A new copper(II) electron paramagnetic resonance signal in two laccases and in cytochrome c oxidase.
A new EPR signal from Cu2+ has been discovered in reductive experiments with type 2 copper-depleted laccase from Polyporus versicolor. A novel EPR signal has also been found in native laccase from Rhus vernicifera on oxidation of the reduced protein with H2O2. In reoxidation experiments with cytochrome c oxidase from beef heart, a new Cu2+ signal has been observed. With Rhus laccase, the new signal is shown to originate from one of the copper ions that are nondetectable in the resting enzyme, and evidence is presented for the signals in Polyporus laccase and cytochrome c oxidase also stemming from the metal pairs that are antiferromagnetically coupled in the oxidized enzymes. The new signals show strong rhombic character, and the EPR parameters place them in a category different from the signals of type 1 as well as of type 2 Cu2+ ions.
D001487:Basidiomycota / Q000201:enzymology*; D003300:Copper / Q000032:analysis*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000032:analysis*; D042845:Laccase; D010088:Oxidoreductases / Q000032:analysis*; D010947:Plants, Toxic; D011124:Polyporaceae / Q000201:enzymology*; D013045:Species Specificity; D012251:Toxicodendron / Q000201:enzymology*
D003300:Copper; D010088:Oxidoreductases; D042845:Laccase; D003576:Electron Transport Complex IV