ESR characteristics of sulfhydryl-containing peptide-nickel (III) complexes: implication for nickel (III) center of hydrogenases.
The Ni(III) complexes of N-mercaptoacetylglycyl-L-histidine and N-mercaptoacetylglycylglycylglycine clearly show the rhombic ESR pattern and g-values similar to the Ni(III) chromophore of hydrogenases. The present results strongly suggest that the Ni(III) center of hydrogenases contains one cysteine sulfur coordination as equatorial ligand in a tetragonal geometry. In addition, axial nitrogen ligand and a sulfur-rich Ni(III) site as in an S4 donor set may be ruled out. Indeed, the Ni(III) ESR features are a useful probe of the Ni(III) center in hydrogenases.
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D003901:Desulfovibrio / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D019605:Euryarchaeota / Q000201:enzymology; D006864:Hydrogenase; D008954:Models, Biological; D009532:Nickel / Q000378:metabolism*; D009842:Oligopeptides; D010088:Oxidoreductases / Q000378:metabolism*; D011485:Protein Binding; D013045:Species Specificity
D009842:Oligopeptides; D009532:Nickel; D010088:Oxidoreductases; D006864:Hydrogenase