The allosteric protein interactions in the proton-motive function of mammalian redox enzymes of the respiratory chain

Abstract

Insight into mammalian respiratory complexes defines the role of allosteric protein interactions in their proton-motive activity. In cytochrome c oxidase (CxIV) conformational change of subunit I, caused by O₂ binding to heme a₃²⁺-Cu_B⁺ and reduction, and stereochemical transitions coupled to oxidation/reduction of heme a and Cu_A, combined with electrostatic effects, determine the proton pumping activity. In ubiquinone-cytochrome c oxidoreductase (CxIII) conformational movement of Fe-S protein between cytochromes b and c₁ is the key element of the proton-motive activity. In NADH-ubiquinone oxidoreductase (CxI) ubiquinone binding and reduction result in conformational changes of subunits in the quinone reaction structure which initiate proton pumping.

Keywords: Allosteric protein interactions; Mitochondria; Proton energy conversion; Proton-motive activity; Redox enzyme complexes; Respiratory chain.