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Substrate and Dioxygen Binding to the Endospore Coat Laccase from Bacillus subtilis.

Authors :
Enguita, Francisco J.
Marçal, David
Martins, Lígia O.
Grenha, Rosa
Henriques, Adriano O.
Lindley, Peter F.
Carrondo, Maria Arménia
Source :
Journal of Biological Chemistry. 5/28/2004, Vol. 279 Issue 22, p23472-23476. 5p. 4 Diagrams, 1 Chart.
Publication Year :
2004

Abstract

The CotA laccase from the endospore coat of Bacillus subtilis has been crystallized in the presence of the noncatalytic co-oxidant 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS), and the structure was determined using synchrotron radiation. The binding site for this adduct is well defined and indicates how ABTS, in conjunction with laccases, could act as an oxidative mediator toward non-phenolic moieties. In addition, a alioxygen moiety is clearly defined within the solvent channel oriented toward one of the T3 copper atoms in the trinuclear center. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219258
Volume :
279
Issue :
22
Database :
Academic Search Index
Journal :
Journal of Biological Chemistry
Publication Type :
Academic Journal
Accession number :
13600428
Full Text :
https://doi.org/10.1074/jbc.M314000200