大学化学 >> 2024, Vol. 39 >> Issue (7): 287-293.doi: 10.3866/PKU.DXHX202310133

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固氮酶活性中心研究五十年

陈全亮1, 周朝晖2   

  1. 1 西南民族大学化学与环境学院, 成都 610041;
    2 厦门大学化学化工学院, 固体表面物理化学国家重点实验室, 福建 厦门 361005
  • 收稿日期:2023-10-31 录用日期:2024-02-01 发布日期:2024-02-21
  • 通讯作者: 陈全亮 E-mail:qlchen@swun.edu.cn
  • 基金资助:
    国家自然科学基金(22179110)

Research on the Active Site of Nitrogenase over Fifty Years

Quanliang Chen1, Zhaohui Zhou2   

  1. 1 College of Chemistry and Environment, Southwest Minzu University, Chengdu 610041, China;
    2 State Key Laboratory of Physical Chemistry of Solid Surfaces, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, Fujian Province, China
  • Received:2023-10-31 Accepted:2024-02-01 Published:2024-02-21
  • Contact: Quanliang Chen E-mail:qlchen@swun.edu.cn

摘要: 固氮酶是固氮微生物在常温常压下固氮成氨的催化剂,其活性中心的结构从Fe2S2∙Mo2O2演变到MoFe7S9C(R-Hhomocit)(cys)(his) (H4homocit = 高柠檬酸,Hcys = 半胱氨酸,Hhis = 组氨酸)。本文将回顾这一重要的历史过程,探讨化学模拟、光谱学、理论计算和生物化学,特别是结构生物学等领域在固氮酶活性中心研究中的重要成就,从化学结构的角度看固氮酶活性中心研究五十年。

关键词: 固氮酶, 钼铁蛋白, 铁钼辅基, 活性中心

Abstract: Nitrogenase is a catalyst used by nitrogen-fixing microorganisms to convert atmospheric nitrogen into ammonia at ambient temperature and pressure. The structure of the active site in molybdenum nitrogenase has evolved from Fe2S2∙Mo2O2 to MoFe7S9C(R-Hhomocit)(cys)(his) (H4homocit = homocitric acid, Hcys = cysteine, Hhis = histidine) through advancements in chemical modeling, spectroscopy, and theoretical calculations, especially for structural biology. This paper provides a comprehensive review of the important achievements in the study of the active site of nitrogenase from a chemical structure perspective over the past fifty years.

Key words: Nitrogenase, MoFe-protein, FeMo-cofactor, Active site