Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R-sphaeroides
Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R-sphaeroides
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DOI：
10.1021/bi971813b
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发表时间：
1998-02-24
期刊：
影响因子：
2.9
通讯作者：
Brzezinski, P
中科院分区：
文献类型：
--
作者：
Adelroth, P;Gennis, RB;Brzezinski, P
在这项研究中，我们已经结合使用定点突变的时间分辨光学吸收光谱研究质子化亚基-I残基赖氨酸-362（K（I-362））和苏氨酸-359（T（I-359））的作用，在细胞色素c氧化酶从球形红细菌的电子和质子转移。这些残基被认为是副球菌和牛心细胞色素氧化酶质子转移途径的一部分。K（I-362）和T（I-359）分别突变为甲硫氨酸和丙氨酸，导致总周转活性降低，
In this study we have combined the use of site-directed mutants with time-resolved optical absorption spectroscopy to investigate the role of the protonatable subunit-I residues lysine-362 (K(I-362)) and threonine-359 (T(I-359)) in cytochrome c oxidase from Rhodobacter sphaeroides in electron and proton transfer. These residues have been proposed to be part of a proton-transfer pathway ill cytochrome oxidases from Paracoccus denitrificans and bovine heart. Mutation of K(I-362) and T(I-359) to methionine and alanine, respectively, results in reduction of the overall turnover activities to