Role of a bound ubiquinone on reactions of theEscherichia colicytochromebowith ubiquinol and dioxygen
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(99)01007-8/fullpdf
Reference22 articles.
1. The happy family of cytochrome oxidases
2. Properties of the two terminal oxidases of Escherichia coli
3. Identification of the ubiquinol-binding site in the cytochrome bo3-ubiquinol oxidase of Escherichia coli.
4. Using Matrix-Assisted Laser Desorption Ionization Mass Spectrometry To Map the Quinol Binding Site of Cytochrome bo3 from Escherichia coli
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1. Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli;Journal of the American Chemical Society;2017-06-06
2. Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2017-05
3. Single Proteoliposomes with E. coli Quinol Oxidase: Proton Pumping without Transmembrane Leaks;Israel Journal of Chemistry;2017-02-10
4. Q-Band Electron-Nuclear Double Resonance Reveals Out-of-Plane Hydrogen Bonds Stabilize an Anionic Ubisemiquinone in Cytochrome bo3 from Escherichia coli;Biochemistry;2016-09-28
5. Exploring by Pulsed EPR the Electronic Structure of Ubisemiquinone Bound at the QH Site of Cytochrome bo3 from Escherichia coli with in Vivo 13C-Labeled Methyl and Methoxy Substituents;Journal of Biological Chemistry;2011-03
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