Wikström M K, Saari H T
Biochim Biophys Acta. 1977 Nov 17;462(2):347-61. doi: 10.1016/0005-2728(77)90133-5.
Oxidation of ferrocytochrome c by molecular oxygen catalysed by cytochrome c oxidase (cytochrome aa3) is coupled to translocation of H+ ions across the mitochondrial membrane. The proton pump is an intrinsic property of the cytochrome c oxidase complex as revealed by studies with phospholipid vesicles inlayed with the purified enzyme. As the conformation of cytochrome aa3 is specifically sensitive to the electrochemical proton gradient across the mitochondrial membrane, it is likely that redox energy is primarily conserved as a conformational "strain" in the cytochrome aa3 complex, followed by relaxation linked to proton translocation. Similar principles of energy conservation and transduction may apply on other respiratory chain complexes and on mitochondrial ATP synthase.
细胞色素c氧化酶(细胞色素aa3)催化分子氧将亚铁细胞色素c氧化,这一过程与氢离子跨线粒体膜的转运相偶联。质子泵是细胞色素c氧化酶复合物的固有特性,这一点已通过对嵌入纯化酶的磷脂囊泡的研究得以揭示。由于细胞色素aa3的构象对跨线粒体膜的电化学质子梯度具有特异性敏感性,氧化还原能量很可能主要以细胞色素aa3复合物中的构象“应变”形式得以保存,随后通过与质子转运相关的松弛过程释放。类似的能量保存和转导原理可能也适用于其他呼吸链复合物和线粒体ATP合酶。