Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada
- A. N. Bach Institute of Biochemistry, Leninsky pr. 33, Moscow 119071 (Russian Federation)
- BOKU – University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Wien (Austria)
- RSC ‘Kurchatov Institute’, Acad. Kurchatov sq. 1, Moscow 123182 (Russian Federation)
The restoration of the native form of laccase from B. aclada from the type 2 copper-depleted form of the enzyme was investigated. Copper ions were found to be incorporated into the active site after soaking the depleted enzyme in a Cu{sup +}-containing solution. Laccases belong to the class of multicopper oxidases catalyzing the oxidation of phenols accompanied by the reduction of molecular oxygen to water without the formation of hydrogen peroxide. The activity of laccases depends on the number of Cu atoms per enzyme molecule. The structure of type 2 copper-depleted laccase from Botrytis aclada has been solved previously. With the aim of obtaining the structure of the native form of the enzyme, crystals of the depleted laccase were soaked in Cu{sup +}- and Cu{sup 2+}-containing solutions. Copper ions were found to be incorporated into the active site only when Cu{sup +} was used. A comparative analysis of the native and depleted forms of the enzymes was performed.
- OSTI ID:
- 22515177
- Journal Information:
- Acta Crystallographica. Section F, Structural Biology Communications, Vol. 71, Issue Pt 12; Other Information: PMCID: PMC4666473; PMID: 26625287; PUBLISHER-ID: no5089; PUBLISHER-ID: S2053230X1502052X; OAI: oai:pubmedcentral.nih.gov:4666473; Copyright (c) Osipov et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 2053-230X
- Country of Publication:
- United States
- Language:
- English
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