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NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I) Vinogradov ADBiochim Biophys Acta 2008[Jul]; 1777 (7-8): 729-34The quantitative data on the binding affinity of NADH, NAD(+), and their analogues for complex I as emerged from the steady-state kinetics data and from more direct studies under equilibrium conditions are summarized and discussed. The redox-dependency of the nucleotide binding and the reductant-induced change of FMN affinity to its tight non-covalent binding site indicate that binding (dissociation) of the substrate (product) may energetically contribute to the proton-translocating activity of complex I.|Animals[MESH]|Bacterial Proteins/metabolism[MESH]|Electron Transport Complex I/*metabolism[MESH]|Energy Metabolism[MESH]|Kinetics[MESH]|Mitochondria/*enzymology[MESH]|NAD/*metabolism[MESH]|Oxidation-Reduction[MESH]|Oxygen Consumption[MESH]|Submitochondrial Particles/enzymology[MESH] |
