期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1787, 期 10, 页码 1266-1271出版社
ELSEVIER
DOI: 10.1016/j.bbabio.2009.05.001
关键词
Complex I; NADH dehydrogenase; Iron-sulfur cluster; Electron transfer; Redox potential; Poisson-Boltzmann equation
资金
- NSF [PHY 0646273]
- NIH [GM54052]
- Russian Foundation for Fundamental Research [08-03-00094-a]
Respiratory complex I couples the transfer of electrons from NADH to ubiquinone and the translocation of protons across the mitochondrial membrane. A detailed understanding of the midpoint reduction potentials (E-m) of each redox center and the factors which influence those potentials are critical in the elucidation of the mechanism of electron transfer in this enzyme. We present accurate electrostatic interaction energies for the iron-sulfur (FeS) clusters of complex I to facilitate the development of models and the interpretation of experiments in connection to electron transfer (ET) in this enzyme. To calculate redox titration curves for the FeS clusters it is necessary to include interactions between clusters,which in turn can be used to refine E-m values and validate spectroscopic assignments of each cluster. Calculated titration curves for clusters N4, N5, and N6a are discussed. Furthermore, we present some initial findings on the electrostatics of the redox centers of complex I under the influence of externally applied membrane potentials. A means of determining the location of the FeS cofactors within the holo-complex based on electrostatic arguments is proposed. A simple electrostatic model of the protein/membrane system is examined to illustrate the viability of our hypothesis. (C) 2009 Elsevier B.V. All rights reserved.
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