一氧化碳血红蛋白与脱辅基过氧化物酶的结合物。
The combination of carbon monoxide-haem with apoperoxidase.
作者信息
Phelps C, Antonini E
出版信息
Biochem J. 1969 Oct;114(4):719-24. doi: 10.1042/bj1140719.
Abstract
- Static titrations reveal an exact stoicheiometry between various haem derivatives and apoperoxidase prepared from one isoenzyme of the horseradish enzyme. 2. Carbon monoxide-protohaem reacts rapidly with apoperoxidase and the kinetics can be accounted for by a mechanism already applied to the reaction of carbon monoxide-haem derivatives with apomyoglobin and apohaemoglobin. 3. According to this mechanism a complex is formed first whose combination and dissociation velocity constants are 5x10(8)m(-1)sec.(-1) and 10(3)sec.(-1) at pH9.1 and 20 degrees . The complex is converted into carbon monoxide-haemoprotein in a first-order process with a rate constant of 235sec.(-1) for peroxidase and 364sec.(-1) for myoglobin at pH9.1 and 20 degrees . 4. The effects of pH and temperature were examined. The activation energy for the process of complex-isomerization is about 13kcal./mole. 5. The similarity in the kinetics of the reactions of carbon monoxide-haem with apoperoxidase and with apomyoglobin suggests structural similarities at the haem-binding sites of the two proteins.
摘要
- 静态滴定显示，从辣根酶的一种同工酶制备的各种血红素衍生物与脱辅基过氧化物酶之间存在精确的化学计量关系。2. 一氧化碳原血红素与脱辅基过氧化物酶迅速反应，其动力学可以用已应用于一氧化碳血红素衍生物与脱辅肌红蛋白和脱辅血红蛋白反应的机制来解释。3. 根据该机制，首先形成一种复合物，在pH9.1和20摄氏度时，其结合和解离速度常数分别为5×10⁸m⁻¹sec⁻¹和10³sec⁻¹。在pH9.1和20摄氏度时，该复合物以一级过程转化为一氧化碳血红蛋白，过氧化物酶的速率常数为235sec⁻¹，肌红蛋白的速率常数为364sec⁻¹。4. 研究了pH和温度的影响。复合物异构化过程的活化能约为13千卡/摩尔。5. 一氧化碳血红素与脱辅基过氧化物酶和脱辅肌红蛋白反应动力学的相似性表明这两种蛋白质的血红素结合位点在结构上具有相似性。
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