Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8299136 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2008 | 6 Pages |
Abstract
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.
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Authors
Andrei D. Vinogradov,