期刊
MOLECULAR BIOLOGY
卷 52, 期 1, 页码 23-29出版社
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0026893318010041
关键词
two-domain laccases; T2/T3 copper centers; channels; X-ray structures; Streptomyces griseoflavus
资金
- Presidium of the Russian Academy of Sciences
- Russian Foundation for Basic Research [15-04-03002]
- Russian Science Foundation [17-14-01207]
Laccase belongs to the family of copper-containing oxidases. A study was made of the mechanism that sustains the incorporation of copper ions into the T2/T3 centers of recombinant two-domain laccase Streptomyces griseoflavus Ac-993. The occupancy of the T3 center by copper ions was found to increase with an increasing copper content in the culture medium and after dialysis of the protein preparation against a copper sulfate-containing buffer. The T2 center was filled only when overproducer strain cells were grown at a higher copper concentration in the medium. Two-domain laccases were assumed to possess a channel that serves to deliver copper ions to the T3 center during the formation of the three-dimensional laccase conformation and dialysis of the protein preparation. A narrower channel leads to the T2 center in two-domain laccases compared with three-domain ones, rendering the center less accessible for copper atoms. The incorporation of copper ions into the T2 center of two-domain laccases is likely to occur in the course of their biosynthesis or the formation of a functional trimer.
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