Brzezinski P, Malmström B G
FEBS Lett. 1985 Jul 22;187(1):111-4. doi: 10.1016/0014-5793(85)81224-2.
The rate of formation of the mixed-valence state of cytochrome c oxidase on incubation with carbon monoxide is strongly dependent on pH, supporting the concept that CO itself is the reducing agent. The reaction is biphasic due to the presence of two different enzyme forms in the resting oxidase. The kinetics of the reaction with the major enzyme form suggests an initial rapid binding of CO in a heme pocket of the oxidized enzyme and a subsequent slow intramolecular electron transfer to the cytochrome alpha 3-CuB site. Cytochrome alpha and CuA are not reduced even on prolonged incubation.
细胞色素c氧化酶与一氧化碳孵育时混合价态的形成速率强烈依赖于pH值，这支持了CO本身就是还原剂的观点。由于静息氧化酶中存在两种不同的酶形式，该反应是双相的。与主要酶形式的反应动力学表明，CO最初在氧化酶的血红素口袋中快速结合，随后分子内电子缓慢转移至细胞色素α3-CuB位点。即使长时间孵育，细胞色素α和CuA也不会被还原。
