Brunori M, Gibson Q H
EMBO J. 1983;2(11):2025-6. doi: 10.1002/j.1460-2075.1983.tb01695.x.
The reaction of cytochrome-c-oxidase with O2 has been reinvestigated at 2 degrees C by a flow laser pulsed method. The experiments indicate that a new spectral intermediate, populated with a rate constant of approximately 5000/s, is observed in a wavelength range in which heme a is the only chromophore (445 and 430 nm). The results are interpreted with reference to previous data obtained in the near infrared region, and it is suggested that breakage of the (enzyme bound) dioxygen bond is associated to a spectral perturbation of the cytochrome a3-CuB binuclear center.
通过流动激光脉冲法在2℃下对细胞色素c氧化酶与O2的反应进行了重新研究。实验表明,在血红素a是唯一发色团的波长范围内(445和430nm)观察到一种新的光谱中间体,其生成速率常数约为5000/s。参考先前在近红外区域获得的数据对结果进行了解释,并表明(酶结合的)双氧键的断裂与细胞色素a3-CuB双核中心的光谱扰动有关。