用蛋白质电荷梯检测到的错误金属化位的质子合电子转移
Mayte Gonzalez1, Matthew J Guberman-Pfeffer1, Jordan C Koone1
1Department of Chemistry and Biochemistry, Baylor University, Waco, TX, USA. bryan_shaw@baylor.edu.
Physical chemistry chemical physics : PCCP
|August 28, 2024
概括
在超氧化物脱酶-1中,使用蛋白质电荷梯子研究了质子合电子转移 (PCET). 结果表明,PCET发生在所有四个铜原子上,由histidine连接体促进.
科学领域:
- 生物化学 生化学
- 生物有机化学 生物有机化学
- 蛋白质还原机制 蛋白质还原机制
背景情况:
- 在蛋白质中区分质子合电子转移 (PCET) 和电子转移 (ET) 对于理解生物氧化还原过程至关重要.
- 之前的研究表明,蛋白质电荷梯和毛细血管电泳可以通过测量电荷变化 (ΔZ_ET) 来区分ET和PCET.
研究的目的:
- 为了研究在无,无,无中PCET机制.
- 它是双铜的双铜.
- 使用充电梯方法使用超氧化物脱酶-1 (4Cu-SOD1).
- 在准型III铜中心确定参与PCET的质子受体.
主要方法:
- 使用蛋白质电荷梯和毛细血管电泳来测量4Cu-SOD1.1中铜离子减少后净蛋白质电荷的变化 (ΔZ_ET).
- 采用分子动力学和Poisson-Boltzmann计算来建模质子转移通路.
主要成果:
- 在pH 7.4.4下减少所有四个Cu2+离子时,4Cu-SOD1二元体的净电荷保持不变 (ΔZ_4ET = -0.09 ± 0.05每二元体).
- 这种缺乏电荷变化表明所有四个铜中心的电子和质子同时转移 (PCET).
- 计算分析确定了一种金属协调胺 (His71) 作为可能的质子受体.
结论:
- 当适当的氧化还原金属被纳入时,原生结合部位内的配体可以促进PCET.
- 这项研究提供了关于蛋白质结构和金属协调在调节氧化还原反应中的作用的见解.
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