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Updated: May 10, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Glutathione-complexed iron-sulfur clusters. Reaction intermediates and evidence for a template effect promoting
Wenbin Qi1, Jingwei Li, C Y Chain
1Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Ave, Columbus, OH 43210, USA.
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-).
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