Probing the dioxygen route in Melanocarpus albomyces laccase with pressurized xenon gas.
Biochemistry
; 50(21): 4396-8, 2011 May 31.
Article
em En
| MEDLINE
| ID: mdl-21524088
ABSTRACT
Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxigênio
/
Ascomicetos
/
Xenônio
/
Sondas Moleculares
/
Lacase
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Finlândia