Ledenev A N, Davydov R M, Bliumenfel'd L A
Biofizika. 1981 Sep-Oct;26(5):782-5.
Using flash photolysis, horseradish peroxidase rebinding of carbon monoxide has been observed in the temperature range between 20 and -70 degrees C. A lag-period of about 50 ms immediately after photodissociation takes place. This lag-period is assumed to be due to the formation of the intermediate protein form with the low reactivity. Following rebinding is bimolecular process with the rate constant 4 x 10(3) M-1 S-1 usually observed for the peroxidase reaction with carbon monoxide. For some peroxidase molecules (about 10 per cent) rebinding of carbon monoxide is CO-concentration independent monomolecular process, which implies, apparently, ligands in these molecules do not leave the protein after photodissociation.
利用闪光光解技术，在20至 -70摄氏度的温度范围内观察到了辣根过氧化物酶与一氧化碳的重新结合。光解离后立即出现约50毫秒的延迟期。这个延迟期被认为是由于形成了反应活性较低的中间蛋白质形式。随后的重新结合是一个双分子过程，其速率常数为4×10³ M⁻¹ s⁻¹，这是过氧化物酶与一氧化碳反应通常观察到的。对于一些过氧化物酶分子（约10%），一氧化碳的重新结合是与CO浓度无关的单分子过程，这显然意味着这些分子中的配体在光解离后不会离开蛋白质。
