Respiratory Complex I: Structure, Redox Components, and Possible Mechanisms of Energy Transduction

A. D. Vinogradov

Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-3955; E-mail: adv@biochem.bio.msu.su

Received May 18, 2001

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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.

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KEY WORDS: NADH:quinone oxidoreductase, Complex I, respiratory chain, proton translocation, electrochemical coupling

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