Jones G D, Jones M G, Wilson M T, Brunori M, Colosimo A, Sarti P
Biochem J. 1983 Jan 1;209(1):175-82. doi: 10.1042/bj2090175.
The reduction of cytochrome c oxidase (EC 1.9.3.1) by dithionite was investigated by stopped-flow spectrophotometry and flow-flash techniques in the presence of CO. Of the two haem groups present in the enzyme, that associated with cytochrome alpha is the first reduced. The second-order rate constants for reduction of a number of redox proteins (cytochrome c, stellacyanin and azurin) by the S2O4(2-) and SO2.- anions are reported, and the values are compared with those determined for cytochrome c oxidase. These results are discussed in terms of the accessibility and charge distribution of the electron-entry site of cytochrome c oxidase.
在一氧化碳存在的情况下,通过停流分光光度法和流动闪光技术研究了连二亚硫酸盐对细胞色素c氧化酶(EC 1.9.3.1)的还原作用。该酶中存在的两个血红素基团中,与细胞色素α相关的那个是第一个被还原的。报道了S2O4(2-)和SO2.-阴离子对多种氧化还原蛋白(细胞色素c、杨梅素和天青蛋白)的还原二级速率常数,并将这些值与细胞色素c氧化酶的测定值进行了比较。根据细胞色素c氧化酶电子进入位点的可及性和电荷分布对这些结果进行了讨论。