三甲基膦马心肌红蛋白的电子转移自交换动力学

Electron-transfer self-exchange kinetics of trimethylphosphine horse-heart myoglobin.

作者信息

Brunel C, Bondon A, Simonneaux G

机构信息

Laboratoire de Chimie Organométallique et Biologique, Université de Rennes, France.

出版信息

Biochim Biophys Acta. 1992 Jul 6;1101(1):73-8. doi: 10.1016/0167-4838(92)90469-t.

DOI:10.1016/0167-4838(92)90469-t

PMID:1633178

Abstract

Electron self-exchange has been measured by an NMR technique for horse-heart myoglobin. The rate is 3.1 x 10(3) M-1 s-1 at 23 degrees in 0.1 M phosphate at pH 6.9. The rate was weakly dependent on ionic strength up to 0.7 M in added KCl (3.9 x 10(3) M-1 s-1). The enthalpy of activation was 12.1 +/- 0.5 kcal mol-1, and the entropy of activation was -1.2 +/- 0.5 cal mol-1 deg-1. Analysis of the data in terms of the Marcus theory gives a reorganization energy, lambda, for self-exchange of 1.6 eV mol-1.

摘要

已通过核磁共振技术测量了马心脏肌红蛋白的电子自交换。在23摄氏度、pH值为6.9的0.1M磷酸盐中，其速率为3.1×10³M⁻¹ s⁻¹。在添加KCl至0.7M时，该速率对离子强度的依赖性较弱（3.9×10³M⁻¹ s⁻¹）。活化焓为12.1±0.5千卡/摩尔，活化熵为-1.2±0.5卡/摩尔·开尔文⁻¹。根据马库斯理论对数据进行分析，得出电子自交换的重组能λ为1.6电子伏特/摩尔。