Investigation of sulfur containing amino acids at the lipoxygenase active site using a platinum complex.
Biochem Biophys Res Commun
; 182(2): 779-85, 1992 Jan 31.
Article
en En
| MEDLINE
| ID: mdl-1310394
ABSTRACT
Inactivation of native soybean lipoxygenase-1 was observed upon preincubation with (NEt4)[PtCl3(P(Bun)3)]. Removal of the platinum complex(es) from the inactivated enzyme by treatment with sodium diethyldithiocarbamate (Naddtc) which reverses methionine but not cysteine binding, restores most of the activity. Linoleic acid, an enzyme substrate, protects it from inactivation. The quenching of the fluorescence of the putative active site tryptophans which accompanies inactivation disappears after Naddtc reactivation. The (NEt4)[PtCl3(P(Bun)3)]-inactivated enzyme iron(II) cannot be oxidized at variance with that of the native or Naddtc reactivated enzyme, as checked by EPR spectroscopy. These results show that at least one methionine is close to the iron binding site in soybean lipoxygenase-1.
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Banco de datos:
MEDLINE
Asunto principal:
Compuestos Organoplatinos
/
Inhibidores de la Lipooxigenasa
/
Lipooxigenasa
/
Ditiocarba
/
Cisteína
/
Metionina
Idioma:
En
Año:
1992
Tipo del documento:
Article