Biochemical and spectroscopic probes of mercury(II) coordination environments in proteins.

摘要: Publisher Summary The high affinity of mercuric ion for thiolate ligands and the rapid ligand exchange rates resulting complexes make Hg(II) a relatively easy metal to bind active sites variety cysteine-containing enzymes. This feature has made useful biochemical tool selectively displacing one type copper from multicopper enzyme. It become apparent that several spectroscopic features in their own right could be distinguishing coordination environments. Although is d 10 metal, it would mistake consider spectroscopically silent. As described here, interaction with biopolymers can probed using extended X-ray absorption fine structure (EXAFS), UV-Vis, 199 Hg nuclear magnetic resonance (NMR), circular dichroism (CD) spectroscopies. Several spectra structurally characterized model have been correlated primary number aiding determination environments proteins. chapter discusses advantages limitations substitution structure, function, studies Given these handles, geometry, identity, binding stoichiometry, dissociation rates, constants are possible. Practical techniques, such as common methods proteins, discussed. presents mercury chemistry, including structural thermodynamic trends biologically relevant compounds.