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Article Dans Une Revue Biochemical and Biophysical Research Communications Année : 1992

Investigation of sulfur containing amino acids at the lipoxygenase active site using a platinum complex.

J. C. Chottard
  • Fonction : Auteur

Résumé

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.

Dates et versions

hal-01063004 , version 1 (11-09-2014)

Identifiants

Citer

I. Michaud-Soret, J. C. Chottard. Investigation of sulfur containing amino acids at the lipoxygenase active site using a platinum complex.. Biochemical and Biophysical Research Communications, 1992, 182 (2), pp.779-85. ⟨10.1016/0006-291X(92)91800-6⟩. ⟨hal-01063004⟩
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