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Biochemistry (Mosc). 2001 Oct;66(10):1086-97.

Respiratory complex I: structure, redox components, and possible mechanisms of energy transduction.

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1
Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. adv@biochem.bio.msu.su

Abstract

Structural arrangements and properties of redox components of the mitochondrial and bacterial proton-translocating NADH:quinone oxidoreductases are briefly described. A model for the mechanism of proton translocation at first coupling site, which emphasizes participation of specifically Complex I-associated ubisemiquinones, is discussed. An alternative mechanism is proposed where all redox reactions take place in a hydrophilic part of the enzyme and the free energy accumulated as conformational constraint drives the proton pump associated with the hydrophobic polypeptides.

PMID:
11736630
[Indexed for MEDLINE]
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