Characterization of coppers in Coliolus consors laccase
1991
Sakurai, T.
Laccase was purified from Coliolus consors and its coppers were spectroscopically characterized. While the absorption spectral feature is considerably similar to that of tree laccase, two CD bands coming from the charge transfer (S- leads to CU2+) are inverted. The EPR spectrum and copper analysis indicated that the enzyme contains one type 1, one type 2, and two type 3 coppers, of which the former two types of coppers are EPR detectable. The type 2 copper-depleted enzyme was prepared and characterized. An EPR detectable form of the type 3 coppers was developed from the type 2 copper-depleted derivative at pH 9.5.
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