固氮酶活性中心研究五十年  

Research on the Active Site of Nitrogenase over Fifty Years

作　　者：陈全亮 周朝晖[2] Quanliang Chen;Zhaohui Zhou(College of Chemistry and Environment,Southwest Minzu University,Chengdu 610041,China;State Key Laboratory of Physical Chemistry of Solid Surfaces,College of Chemistry and Chemical Engineering,Xiamen University,Xiamen 361005,Fujian Province,China)

机构地区：[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

出　　处：《大学化学》2024年第7期287-293,共7页University Chemistry

基　　金：国家自然科学基金(22179110)。

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Fe_(2)S_(2)·Mo_(2)O_(2)演变到MoFe_(7)S_(9)C(RHhomocit)(cys)(his)(H_(4)homocit=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。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 Fe_(2)S_(2)·Mo_(2)O_(2) to MoFe_(7)S_(9)C(R-Hhomocit)(cys)(his)(H_(4)homocit=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.

关 键 词：固氮酶 钼铁蛋白 铁钼辅基 活性中心 

分 类 号：O6[理学—化学] G64[文化科学—高等教育学]