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对细胞染色体c氧化酶的晶体化物探测揭示了结构基础,表明假定的质子转移H通路出质子

Atsuhiro Shimada¹, Jumpei Baba¹, Shuhei Nagao¹

¹Picobiology Institute, Graduate School of Life Science, University of Hyogo, Hyogo, Japan.

The Journal of biological chemistry

|September 24, 2023

概括

细胞染色体c氧化酶使用低潜力金属位点来驱动对质子送至关重要的结构变化. 这些变化与氧气减少部位无关,证实了低潜能部位.

科学领域:

生物化学和生物物理学
结构生物学结构生物学
生物能源学生物能源学

背景情况:

细胞染色体c氧化酶 (CcO) 是一种关键的酶复合物,它催化了有氧呼吸的最后一步,将分子氧减少到水中.
CcO配对电子转移到穿过膜的质子,这是细胞能量生产所必不可少的过程.
之前的研究发现了CcO的氧化还原合结构变化,但没有确定它们与特定的金属位点或它们在质子中的作用有关.

研究的目的:

为了确定细胞染色体c氧化酶中负责氧化还原合结构变化的特定金属位点.
阐明这些结构变化在CcO的质子机制中的功能作用.
为了研究低氧诱导激活剂Higd1a对CcO活性和电子转移的影响.

主要方法:

采用X射线晶体学,在各种氧化状态下确定化物结合的CcO的结构.
进行了比较结构分析,以确定与不同氧化还原状态和连接体结合相关的明显变化.
使用动态分析来评估Higd1a对CcO活性的影响.

主要成果:

低电位金属位点 (CuA和Fea) 被确定为Asp51,Arg438,Glu198的结构变化的诱导物,而血是一种基法纳基乙烯基组.
氧气减少部位主要影响了Ser382.2的结构变化.
质子/电子合效率保持不变 (1:1),表明低电位诱导的结构变化直接参与了质子.

结论:

CcO的低电位金属位点对于驱动质子转移所必需的结构重组至关重要.
鉴定到的结构变化,由H路径促进,与CcO的质子功能直接相关.
低氧诱导激活剂Higd1a增强了CcO活动,而不会改变通过低电位点的电子转移途径.

关键词:

在O (((2)-减少减少.进行X射线结晶学分析.化物抑制抑制的方法细胞染色体c氧化酶的作用血液蛋白质是血液中的蛋白质.质子是一个质子.

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