Green D E, Fry M
Proc Natl Acad Sci U S A. 1980 Apr;77(4):1951-5. doi: 10.1073/pnas.77.4.1951.
Cytochrome oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) of beef heart mitochondria, prepared by a standard method and brought to the highest purity level, is essentially inactive when tested in the aerobic assay involving oxidation of reduced cytochrome c by molecular oxygen. Three reagents (lysolecithin, Tween 20, and exogenous phospholipids) can convert cytochrome oxidase from an inactive to an active coupling state. These conversions are reversible: i.e., removal of the inducing agent leads to loss of activity. The evidence for the intrinsic coupling capability is that cytochrome oxidase in the active state invariably generates a proton gradient during respiration, and such gradient formation is demonstrable even when cytochrome oxidase is not inserted into a liposome.
用标准方法制备并达到最高纯度水平的牛心线粒体细胞色素氧化酶(亚铁细胞色素c:氧氧化还原酶,EC 1.9.3.1),在涉及分子氧氧化还原型细胞色素c的需氧测定中进行测试时基本上没有活性。三种试剂(溶血卵磷脂、吐温20和外源性磷脂)可将细胞色素氧化酶从不活性状态转变为活性偶联状态。这些转变是可逆的,即去除诱导剂会导致活性丧失。内在偶联能力的证据是,处于活性状态的细胞色素氧化酶在呼吸过程中总是会产生质子梯度,而且即使细胞色素氧化酶未插入脂质体中,这种梯度形成也是可以证明的。