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: http://www.biochem.bio.msu.ru/publications/publication.php?pubmedID=18471432
Дата изменения: Unknown Дата индексирования: Sun Feb 3 00:03:18 2013 Кодировка: |
Title: | NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I). |
Authors: | Vinogradov AD |
Publication: | Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):729-34. doi: 10.1016/j.bbabio.2008.04.014. Epub 2008 Apr 18. |
PubmedID | 18471432 |
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. |