Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.
Acta Crystallogr F Struct Biol Commun
; 71(Pt 12): 1465-9, 2015 Dec.
Article
em En
| MEDLINE
| ID: mdl-26625287
ABSTRACT
Laccases belong to the class of multicopper oxidases catalyzing the oxidation of phenols accompanied by the reduction of molecular oxygen to water without the formation of hydrogen peroxide. The activity of laccases depends on the number of Cu atoms per enzyme molecule. The structure of type 2 copper-depleted laccase from Botrytis aclada has been solved previously. With the aim of obtaining the structure of the native form of the enzyme, crystals of the depleted laccase were soaked in Cu(+)- and Cu(2+)-containing solutions. Copper ions were found to be incorporated into the active site only when Cu(+) was used. A comparative analysis of the native and depleted forms of the enzymes was performed.
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01-internacional
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MEDLINE
Assunto principal:
Cobre
/
Botrytis
/
Lacase
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2015
Tipo de documento:
Article