血红素蛋白与一氧化碳结合的动力学

Dynamics of carbon monoxide binding by heme proteins.

作者信息

Austin R H, Beeson K, Eisenstein L, Frauenfelder H, Gunsalus I C, Marshall V P

出版信息

Science. 1973 Aug 10;181(4099):541-3. doi: 10.1126/science.181.4099.541.

DOI:10.1126/science.181.4099.541

Abstract

Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50 degrees K for myoglobin and 25 degrees K for cytochrome P-450 in glycerol-water solution. Above 240 degrees K the reaction is second order; between 240 degrees and 200 degrees K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150 degrees K the reaction follows a power law and is approximately 10(3) times faster for cytochrome P-450 than for myoglobin.

摘要

在甘油 - 水溶液中，用闪光去除一氧化碳后，一氧化碳与肌红蛋白和细胞色素P - 450的再结合，对于肌红蛋白在低至50K时发生，对于细胞色素P - 450在25K时发生。在240K以上，反应是二级反应；在240K至200K之间，再结合变为指数形式且与一氧化碳浓度无关。在150K以下，反应遵循幂律，细胞色素P - 450的反应速度比肌红蛋白快约10³倍。