Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.
Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.
复制标题
二磷脂酰甘油是牛心细胞色素 C 氧化酶最佳活性所必需的。
DOI:
10.1073/pnas.78.3.1456
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发表时间:
1981
影响因子:
11.1
通讯作者:
Capaldi,RA
中科院分区:
文献类型:
--
作者:
Vik,SB;Georgevich,G;Capaldi,RA
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.