Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1777, Issue 7-8, Pages 729-734Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2008.04.014
Keywords
bioenergetics; respiration; mitochondria; complex I; nucleotide binding
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Funding
- FIC NIH HHS [R03 TW007825, R03 TW007825-01, R03 TW007825-02, R03 TW07825] Funding Source: Medline
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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. (c) 2008 Elsevier B.V. All rights reserved.
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