铁钼辅因子在NifEN上的成熟
FeMo cofactor maturation on NifEN.
作者信息
Hu Yilin, Corbett Mary C, Fay Aaron W, Webber Jerome A, Hodgson Keith O, Hedman Britt, Ribbe Markus W
机构信息
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
出版信息
Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17119-24. doi: 10.1073/pnas.0602647103. Epub 2006 Oct 18.
Abstract
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.
摘要
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。
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