Results 11 to 20 of about 8,975 (219)
Isolable Cysteine Sulfenyl Iodide: Stabilization by a Molecular Cradle, Crystal Structure, and Biologically Relevant Reactivity. [PDF]
ChembiochemAn isolable cysteine sulfenyl iodide (Cys–SI) stabilized by a molecular cradle is reported. X‐ray analysis and reactivity studies reveal hydrolysis to sulfenic acid, electrophilic substitution with indoles, and high reactivity toward amines and dimedone, providing direct evidence for long‐standing proposals on iodine‐mediated protein modification ...
Otaka S +4 more
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Cofactor binding protects flavodoxin against oxidative stress. [PDF]
PLoS ONE, 2012 In organisms, various protective mechanisms against oxidative damaging of proteins exist. Here, we show that cofactor binding is among these mechanisms, because flavin mononucleotide (FMN) protects Azotobacter vinelandii flavodoxin against hydrogen ...
Simon Lindhoud +5 more
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Cysteinyl and methionyl redox switches: Structural prerequisites and consequences
Redox Biology, 2023 Redox modifications of specific cysteinyl and methionyl residues regulate key enzymes and signal-transducing proteins in various pathways. Here, we analyzed the effect of redox modifications on protein structure screening the RCSB protein data bank for ...
Yana Bodnar, Christopher Horst Lillig
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H<sub>2</sub>S Is a Potential Universal Reducing Agent for Prx6-Type Peroxiredoxins. [PDF]
Adv Sci (Weinh)We report the identification of H2S as reducing agent for Prx6‐type peroxiredoxins. In contrast to common physiological reducing agents of other peroxiredoxins, HS− is small enough to access the active site of oxidized Prx6‐type enzymes in the fully‐folded protein conformation.
Lang L, Leiskau L, Bambach L, Deponte M.
europepmc +2 more sources
Isolable small-molecule cysteine sulfenic acid
Chemical Communications, 2021 A small-molecule cysteine sulfenic acid (Cys–SOH) with ‘shelf stability’ protected by a molecular cradle was synthesized by direct oxidation of a thiol with H2O2. Its crystal structure and biologically relevant reactivity were elucidated.
Tsukasa Sano +3 more
openaire +3 more sources
Reaction-based fluorogenic probes for detecting protein cysteine oxidation in living cells
Nature Communications, 2022 Fluorogenic detection of H2O2 in cells is established, but equivalent tools to monitor its cellular targets remain in their infancy. Here authors develop fluorogenic probes for detecting cysteine sulfenic acid, a redox modification inextricably linked to
Renan B. Ferreira +4 more
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Biomolecules, 2021 This review focuses on the consequences of GAPDH S-nitrosylation at the catalytic cysteine residue. The widespread hypothesis according to which S-nitrosylation causes a change in GAPDH structure and its subsequent binding to the Siah1 protein is ...
Vladimir I. Muronetz +3 more
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Antioxidants, 2023 Thiol antioxidants play important roles in cell and body defense against oxidative stress. In body fluid, albumin is the richest source of thiol antioxidants.
Yang Sui +6 more
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Brazilian Journal of Medical and Biological Research, 2009 Human serum albumin (HSA) is the most abundant protein in the intravascular compartment. It possesses a single thiol, Cys34, which constitutes ~80% of the total thiols in plasma. This thiol is able to scavenge plasma oxidants.
L. Turell +4 more
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Redox Biology, 2021 Albumin (Alb) is the most abundant plasma protein with multiple biological functions, including antioxidative property through its thiol activity. Given that inflammatory bowel disease is associated with a decreased level of Alb and an increased level of
Xiawen Yang +7 more
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