Nitrite reactivity of the binuclear copper site in T2D Rhus laccase: preparation of half met-NO2- T2D laccase and its correlation to half met-NO2- hemocyanin and tyrosinase.
Through chemistry directly comparable to that of the hemocyanins and tyrosinase, half met-NO2- T2D laccase derivatives have been prepared; this NO2- reactivity entails both two electron oxidation of the cuprous binuclear site in deoxy T2D laccase and one electron reduction of the coupled cupric site in the met derivative. However, the labile ligand substitution chemistry and lack of dimer formation in half met-NO2- T2D are in marked contrast to behavior of the simpler binuclear copper containing proteins under analagous conditions. This chemistry supports and extends our earlier studies on the ferrocyanide-generated half met T2D which first indicated an inability of exogenous ligands to bridge the binuclear copper site in laccase.
D001665:Binding Sites / Q000187:drug effects; D004156:Catechol Oxidase; D055598:Chemical Phenomena; D002621:Chemistry; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006433:Hemocyanins; D042845:Laccase; D008024:Ligands; D014442:Monophenol Monooxygenase; D009573:Nitrites / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D010947:Plants, Toxic; D012251:Toxicodendron / Q000201:enzymology*
D008024:Ligands; D009573:Nitrites; D003300:Copper; D006433:Hemocyanins; D010088:Oxidoreductases; D004156:Catechol Oxidase; D042845:Laccase; D014442:Monophenol Monooxygenase