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(2003) J Biol Chem 278 : 46938-46948 PubMed: 12937169 Search on PubMed DOI: Primary Citation Related Structures: 22GS PubMed Abstract: The thermodynamics of binding of both the substrate glutathione (GSH) and the competitive inhibitor S-hexylglutathione to the mutant Y49F of human glutathione S-transferase (hGST P1-1), a key residue at the dimer interface, has been investigated by isothermal titration calorimetry and fluorescence spectroscopy
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