Structural basis of biological nitrogen fixation
Structural basis of biological nitrogen fixation
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DOI：
10.1098/rsta.2004.1539
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发表时间：
2005-04-15
期刊：
影响因子：
5
通讯作者：
Howard, JB
中科院分区：
文献类型：
--
作者：
Rees, DC;Tezcan, FA;Howard, JB
生物固氮是由固氮酶系统介导的，该系统催化大气中的二氮依赖于ATP还原成氨。固氮酶由两种组分金属蛋白组成，具有FeMo辅因子的MoFe蛋白提供底物还原的活性位点，并且Fe蛋白将ATP水解与电子转移偶联。概述了固氮酶系统，强调的蛋白质和相关的蛋白质簇，具有显着的能力，在环境条件下催化固氮的结构组织。虽然固氮酶形成氨的机制仍然是谜，机械推理的动机在固氮酶生物化学，光谱学，模型化学和计算研究领域的最新发展在这个结构框架内进行了讨论。
Biological nitrogen fixation is mediated by the nitrogenase enzyme system that catalyses the ATP dependent reduction of atmospheric dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the MoFe-protein with the FeMo-cofactor that provides the active site for substrate reduction, and the Fe-protein that couples ATP hydrolysis to electron transfer. An overview of the nitrogenase system is presented that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions. Although the mechanism of ammonia formation by nitrogenase remains enigmatic, mechanistic inferences motivated by recent developments in the areas of nitrogenase biochemistry, spectroscopy, model chemistry and computational studies are discussed within this structural framework.