期刊
BIOORGANIC CHEMISTRY
卷 37, 期 1-3, 页码 1-5出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2008.09.002
关键词
Laccase; Plant; Fungal; Manganese; T1 site; T2/T3 cluster; Biocatalysis
资金
- Swedish Research Council [621-2005-3581]
- Russian Foundation of Basic Research [08-04-01450a]
The principal possibility of enzymatic oxidation of manganese ions by fungal Trametes hirsuta laccase in the presence of oxalate and tartrate ions, whereas not for plant Rhus vernicifera laccase, was demonstrated. Detailed kinetic studies of the oxidation of different enzyme substrates along with oxygen reduction by the enzymes show that in air-saturated solutions the rate of oxygen reduction by the T2/T3 cluster of laccases is fast enough not to be a readily noticeable contribution to the overall turnover rate. Indeed, the limiting step of the oxidation of high-redox potential compounds, such as chelated manganese ions, is the electron transfer from the electron donor to the T1 site of the fungal laccase. (C) 2008 Elsevier Inc. All rights reserved.
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