Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.
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.
Enguita
Francisco J
FJ
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal.
Marçal
David
D
Martins
Lígia O
LO
Grenha
Rosa
R
Henriques
Adriano O
AO
Lindley
Peter F
PF
Carrondo
Maria Arménia
MA
D001412:Bacillus subtilis / Q000201:enzymology*; D001665:Binding Sites; D042845:Laccase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010100:Oxygen / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013379:Substrate Specificity
D042845:Laccase; D010100:Oxygen