1. Investigation of sulfur containing amino acids at the lipoxygenase active site using a platinum complex
- Author
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Isabelle Michaud-Soret, Jean-Claude Chottard, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
- Subjects
Organoplatinum Compounds ,Protein Conformation ,Lipoxygenase ,Biochemistry ,chemistry.chemical_compound ,Methionine ,MESH: Protein Conformation ,Lipoxygenase Inhibitors ,MESH: Soybeans ,chemistry.chemical_classification ,0303 health sciences ,biology ,MESH: Kinetics ,030302 biochemistry & molecular biology ,MESH: Organoplatinum Compounds ,Tryptophan ,Amino acid ,Seeds ,Ditiocarb ,MESH: Ditiocarb ,MESH: Spectrometry, Fluorescence ,Stereochemistry ,Biophysics ,Fluorescence spectrometry ,MESH: Lipoxygenase Inhibitors ,03 medical and health sciences ,Cysteine ,Binding site ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,Molecular Biology ,MESH: Tryptophan ,MESH: Lipoxygenase ,030304 developmental biology ,Binding Sites ,Electron Spin Resonance Spectroscopy ,Substrate (chemistry) ,Active site ,Cell Biology ,MESH: Cysteine ,Kinetics ,Spectrometry, Fluorescence ,Enzyme ,chemistry ,MESH: Binding Sites ,MESH: Seeds ,MESH: Methionine ,biology.protein ,MESH: Electron Spin Resonance Spectroscopy ,Soybeans - Abstract
International audience; 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.
- Published
- 1992
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