The accessibility of type I Cu(II) centers in laccase, azurin, and stellacyanin to exchangeable hydrogen and ambient water.
The characteristic deuterium modulation pattern was observed in the electron spin-echo envelopes for laccase, decupro laccase (from which Type 2 copper had been removed), stellacyanin, and azurin that had been exchanged against D2O. From the decay rate of the modulation pattern and from a quantitative analysis of the modulation depth, we conclude that the Cu(II) sites in these proteins are directly accessible to solvent. Similar results were obtained for laccase and decupro laccase.
D001400:Azurin / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D003300:Copper / Q000032:analysis*; D003903:Deuterium; D017666:Deuterium Oxide; D004578:Electron Spin Resonance Spectroscopy; D042845:Laccase; D008667:Metalloproteins / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010947:Plants, Toxic; D012251:Toxicodendron / Q000201:enzymology; D014867:Water
D001426:Bacterial Proteins; D008667:Metalloproteins; D010940:Plant Proteins; D014867:Water; D001400:Azurin; C003343:stellacyanin protein, plant; D003300:Copper; D003903:Deuterium; D010088:Oxidoreductases; D042845:Laccase; D017666:Deuterium Oxide