NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I).
The 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.
Vinogradov
Andrei D
AD
Department of Biochemistry, School of Biology, Moscow State University, Moscow 119992, Russian Federation. adv@biochem.bio.msu.su
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D042967:Electron Transport Complex I / Q000378:metabolism*; D004734:Energy Metabolism; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D009243:NAD / Q000378:metabolism*; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D013367:Submitochondrial Particles / Q000201:enzymology
D001426:Bacterial Proteins; D009243:NAD; D042967:Electron Transport Complex I