Kowalska Joanna, DeBeer Serena
Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Biochim Biophys Acta. 2015 Jun;1853(6):1406-15. doi: 10.1016/j.bbamcr.2014.11.027. Epub 2014 Dec 5.
X-ray absorption (XAS) and X-ray emission spectroscopy (XES) provide element specific probes of the geometric and electronic structures of metalloprotein active sites. As such, these methods have played an integral role in nitrogenase research beginning with the first EXAFS studies on nitrogenase in the late 1970s. Herein, we briefly explain the information that can be extracted from XAS and XES. We then highlight the recent applications of these methods in nitrogenase research. The influence of X-ray spectroscopy on our current understanding of the atomic structure and electronic structure of iron molybdenum cofactor (FeMoco) is emphasized. Contributions of X-ray spectroscopy to understanding substrate interactions and cluster biosynthesis are also discussed. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.
X射线吸收光谱（XAS）和X射线发射光谱（XES）能提供针对金属蛋白活性位点几何结构和电子结构的元素特异性探针。因此，自20世纪70年代末对固氮酶进行首次扩展X射线吸收精细结构（EXAFS）研究以来，这些方法在固氮酶研究中发挥了不可或缺的作用。在此，我们简要解释可从XAS和XES中提取的信息。然后，我们重点介绍这些方法在固氮酶研究中的最新应用。强调了X射线光谱对我们当前理解铁钼辅因子（FeMoco）原子结构和电子结构的影响。还讨论了X射线光谱对理解底物相互作用和簇生物合成的贡献。本文是名为“铁/硫蛋白：分析、结构、功能、生物合成与疾病”特刊的一部分。
