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.

深入了解哺乳动物呼吸复合物定义了变构蛋白相互作用在其质子动力活动中的作用。

在细胞色素c氧化酶 (CxIV) 中，亚基 I 的构象变化由 O ₂与血红素 a ₃ ²⁺ -Cu _B ^{+ 结合}并还原，以及与血红素a和 Cu _{A 的}氧化/还原耦合的立体化学转变以及静电效应引起，确定质子泵活动。

在泛醌-细胞色素c氧化还原酶 (CxIII) 中，Fe-S 蛋白在细胞色素b和c ₁之间的构象运动是质子驱动活性的关键因素。

在 NADH-泛醌氧化还原酶 (CxI) 中，泛醌结合和还原导致醌反应结构中亚基的构象变化，从而引发质子泵。