The peroxymonocarbonate anion, HCO, the covalent adduct between the carbon dioxide and hydrogen peroxide anion, effectively reacts with SO in the gas phase following three oxidative routes. Mass spectrometric and electronic structure calculations show that sulphur dioxide is oxidised through a common intermediate to the hydrogen sulphate anion, sulphur trioxide, and sulphur trioxide anion as primary products through formal HO, oxygen atom, and oxygen ion transfers. The hydrogen sulphite anion is also formed as a secondary product from the oxygen atom transfer path. The uncommon nucleophilic behaviour of HCO is disclosed by the Lewis acidic properties of SO, an amphiphilic molecule that forms intermediates with characteristic and diagnostic geometries with peroxymonocarbonate.
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http://dx.doi.org/10.3390/molecules28010132 | DOI Listing |
Biochem J
December 2024
Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Blegdamsvej 3, Copenhagen 2200, Denmark.
The active site Cys residue in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is sensitive to oxidation by hydrogen peroxide (H2O2), with this resulting in enzyme inactivation. This re-routes the carbon flux from glycolysis to the pentose phosphate pathway favoring the formation of NADPH and synthetic intermediates required for antioxidant defense and repair systems. Consequently, GAPDH inactivation serves as a redox switch for metabolic adaptation under conditions of oxidative stress.
View Article and Find Full Text PDFWater Res
January 2025
State Key Laboratory for Oxo Synthesis and Selective Oxidation, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, China. Electronic address:
Advanced oxidation processes that utilize peroxymonocarbonate (HCO), generated in-situ through the reaction of HCO and HO, are employed for the removal of pollutants in water. Nevertheless, the precise role of HO in these processes remains a subject of debate. This study established a HCO-based oxidation system using NaHCO and HO for the degradation of acetaminophen and investigated the activation mechanisms of coexisting oxidants.
View Article and Find Full Text PDFFree Radic Biol Med
February 2025
Mātai Hāora - Centre for Redox Biology & Medicine, Department of Pathology and Biomedical Science, University of Otago, Christchurch, New Zealand. Electronic address:
Oxidation of thiol proteins and redox signaling occur in cells exposed to HO but mechanisms are unclear. We used redox proteomics to seek evidence of oxidation of specific proteins either by a mechanism involving reaction of HO with CO/bicarbonate to give the more reactive peroxymonocarbonate, or via a relay involving peroxiredoxins (Prdxs). Changes in oxidation state of specific Cys-SH residues on treating Jurkat T lymphoma cells with HO were measured by isotopically labeling reduced thiols and analysis by mass spectrometry.
View Article and Find Full Text PDFCurr Opin Chem Biol
December 2024
Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden; Department of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, Budapest, Hungary. Electronic address:
Endogenously formed reactive molecules, such as lipid peroxides, 4-hydroxynonenal, methylglyoxal and other reactive oxygen species, can have major effects on cells. Accumulation of these molecules is counteracted by antioxidant enzymes, including the glutathione (GSH) and thioredoxin (Trx) systems, in turn regulated by the KEAP1/NRF2 system. Receptor tyrosine kinases (RTK) and their counteracting protein tyrosine phosphatases (PTP) are also modulated through redox regulation of PTP activities.
View Article and Find Full Text PDFChem Res Toxicol
July 2024
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Sao Paulo 05508-900, Brazil.
Peroxymonocarbonate (HCO/HOOCO) is produced by the reversible reaction of CO/HCO with HO ( = 0.33 M, pH 7.0).
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