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 UV/Vis absorption maxima were red-shifted as increasing sulfide 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.

Characterization of the bactericidal effects of sodium nitroprusside and other pentacyanonitrosyl complexes on the food spoilage bacterium Clostridium sporogenes.

The potent bactericidal activity of sodium nitroprusside (SNP; Na2[Fe(CN)5(NO)]) towards Clostridium sporogenes has been investigated. SNP inhibited cell growth in the concentration range of 10 to 40 microM. Concentrations above 80 microM caused irreversible loss of cell viability and cell lysis. Inhibition of cell growth was similar in complex and in defined media. SNP was found to be unreactive towards individual components of the defined medium, with the exception of cysteine. The chemical characteristics responsible for the potency of SNP were investigated by synthesizing analogs of SNP in which the Fe was replaced by different metals. The inhibitory potency of the pentacyanonitrosyl complexes decreased in the order Fe > Cr > V, which correlates with N-O stretching frequency (vNO). In contrast, the Ru complex which had a vNO comparable to that of Fe was a poor inhibitor. Electron paramagnetic resonance spectroscopy showed that SNP was rapidly reduced to the paramagnetic Fe(I) compound [Fe(CN)4(NO)](2-) on contact with cells. Analysis of fractions from SNP-treated cells showed 90% oxidation of thiols in the cell walls compared with those in control cells. The toxicity of SNP involves S-nitrosation and reduction, the lack of toxicity of the Ru analog being consistent with the fact that it has poor reactivity towards thiols. When C. sporogenes cells were exposed to sublethal concentrations of SNP and viewed under the electron microscope, they showed blisters on the surface. These results point to the cell wall surface as a primary point of attack of the nitrosyl complex.