Hu Yilin, Corbett Mary C, Fay Aaron W, Webber Jerome A, Hodgson Keith O, Hedman Britt, Ribbe Markus W
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17119-24. doi: 10.1073/pnas.0602647103. Epub 2006 Oct 18.
FeMo cofactor (FeMoco) biosynthesis is one of the most complicated processes in metalloprotein biochemistry. Here we show that Mo and homocitrate are incorporated into the Fe/S core of the FeMoco precursor while it is bound to NifEN and that the resulting fully complemented, FeMoco-like cluster is transformed into a mature FeMoco upon transfer from NifEN to MoFe protein through direct protein-protein interaction. Our findings not only clarify the process of FeMoco maturation, but also provide useful insights into the other facets of nitrogenase chemistry.
铁钼辅因子（FeMoco）的生物合成是金属蛋白生物化学中最复杂的过程之一。我们在此表明，钼和高柠檬酸在FeMoco前体的铁硫核心与NifEN结合时被掺入其中，并且通过直接的蛋白质-蛋白质相互作用，由此产生的完全互补的、类似FeMoco的簇在从NifEN转移到钼铁蛋白后转化为成熟的FeMoco。我们的发现不仅阐明了FeMoco成熟的过程，还为固氮酶化学的其他方面提供了有用的见解。
