Brunori M, Silvestrini M C, Wilson M T, Weiss H
Biochem J. 1983 Nov 1;215(2):425-7. doi: 10.1042/bj2150425.
The reaction of Neurospora crassa cytochrome c oxidase with CO was studied by flash-photolysis and rapid-mixing experiments, leading to the determination of the association and dissociation rate constants (7 X 10(4) M-1 X s-1 and 0.02s-1 respectively). Pre-steady-state kinetic investigations of the catalytic properties of the enzyme showed that under proper conditions Neurospora cytochrome c oxidase can be 'pulsed', i.e. activated, like the mammalian enzyme. The 'pulsed' species is spectroscopically different from the 'resting' one, and the decay into the 'resting' state is fast (t1/2 approx. 3 min).
通过闪光光解和快速混合实验研究了粗糙脉孢菌细胞色素c氧化酶与CO的反应,从而测定了缔合和解离速率常数(分别为7×10⁴ M⁻¹×s⁻¹和0.02 s⁻¹)。对该酶催化特性的稳态前动力学研究表明,在适当条件下,粗糙脉孢菌细胞色素c氧化酶可以像哺乳动物酶一样被“脉冲式激发”,即被激活。“脉冲式激发”的物种在光谱上与“静止”物种不同,并且向“静止”状态的衰减很快(半衰期约为3分钟)。