NMR Reveals Double Occupancy of Quinone-type Ligands in the Catalytic Quinone Binding Site of the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
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3. Oxidant-induced formation of a neutral flavosemiquinone in the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae;Tao;Biochim. Biophys. Acta,2008
4. Localization and function of the membrane-bound riboflavin in the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae;Casutt;J. Biol. Chem,2010
5. Redox properties of the prosthetic groups of Na+-translocating NADH:quinone oxidoreductase. 2. Study of the enzyme by optical spectroscopy;Bogachev;Biochemistry,2009
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1. Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy;Methods in Molecular Biology;2022-10-01
2. Identification of the riboflavin cofactor-binding site in the Vibrio cholerae ion-pumping NQR complex: A novel structural motif in redox enzymes;Journal of Biological Chemistry;2022-08
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4. The side chain of ubiquinone plays a critical role in Na+ translocation by the NADH-ubiquinone oxidoreductase (Na+-NQR) from Vibrio cholerae;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2022-06
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