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Published on: July 19, 2024
Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model
Dénison S Sánchez-Miguel1, Jahir Romero-Jiménez, César A Reyes-López
1Laboratorio de Investigación Bioquímica, Programa Institucional en Biomedicina Molecular, Sección de Estudios de Posgrado, ENMyH-Instituto Politécnico Nacional, Guillermo Massieu Helguera No. 239, La Escalera Ticoman, DF, 07320, Mexico.
Abstract:
Enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface of several organisms, among other functions. Despite its participation in a variety of biological and pathophysiological processes, its stability and folding/unfolding reaction have not been fully explored. In this paper we present, the urea and GdnHCl-induced denaturation of enolase studied by means of fluorescence and circular dichroism spectroscopies. We found that enolase unfolds through a highly reversible pathway, populating a stable intermediate species in a range of experimental conditions. The refolding reaction also exhibits an intermediate state that might have a slightly more compact conformation compared to the unfolding intermediate. The thermodynamic parameters associated with the unfolding reaction are presented and discussed.
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