Howard James B, Rees Douglas C
Department of Biochemistry, University of Minnesota, Minneapolis, MN 55455, USA.
Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17088-93. doi: 10.1073/pnas.0603978103. Epub 2006 Nov 6.
During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein; the Fe protein mediates the coupling of ATP hydrolysis to interprotein electron transfer, whereas the active site of the MoFe protein contains the polynuclear FeMo cofactor, a species composed of seven iron atoms, one molybdenum atom, nine sulfur atoms, an interstitial light atom, and one homocitrate molecule. This Perspective provides an overview of biological nitrogen fixation and introduces three contributions to this special feature that address central aspects of the mechanism and assembly of nitrogenase.
在生物固氮过程中,固氮酶催化以ATP为依赖的将氮气还原为氨的反应。固氮酶由两种金属蛋白组成,即铁(Fe)蛋白和钼铁(MoFe)蛋白;Fe蛋白介导ATP水解与蛋白间电子转移的偶联,而MoFe蛋白的活性位点包含多核FeMo辅因子,该辅因子由七个铁原子、一个钼原子、九个硫原子、一个间隙轻原子和一个高柠檬酸分子组成。本综述概述了生物固氮,并介绍了对这一专题的三篇论文,它们阐述了固氮酶机制和组装的核心方面。