Jones G D, Wilson M T
J Inorg Biochem. 1984 Jun;21(2):147-58. doi: 10.1016/0162-0134(84)85047-3.
The reduction of cytochrome c oxidase (EC 1.9.3.1) by Cr2+ ions has been studied by stopped-flow spectrophotometry and is compared with the Cr2+ reduction of cytochrome c and azurin. The effects of temperature, pH, and added anions (e.g., SCN-) have been investigated. The behavior of the electron acceptor site of cytochrome c oxidase stands in contrast to that of the other redox proteins with regard to the effects of added anions and we suggest that this reflects the more buried nature of this site in the complex enzyme.
利用停流分光光度法研究了Cr2+离子对细胞色素c氧化酶（EC 1.9.3.1）的还原作用，并与Cr2+对细胞色素c和天青蛋白的还原作用进行了比较。研究了温度、pH值和添加阴离子（如SCN-）的影响。就添加阴离子的影响而言，细胞色素c氧化酶电子受体位点的行为与其他氧化还原蛋白的行为形成对比，我们认为这反映了该位点在复合酶中埋藏得更深的性质。
