DYNAMICS OF CARBON-MONOXIDE BINDING BY HEME PROTEINS
DYNAMICS OF CARBON-MONOXIDE BINDING BY HEME PROTEINS
复制标题
DOI：
10.1126/science.181.4099.541
复制
发表时间：
1973-01-01
期刊：
影响因子：
56.9
通讯作者：
MARSHALL, VP
中科院分区：
文献类型：
--
作者：
AUSTIN, RH;BEESON, K;MARSHALL, VP
在甘油-水溶液中，用闪光灯去除后，一氧化碳与肌红蛋白和细胞色素P-450的结合可降低到肌红蛋白50°K和细胞色素P-450 25°K。在240°K以上，反应为二级反应，在240°~200°K之间，再结合成指数关系，与一氧化碳浓度无关。在150°K以下，该反应遵循幂定律，细胞色素P-450的反应速度约为肌红蛋白的103倍。
Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 103times faster for cytochrome P-450 than for myoglobin.