Copper transfer from Rhus vernicifera laccase.
Tree laccase, a multi-copper oxidase, has been studied as a copper donor in conjunction with the demetalated forms of three blue copper proteins. Copper transfer could be observed under reducing conditions in the absence of air. Only about 10% of the total copper in laccase could be transferred regardless of the amount of acceptor present in solution, hence, the laccase is heterogeneous as isolated. Potential sources of the heterogeneity are considered. After transfer, laccase could be partially resolved into copper-deficient and nearly holoprotein fractions that would not donate copper when recombined with acceptor protein. EPR results in conjunction with thiol titrations indicate that there is no net loss of type 1 copper from laccase but that there is loss of type 2 copper as well as a small amount of type 3 copper. Very little transfer is observed when type 2-depleted laccase is used as the donor. Finally, the implications that these results could have in the elucidation of possibly more physiologically relevant processes are briefly summarized.
Meadows
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KA
Department of Chemistry, Purdue University, West Lafayette, IN 47907-3699.
Morie-Bebel
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MM
McMillin
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DR
D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D042845:Laccase; D010088:Oxidoreductases / Q000378:metabolism*; D010947:Plants, Toxic; D012251:Toxicodendron / Q000201:enzymology*
D003300:Copper; D010088:Oxidoreductases; D042845:Laccase