Results 21 to 30 of about 2,511 (170)

Commonly Used Alkylating Agents Limit Persulfide Detection by Converting Protein Persulfides into Thioethers

open access: yesAngewandte Chemie, 2022
AbstractProtein persulfides (R‐S‐SH) have emerged as a common post‐translational modification. Detection and quantitation of protein persulfides requires trapping with alkylating agents. Here we show that alkylating agents differ dramatically in their ability to conserve the persulfide's sulfur–sulfur bond for subsequent detection by mass spectrometry.
Danny Schilling   +5 more
openaire   +2 more sources

Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides

open access: yesBiomolecules, 2020
Cysteine persulfide (CysSSH) and cysteine polysulfides (CysSSnH, n > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that ...
Tomohiro Sawa   +3 more
doaj   +1 more source

Reactions of isolated persulfides provide insights into the interplay between H2S and persulfide reactivity [PDF]

open access: yesFree Radical Biology and Medicine, 2015
Hydrogen sulfide is ubiquitous in biological systems and exerts function over a wide range of important physiological processes. Complementing free H2S, the reductant-labile sulfur pool plays significant roles in the translocation and action of sulfide, however the chemistry of reductant-labile sulfide sources has not been studied systematically. Using
T Spencer, Bailey, Michael D, Pluth
openaire   +2 more sources

Synthesis of Sulfides and Persulfides Is Not Impeded by Disruption of Three Canonical Enzymes in Sulfur Metabolism

open access: yesAntioxidants, 2023
Reactive sulfur species, or persulfides and polysulfides, such as cysteine hydropersulfide and glutathione persulfide, are endogenously produced in abundance in both prokaryotes and eukaryotes, including mammals.
Qamarul Hafiz Zainol Abidin   +13 more
doaj   +1 more source

The Response of Acinetobacter baumannii to Hydrogen Sulfide Reveals Two Independent Persulfide-Sensing Systems and a Connection to Biofilm Regulation

open access: yesmBio, 2020
Acinetobacter baumannii is an opportunistic nosocomial pathogen that is the causative agent of several serious infections in humans, including pneumonia, sepsis, and wound and burn infections. A.
Brenna J. C. Walsh   +7 more
doaj   +1 more source

Persulfide-Responsive Transcription Factor SqrR Regulates Gene Transfer and Biofilm Formation via the Metabolic Modulation of Cyclic di-GMP in Rhodobacter capsulatus

open access: yesMicroorganisms, 2022
Bacterial phage-like particles (gene transfer agents—GTAs) are widely employed as a crucial genetic vector in horizontal gene transfer. GTA-mediated gene transfer is induced in response to various stresses; however, regulatory mechanisms are poorly ...
Takayuki Shimizu   +3 more
doaj   +1 more source

Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species

open access: yesAntioxidants, 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

Metabolic and Structural Insights into Hydrogen Sulfide Mis-Regulation in Enterococcus faecalis

open access: yesAntioxidants, 2022
Hydrogen sulfide (H2S) is implicated as a cytoprotective agent that bacteria employ in response to host-induced stressors, such as oxidative stress and antibiotics.
Brenna J. C. Walsh   +6 more
doaj   +1 more source

Direct Proteomic Mapping of Cysteine Persulfidation [PDF]

open access: yesAntioxidants & Redox Signaling, 2020
Aims: Cysteine persulfidation (also called sulfhydration or sulfuration) has emerged as a potential redox mechanism to regulate protein functions and diverse biological processes in hydrogen sulfide (H2S) signaling. Due to its intrinsically unstable nature, working with this modification has proven to be challenging.
Ling, Fu   +5 more
openaire   +2 more sources

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

open access: yesInorganics, 2020
Iron–sulfur (Fe–S) clusters are protein cofactors of a multitude of enzymes performing essential biological functions. Specialized multi-protein machineries present in all types of organisms support their biosynthesis.
Batoul Srour   +3 more
doaj   +1 more source

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