Substrate and doxygen binding to the endospore coat laccase from Bacillus subtilis

被引：157

作者：

Enguita, FJ

Marçal, D

Martins, LO

Grenha, R

Henriques, AO

Lindley, PF

Carrondo, MA ^{[1
]}

机构：

[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, Prot Crystallog Lab, P-2781901 Oeiras, Portugal

[2] Univ Lusofona Humanidades & Tecnol, Dept Engn & Tecnol, P-1749024 Lisbon, Portugal

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2004年 / 279卷 / 22期

关键词：

D O I：

10.1074/jbc.M314000200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 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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页码：23472 / 23476

页数：5

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