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- W2011979165 abstract "Laccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. A new laccase was isolated from the basidiomycete Coriolopsis caperata strain 0677 and its amino-acid sequence was determined. According to its physicochemical properties and spectroscopic features, the laccase from C. caperata is a high redox-potential blue laccase. Attempts to crystallize the native enzyme were unsuccessful. The copper type 2-depleted (T2D) laccase was prepared and crystallized. The structure of T2D laccase from C. caperata was solved at 1.6 Å resolution, and attempts to reconstruct the T2 copper centre were performed using Cu + and Cu 2+ ions. The structure of T2D+Cu + laccase was solved at 1.89 Å resolution. It was shown that the T2D+Cu + laccase structure contained four copper ions in the active site. Reconstruction could not be achieved when the T2D laccase crystals were treated with CuSO 4 ." @default.
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- W2011979165 date "2015-03-26" @default.
- W2011979165 modified "2023-09-27" @default.
- W2011979165 title "Elucidation of the crystal structure of<i>Coriolopsis caperata</i>laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions" @default.
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- W2011979165 doi "https://doi.org/10.1107/s1399004715001595" @default.
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