Structural basis of biological nitrogen fixation

作者：Douglas C. Rees, F. Akif Tezcan, Chad Haynes, Mika Y. Walton, Susana L. A. Andrade, Oliver Einsle, James B. Howard · 发表于：Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · 年份：2005 · DOI：10.1098/rsta.2004.1539 · 被引用次数：1121 · 研究领域：Metalloenzymes and iron-sulfur proteins、Ammonia Synthesis and Nitrogen Reduction、Electrocatalysts for Energy Conversion

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.