Vik S B, Georgevich G, Capaldi R A
Proc Natl Acad Sci U S A. 1981 Mar;78(3):1456-60. doi: 10.1073/pnas.78.3.1456.
Isolated beef heart cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) contains four or five molecules of tightly bound diphosphatidylglycerol per monomer (2-heme complex). This lipid could be removed in part, or wholly, by mixing the enzyme with high concentrations of Triton X-100 and then centrifuging the mixture through a glycerol gradient equilibrated in the same detergent. Cytochrome c oxidase retaining three or more diphosphatidylglycerol molecules per monomer was fully active when assayed in 1-oleoyl lysophosphatidylcholine. Upon removal of one or more of these diphosphatidylglycerols, enzymic activity was lost. Full activation could be obtained by adding diphosphatidylglycerol to the assay mixture along with lysophosphatidylcholine but not by adding phosphatidylcholine or phosphatidylethanolamine. Direct binding experiments, kinetic studies, and previous work using arylazidocytochrome c derivatives [Bisson, R., Jacobs, B. & Capaldi, R. A. (1980) Biochemistry 10, 4173-4178], indicate that diphosphatidylglycerol is involved in binding of substrate cytochrome c to cytochrome c oxidase.
分离得到的牛心细胞色素c氧化酶（亚铁细胞色素c：氧氧化还原酶，EC 1.9.3.1）每个单体（2-血红素复合物）含有四或五个紧密结合的二磷脂酰甘油分子。通过将该酶与高浓度的 Triton X-100混合，然后通过在相同去污剂中平衡的甘油梯度对混合物进行离心，可以部分或全部去除这种脂质。当在1-油酰溶血磷脂酰胆碱中进行测定时，每个单体保留三个或更多二磷脂酰甘油分子的细胞色素c氧化酶具有完全活性。去除一个或多个这些二磷脂酰甘油后，酶活性丧失。通过将二磷脂酰甘油与溶血磷脂酰胆碱一起添加到测定混合物中可以获得完全激活，但添加磷脂酰胆碱或磷脂酰乙醇胺则不能。直接结合实验、动力学研究以及先前使用芳基叠氮细胞色素c衍生物的工作[Bisson, R., Jacobs, B. & Capaldi, R. A. (1980) Biochemistry 10, 4173 - 4178]表明，二磷脂酰甘油参与底物细胞色素c与细胞色素c氧化酶的结合。
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