Kaltashov Igor A, Zhang Mingxuan, Eyles Stephen J, Abzalimov Rinat R
Department of Chemistry, University of Massachusetts-Amherst, 710 North Pleasant Street, Amherst, MA 01003, USA.
Anal Bioanal Chem. 2006 Oct;386(3):472-81. doi: 10.1007/s00216-006-0636-6. Epub 2006 Aug 25.
Electrospray ionization mass spectrometry (ESI MS) has emerged recently as a powerful tool for analyzing many structural and behavioral aspects of metalloproteins in great detail. In this review we discuss recent developments in the field, placing particular emphasis on the unique features of ESI MS that lend themselves to metalloprotein characterization at a variety of levels. Direct mass measurement enables the determination of protein-metal ion binding stoichiometry in solution and metalloprotein higher order structure in the case of multi-subunit proteins. MS techniques have been developed for determining the locations of metal-binding centers, metal oxidation states and reaction intermediates of metal-containing enzymes. Other ESI MS techniques are also discussed, such as protein ion charge state distributions and hydrogen/deuterium exchange studies, which can be used to measure metal binding affinities and to shed light on vital dynamic aspects of the functional properties of metalloproteins endowed by metal binding.
电喷雾电离质谱（ESI MS）最近已成为一种强大的工具，可用于非常详细地分析金属蛋白的许多结构和行为方面。在本综述中，我们讨论了该领域的最新进展，特别强调了ESI MS的独特特征，这些特征有助于在多个层面上对金属蛋白进行表征。直接质量测量能够确定溶液中蛋白质 - 金属离子的结合化学计量，对于多亚基蛋白质还能确定其高阶结构。已经开发出质谱技术来确定金属结合中心的位置、金属氧化态以及含金属酶的反应中间体。还讨论了其他ESI MS技术，例如蛋白质离子电荷态分布和氢/氘交换研究，这些技术可用于测量金属结合亲和力，并揭示金属结合赋予金属蛋白功能特性的重要动态方面。
