Krasil'nikov P M, Bashtovyĭ D, Knox P P, Pashchenko V Z
Biofizika. 2004 Sep-Oct;49(5):822-8.
The dark recombination rate constant for the photooxidized bacteriochlorophyll (P) and reduced primary quinone acceptor (QA) in the photosynthetic reaction centers (RC) from purple bacterium Rhodobacter sphaeroides depends nonmonotonically on temperature. The time of this reaction is approximately 100 ms at 270-300 K and decreases as the temperature both increases and decreases beyond this temperature range. It is known that the dome-shaped dependence of the thermodynamic stability on temperature is an intrinsic feature of many proteins in solution. The experimental results on the nonmonotonous temperature dependence of P+ and QA- recombination rate constant are discussed in terms of general thermodynamic approaches. The dynamic properties of the network of hydrogen bonds that are involved in the relaxation processes accompanying the electron transport are considered as a regulatory factor of the efficiency of electron transfer.
来自紫色细菌球形红杆菌光合反应中心（RC）中光氧化细菌叶绿素（P）和还原态初级醌受体（QA）的暗重组速率常数对温度的依赖性呈非单调变化。该反应时间在270 - 300K时约为100毫秒，在此温度范围之外，随着温度升高或降低，反应时间均会缩短。众所周知，热力学稳定性对温度呈圆顶状依赖性是溶液中许多蛋白质的固有特征。本文从一般热力学方法的角度讨论了P⁺和QA⁻重组速率常数对温度非单调依赖性的实验结果。参与伴随电子传递的弛豫过程的氢键网络的动态特性被视为电子转移效率的调节因子。
