ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2015
Theoretical insights into the mechanism of redox switch in heat shock protein Hsp33.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 6 citations in OpenAlex.
- TrypOx, a Novel Eukaryotic Homolog of the Redox-Regulated Chaperone Hsp33 inFrontiers in microbiology · 2020Article
- Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges.Biomolecules · 2015Review
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4 authors at 3 institutions in 2 countries.
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Abstract
Heat shock protein 33 (Hsp33) is activated in the presence of H2O2 by a very interesting redox switch based on a tetra-coordinated zinc-cysteine complex present in the fully reduced and inactive protein form. The oxidation of this zinc center by H2O2 induces formation of two S-S bridges and the zinc release followed by the protein unfolding. We report here a theoretical study of the step-by-step sequence of the overall process starting with the oxidation of the first cysteine residue and ending with the zinc release. Each reaction step is characterized by its Gibbs free energy barrier (∆G (‡)). It is predicted that the first reaction step consists in the oxidation of Cys263 by H2O2 which is by far the most reactive cysteine (∆G (‡) = 15.4 kcal mol(-1)). The next two reaction steps are the formation of the first S-S bridge between Cys263 and Cys266 (∆G (‡) = 13.6 kcal mol(-1)) and the oxidation of Cys231 by H2O2 (∆G (‡) = 20.4 kcal mol(-1)). It is then shown that the formation of the second S-S bridge (Cys231-Cys233) before the zinc release is most unlikely (∆G (‡) = 34.8 kcal mol(-1)). Instead, the release of zinc just after the oxidation of the third cysteine (Cys231) is shown to be thermodynamically (dissociation Gibbs free energy ∆G d = 6.0 kcal mol(-1)) and kinetically (reaction rate constant k d ≈ 10(6) s(-1)) favored. This result is in good agreement with the experimental data on the oxidation mechanism of Hsp33 zinc center available to date.
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