An epr signal from the half-reduced type 3 copper pair in Rhus vernicifera laccase |
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Authors: | Bengt Reinhammar |
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Institution: | Department of Biochemistry and Biophysics, University of Göteborg and Chalmers Institute of Technology, Sweden |
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Abstract: | A new type of Cu(II) epr signals have been produced in native and type 2 copper depleted Rhus vernicifera laccase. They are shown to originate from one of the type 3 copper ions that are epr silent in the resting enzyme. The new epr signals show high rhombicity in g tensor and are similar to those observed in other proteins, such as superoxide dismutase and half-met hemocyanin. The half-reduced type 3 copper pair is formed by reduction with an electron from type 1 Cu(I) but only after a reoxidation of the copper pair, either by peroxide or dioxygen. It is suggested that the half-reduction of the type 3 copper pair only occurs in molecules where type 2 copper ion is either reduced or absent. |
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Keywords: | Address reprint request to Dr Bengt Reinhammar Department of Biochemistry and Biophysics Chalmers Institute of Technology S-412 96 Gothenburg Sweden |
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