Cysteines and H2O2 are fundamental players in redox signaling. Cysteine-thiol deprotonation favors the reaction with H2O2 that generates sulfenic acids with dual electrophilic/nucleophilic nature. The protein microenvironment surrounding the target cysteine is believed to control whether a sulfenic acid can be reversibly regulated by disulfide formation or irreversibly oxidized to sulfinates/sulfonates. Here, we present experimental oxidation kinetics and a QM/MM investigation to elucidate the reaction of H2O2 with glycolytic (AtGAPC1) and photosynthetic glyceraldehyde-3-phosphate dehydrogenase (AtGAPA) from Arabidopsis thaliana.
Zaffagnini, M., Fermani, S., Calvaresi, M., Orrù, R., Iommarini, L., Sparla, F., et al. (2016). TUNING CYSTEINE REACTIVITY AND SULFENIC ACID STABILITY BY PROTEIN MICROENVIRONMENT IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES OF ARABIDOPSIS THALIANA. ANTIOXIDANTS & REDOX SIGNALING, 24, 502-517 [10.1089/ars.2015.6417].
TUNING CYSTEINE REACTIVITY AND SULFENIC ACID STABILITY BY PROTEIN MICROENVIRONMENT IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES OF ARABIDOPSIS THALIANA
ZAFFAGNINI, MIRKO;FERMANI, SIMONA;CALVARESI, MATTEO;IOMMARINI, LUISA;SPARLA, FRANCESCA;FALINI, GIUSEPPE;BOTTONI, ANDREA;TROST, PAOLO BERNARDO
2016
Abstract
Cysteines and H2O2 are fundamental players in redox signaling. Cysteine-thiol deprotonation favors the reaction with H2O2 that generates sulfenic acids with dual electrophilic/nucleophilic nature. The protein microenvironment surrounding the target cysteine is believed to control whether a sulfenic acid can be reversibly regulated by disulfide formation or irreversibly oxidized to sulfinates/sulfonates. Here, we present experimental oxidation kinetics and a QM/MM investigation to elucidate the reaction of H2O2 with glycolytic (AtGAPC1) and photosynthetic glyceraldehyde-3-phosphate dehydrogenase (AtGAPA) from Arabidopsis thaliana.File | Dimensione | Formato | |
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Tuning Cysteine Reactivity_2.pdf
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