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