Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase.
FEBS Lett
; 456(3): 409-16, 1999 Aug 13.
Article
em En
| MEDLINE
| ID: mdl-10462054
ABSTRACT
The fluorescence signal of the single tryptophan residue (Trp69) of Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a combination of NMR spectroscopy and chemical detection of free thiol groups with a sulfhydryl reagent we could unambiguously show that the unusual fluorescence behaviour of Trp69 in cutinase is caused by the breaking of the disulfide bond between Cys31 and Cys109 upon irradiation, while the amide-aromatic hydrogen bond between Ala32 and Trp69 remains intact. This is the first example of tryptophan mediated photoreduction of a disulfide bond in proteins.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Triptofano
/
Hidrolases de Éster Carboxílico
/
Fusarium
Tipo de estudo:
Etiology_studies
Idioma:
En
Ano de publicação:
1999
Tipo de documento:
Article