Biochemical and Biophysical Research Communications, Vol.272, No.1, 29-35, 2000
Zinc-histidine as nucleation centers for growth of ZnS nanocrystals
Histidine is a chelator of zinc, most notably in zinc-finger proteins (zinc coordinated by cysteine and histidine) and in hyperaccumulator plants. Sulfide incorporation into molecules containing metal-cysteinyl complexes has been shown to occur in vivo in certain yeasts, leading to enhanced metal tolerance. Demonstrated here for the first time is incorporation of sulfide into zinc-histidine, resulting in histidine-ZnS nanocrystals (NCs) having unique optical properties. Sulfide complexation occurred optimally at alkaline pH into zinc-(histidine)(2) species, and WV/Vis absorption maxima were red-shifted as increasing sufide addition occurred. Intermediate sulfide concentrations led to multiple, thermodynamically preferred NC species within a sample. Fluorescence of histidine-ZnS NCs was greater than ZnS prepared previously with cysteinyl peptides. Transmission electron microscopy and selected-area electron diffraction indicated hexagonal ZnS crystals having an average size of 4.2 nm. A photocatalytic application of histidine-ZnS NCs was shown by efficient degradation of p-nitrophenol and paraquat in the presence of UV irradiation.