Hu Yilin, Fay Aaron W, Lee Chi Chung, Yoshizawa Janice, Ribbe Markus W
Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.
Biochemistry. 2008 Apr 1;47(13):3973-81. doi: 10.1021/bi7025003. Epub 2008 Mar 4.
Assembly of nitrogenase MoFe protein is arguably one of the most complex processes in the field of bioinorganic chemistry, requiring, at least, the participation of nifS, nifU, nifB, nifE, nifN, nifV, nifQ, nifZ, nifH, nifD, and nifK gene products. Previous genetic studies have identified factors involved in MoFe protein assembly; however, the exact functions of these factors and the precise sequence of events during the process have remained unclear until the recent characterization of a number of assembly-related intermediates that provided significant insights into this biosynthetic "black box". This review summarizes the recent advances in elucidation of the mechanism of FeMoco biosynthesis in four aspects: (1) the ex situ assembly of FeMoco on NifEN, (2) the incorporation of FeMoco into MoFe protein, (3) the in situ assembly of P-cluster on MoFe protein, and (4) the stepwise assembly of MoFe protein.
固氮酶钼铁蛋白的组装可以说是生物无机化学领域中最复杂的过程之一,至少需要nifS、nifU、nifB、nifE、nifN、nifV、nifQ、nifZ、nifH、nifD和nifK基因产物的参与。以往的遗传学研究已经确定了参与钼铁蛋白组装的因子;然而,直到最近对一些与组装相关的中间体进行了表征,为这个生物合成的“黑匣子”提供了重要见解,这些因子的确切功能以及该过程中事件的精确顺序仍不清楚。本综述从四个方面总结了铁钼辅因子生物合成机制阐明方面的最新进展:(1)铁钼辅因子在NifEN上的异位组装,(2)铁钼辅因子掺入钼铁蛋白,(3)P簇在钼铁蛋白上的原位组装,以及(4)钼铁蛋白的逐步组装。