title: The binding of the retro-analogue of glutathione disulfide to glutathione reductase.
abstract: The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.
authors.affiliation: Institut für Organische Chemie und Biochemie, Universität Freiburg, Federal Republic of Germany.
authors.forename: W
authors.initials: W
authors.lastname: Janes
authors.forename: G E
authors.initials: GE
authors.lastname: Schulz
mesh_terms: D001665:Binding Sites; D003460:Crystallization; D005978:Glutathione / Q000031:analogs & derivatives* / Q000378:metabolism; D019803:Glutathione Disulfide; D005980:Glutathione Reductase / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D005980:Glutathione Reductase; D005978:Glutathione; D019803:Glutathione Disulfide