Yeast copper-thionein can reconstitute the Japanese-lacquer-tree (Rhus vernicifera) laccase from the Type 2-copper-depleted enzyme via a direct copper(I)-transfer mechanism
- 1 May 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 211 (2) , 515-517
- https://doi.org/10.1042/bj2110515
Abstract
The Type 2-Cu-depleted laccase from the Japanese lacquer tree (Rhus vernicifera) can be reconstituted with CuSO4 aerobically and much more rapidly and efficiently under anaerobic reducing conditions. This is to be related to a more favourable conformation of a laccase in the reduced state, rather than to reduction of the metal ion. In fact, reconstitution with Cu(I)-thionein from baker's yeast (Saccharomyces cerevisiae) only proceeds under anaerobic reducing conditions, via a direct transfer of Cu(I).This publication has 7 references indexed in Scilit:
- Heterogeneity of the Type 3 copper in Japanese-lacquer-tree (Rhus vernicifera) laccaseBiochemical Journal, 1982
- Proton and oxygen-17 magnetic resonance relaxation in Rhus laccase solutions: proton exchange with type 2 copper(II) ligandsBiochemistry, 1980
- Optical properties of japanese-lacquer-tree (Rhus vernicifera) laccase depleted of type 2 copper(II). Involvement of type-2 copper(II) in the 330nm chromophoreBiochemical Journal, 1980
- Titrations with ferrocyanide of japanese-lacquer-tree (Rhus vernicifera) laccase and of the type 2 copper-depleted enzyme. Interrelation of the copper sitesBiochemical Journal, 1980
- Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: A biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitionsJournal of Inorganic Biochemistry, 1980
- Pulsed electron paramagnetic resonance studies of types I and II copper of Rhus vernicifera laccase and porcine ceruloplasminBiochemistry, 1977
- Homologous copper(1)-(thiolate)2-chromophores in yeast copper thioneinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977