Substrate and Dioxygen Binding to the Endospore Coat Laccase from Bacillus subtilis
Связывание субстрата и диоксида кислорода с лакказой оболочки эндоспоры Bacillus subtilis
2004-05-01
SCID: 54.1/3yes3rek
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ABTS oxidative mediatorBacillus subtilisCotA laccasedioxygen bindingtrinuclear copper center
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Abstract (AI)
The 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.
Key Findings
1
A dioxygen moiety is clearly resolved in a solvent channel oriented toward one T3 copper atom of the trinuclear copper center.
2
The ABTS adduct binding site is well defined, revealing how ABTS may mediate laccase-catalyzed oxidation of non-phenolic substrates.
3
The CotA laccase from Bacillus subtilis endospore coats was crystallized with the non-catalytic co-oxidant ABTS, and its structure was determined by synchrotron radiation.
Research Object
CotA laccase enzyme from the Bacillus subtilis endospore coat (including its active/trinuclear copper center and solvent channel)
Research Subject
The structural basis of ABTS substrate/co-oxidant binding and dioxygen positioning at the trinuclear copper center
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2004-05-01
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