[FeFe]-酶HydE结合复合B的晶体结构
Roman Rohac1, Lydie Martin1, Liang Liu2
1Univ. Grenoble Alpes, CEA, CNRS, IBS, Metalloproteins Unit, F-38000 Grenoble, France.
Journal of the American Chemical Society
|May 28, 2021
概括
[FeFe]-酶使用独特的H集群进行转化. 这项研究揭示了HydE与B复合体结合的晶体结构,揭示了合成2FeH中心的新铁物种.
科学领域:
- 生物化学
- 结构生物学
- 生物有机化学
背景情况:
- [FeFe]-酶是通过独特的H集群催化H2转换的关键酶.
- H 集群包括一个 [Fe4S4] 集群与一个 [2Fe] H 中心相连,这是催化作用的活性部位.
- 机械中的酶,如HydG和HydE,对于组装H集群至关重要.
研究的目的:
- 要确定与其基质结合的HydE的高分辨率晶体结构,复合物-B.
- 阐明HydE修饰复合-B以形成 [2Fe]H中心的前体的机制.
- 在H集群生物合成过程中调查基质获取,产品释放和中间转移.
主要方法:
- 通过X射线结晶学获得高分辨率的结构.
- 用于研究HydE活性的酶分析.
- 反应中间体的生物化学分析.
主要成果:
- 确定了复合B结合HydE的晶体结构,揭示了其精确的结构.
- 一种新的五坐标铁物种被捕获,为Hyde的功能提供了机械洞察力.
- 证据支持HydE在修改复合物-B为2FeH中心的单体"SFe(CO) 2CN"前体中的作用.
结论:
- 结构和机制数据提供了对HideE在H集群生物合成中的作用的详细了解.
- 这项工作阐明了组装[FeFe]酶独特活性位点的初步步骤.
- 这些发现有助于了解复杂的金属酶成熟途径.
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