title: X-ray absorption spectroscopy of dinuclear metallohydrolases.
abstract: In this mini-review, we briefly discuss the physical origin of x-ray absorption spectroscopy (XAS) before illustrating its application using dinuclear metallohydrolases as exemplary systems. The systems we have selected for illustrative purposes present a challenging problem for XAS, one that is ideal to demonstrate the potential of this methodology for structure/function studies of metalloenzymes in general. When the metal ion is redox active, XAS provides a sensitive measure of oxidation-state-dependent differences. When the metal ion is zinc, XAS is the only spectroscopic method that will provide easily accessible structural information in solution. In the case of heterodimetallic sites, XAS has the unique ability to interrogate each metal site independently in the same sample. One of the strongest advantages of XAS is its ability to examine metal ion site structures with crystallographic precision, without the need for a crystal. This is key for studying flexible metal ion sites, such as those described in the selected examples, because it allows one to monitor structural changes that occur during substrate turnover.
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio. Electronic address: tiernedl@miamioh.edu.
authors.forename: David L
authors.initials: DL
authors.lastname: Tierney
authors.affiliation: School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland, Australia.
authors.forename: Gerhard
authors.initials: G
authors.lastname: Schenk
mesh_terms: D000818:Animals; D006801:Humans; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D056928:X-Ray Absorption Spectroscopy / Q000379:methods*
chemical_list: D008670:Metals; D006867:Hydrolases