Ad. Vinogradov, Respiratory Complex I: Structure, redox components, and possible mechanisms of energy transduction, BIOCHEM-MOS, 66(10), 2001, pp. 1086-1097
Structural arrangements and properties of redox components of the mitochond
rial and bacterial proton-translocating NADH:quinone oxidoreductases are br
iefly described. A model for the mechanism of proton translocation at first
coupling site, which emphasizes participation of specifically Complex 1-as
sociated ubisemiquinones, is discussed, Ail alternative mechanism is propos
ed where all redox reactions take place in a hydrophilic part of the enzyme
and the free energy accumulated as conformational constraint drives the pr
oton pump associated with the hydrophobic polypeptides.