Substrate and Dioxygen Binding to the Endospore Coat Laccase from Bacillus subtilis
2004; Elsevier BV; Volume: 279; Issue: 22 Linguagem: Inglês
10.1074/jbc.m314000200
ISSN1083-351X
AutoresFrancisco J. Enguita, David Marçal, Lı́gia O. Martins, Rosa Grenha, Adriano O. Henriques, Peter F. Lindley, M.A. Carrondo,
Tópico(s)bioluminescence and chemiluminescence research
ResumoThe CotA laccase from the endospore coat of Bacillus subtilis has been crystallized in the presence of the non-catalytic 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 dioxygen moiety is clearly defined within the solvent channel oriented toward one of the T3 copper atoms in the trinuclear center.
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