Biophysical Features of Bacillithiol, the Glutathione Surrogate of Bacillus subtilis and other Firmicutes [PDF]
, 2013 Bacillithiol (BSH) is the major low-molecular-weight (LMW) thiol in many low-G+C Gram-positive bacteria (Firmicutes). Evidence now emerging suggests that BSH functions as an important LMW thiol in redox regulation and xenobiotic detoxification, analogous
Arbach, Miriam +5 more
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Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling?
Redox Biology, 2018 The reversible oxidation of protein cysteine residues (Cys-SH) is a key reaction in cellular redox signaling involving initial formation of sulfenic acids (Cys-SOH), which are commonly detected using selective dimedone-based probes.
David E. Heppner +11 more
doaj +1 more source
Reactivity of Small Oxoacids of Sulfur
Molecules, 2019 Oxidation of sulfide to sulfate is known to consist of several steps. Key intermediates in this process are the so-called small oxoacids of sulfur (SOS)—sulfenic HSOH (hydrogen thioperoxide, oxadisulfane, or sulfur hydride hydroxide) and sulfoxylic
Sergei V. Makarov +2 more
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Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin [PDF]
, 2014 Metal-sulfenate centers are known to play important roles in biology and yet only limited examples are known due to their instability and high reactivity.
Hadt, Ryan G. +8 more
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Arabidopsis thaliana dehydroascorbate reductase 2 : conformational flexibility during catalysis [PDF]
, 2017 Dehydroascorbate reductase (DHAR) catalyzes the glutathione (GSH)-dependent reduction of dehydroascorbate and plays a direct role in regenerating ascorbic acid, an essential plant antioxidant vital for defense against oxidative stress.
Bodra, Nandita +8 more
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Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species
Antioxidants, 2019 Hydrogen sulfide (H2S/HS⁻) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH).
Dayana Benchoam +3 more
doaj +1 more source
The role of peroxiredoxins in cancer [PDF]
, 2017 Peroxiredoxins (PRDXs) are a ubiquitously expressed family of small (22-27 kDa) non-seleno peroxidases that catalyze the peroxide reduction of H2O2, organic hydroperoxides and peroxynitrite.
CAPALBO, CARLO +4 more
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Biological hydropersulfides and related polysulfides – a new concept and perspective in redox biology [PDF]
, 2018 The chemical biology of thiols (RSH, e.g., cysteine and cysteine‐containing proteins/peptides) has been a topic of extreme interest for many decades due to their reported roles in protein structure/folding, redox signaling, metal ligation, cellular ...
Akaike Takaaki +13 more
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SOHSite: incorporating evolutionary information and physicochemical properties to identify protein S-sulfenylation sites [PDF]
, 2016 Distribution of KEGG pathway annotations for S-sulfenylated proteins.
Cheng-Tsung Lu +5 more
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Role of glutathionylation in infection and inflammation [PDF]
, 2019 Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by dierent cellular oxidoreductases, by which the redox state of the cell
Baldelli, S. +5 more
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