Huynh Boi Hanh
Department of Physics, Emory University, Atlanta, GA 30322, USA.
Methods Mol Biol. 2011;766:221-35. doi: 10.1007/978-1-61779-194-9_15.
Mössbauer spectroscopy has contributed significantly to the studies of Fe-containing proteins. Early applications yielded detailed electronic characterizations of hemeproteins, and thus enhanced our understanding of the chemical properties of this important class of proteins. The next stage of the applications was marked by major discoveries of several novel Fe clusters of complex structures, including the 8Fe7S P cluster and the mixed metal 1Mo7Fe M center in nitrogenase. Since early 1990 s, rapid kinetic techniques have been used to arrest enzymatic reactions for Mössbauer studies. A number of reaction intermediates were discovered and characterized, both spectroscopically and kinetically, providing unprecedented detailed molecular-level mechanistic information. This chapter gives a brief summary of the historical accounts and a concise description of some experimental and theoretical elements in Mössbauer spectroscopy that are essential for understanding Mössbauer spectra. Major biological applications are summarized at the end.
穆斯堡尔谱学对含铁蛋白质的研究做出了重大贡献。早期的应用产生了对血红素蛋白详细的电子表征，从而增进了我们对这一重要蛋白质类化学性质的理解。应用的下一阶段以发现几种具有复杂结构的新型铁簇为标志，包括固氮酶中的8Fe7S P簇和混合金属1Mo7Fe M中心。自20世纪90年代初以来，快速动力学技术已被用于使酶促反应停止以进行穆斯堡尔研究。通过光谱学和动力学方法发现并表征了许多反应中间体，提供了前所未有的详细分子水平的机理信息。本章简要总结了历史记录，并简要描述了穆斯堡尔谱学中一些对于理解穆斯堡尔谱至关重要的实验和理论要素。最后总结了主要的生物学应用。
