title: Glutathione-complexed iron-sulfur clusters. Reaction intermediates and evidence for a template effect promoting assembly and stability.
abstract: Assembly and stabilization of a glutathione-complexed [2Fe-2S] cluster is promoted by aggregation of glutathione. The cluster core selects the tetramer species from a collection of equilibrating solution aggregate species, and in turn the core is stabilized toward hydrolytic degradation. Studies of glutathione derivatives, in combination with mass spectrometric and Mössbauer investigations provide insight on reaction intermediates during formation of [2Fe-2S](GS)4(2-).
authors.affiliation: Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Ave, Columbus, OH 43210, USA.
authors.forename: Wenbin
authors.initials: W
authors.lastname: Qi
authors.forename: Jingwei
authors.initials: J
authors.lastname: Li
authors.forename: C Y
authors.initials: CY
authors.lastname: Chain
authors.forename: G A
authors.initials: GA
authors.lastname: Pasquevich
authors.forename: A F
authors.initials: AF
authors.lastname: Pasquevich
authors.forename: J A
authors.initials: JA
authors.lastname: Cowan
mesh_terms: D005978:Glutathione / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D015394:Molecular Structure
chemical_list: D007506:Iron-Sulfur Proteins; D005978:Glutathione