Bisson R, Azzi A, Gutweniger H, Colonna R, Montecucco C, Zanotti A
J Biol Chem. 1978 Mar 25;253(6):1874-80.
Cytochrome c derivatives labeled with a 3-nitrophenylazido group at lysine 13, at lysine 22, or at both residues have been prepared. The interaction of the cytochrome c derivatives with beef heart cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) in the presence of ultrviolet light results in formation of a covalent complex between cytochrome c and the oxidase. Using the lysine 22 derivative, the polypeptide composition of the oxidase is not modified, nor is its catalytic activity, whereas with the lysine 13 derivative, the gel electrophoretic pattern is altered and the catalytic activity of the complex diminished. The data are consisten with a specfic covalent interaction of the lysine 13 derivative of cytochrome c with the polypeptide of molecular weight 23,700 (Subunit II) of cytochrome c oxidase.
已制备出在赖氨酸13、赖氨酸22或这两个残基处均标记有3-硝基苯基叠氮基的细胞色素c衍生物。在紫外线存在下，这些细胞色素c衍生物与牛心细胞色素c氧化酶（亚铁细胞色素c：氧氧化还原酶，EC 1.9.3.1）相互作用，导致细胞色素c与氧化酶之间形成共价复合物。使用赖氨酸22衍生物时，氧化酶的多肽组成未被改变，其催化活性也未改变，而使用赖氨酸13衍生物时，凝胶电泳图谱发生改变，且复合物的催化活性降低。这些数据与细胞色素c的赖氨酸13衍生物与细胞色素c氧化酶分子量为23,700的多肽（亚基II）发生特异性共价相互作用一致。
