Investigating the influence of histidine residues on the metal ion binding ability of the wheat metallothionein Î³-Ec-1 domain

Article ID	Journal	Published Year	Pages	File Type
7754950	Journal of Inorganic Biochemistry	2015	7 Pages	PDF

Abstract

The Î³-domain of the wheat Ec-1 metallothionein contains a M(II)2Cys6 cluster. Mutation of one of the Cys residues to His increases the metal ion selectivity of the binding sites resulting in a mixed ZnCd cluster with Zn(II) nearly exclusively coordinated to the Cys3His site in accordance with the HSAB principle.87

Keywords

TOF 2-PDS F-AAS Metal ion specificity 2,2′-dithiodipyridine TRIS TOCSY HSQC Cys SEC GST LMCT Ligand-to-metal charge transfer HIS Time-of-Flight Cysteine flame atomic absorption spectroscopy Mass spectrometry Total correlation spectroscopy Zinc Metallothionein Heteronuclear Single Quantum Correlation histidine polymerase chain reaction PCR Cadmium Size exclusion chromatography glutathione S-transferase