Fourier Transform Infrared Difference Spectroscopy and Specific 13C Labeling

5. QH•- Ubisemiquinone Radical in the bo3-Type Ubiquinol Oxidase Studied by Pulsed Electron Paramagnetic Resonance and Hyperfine Sublevel Correlation Spectroscopy

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