ArticleChembiochem : a European journal of chemical biology2025
Isolable Cysteine Sulfenyl Iodide: Stabilization by a Molecular Cradle, Crystal Structure, and Biologically Relevant Reactivity.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Isolable Cysteine Sulfenyl Iodide: Stabilization by a Molecular Cradle, Crystal Structure, and Biologically Relevant Reactivity.Chembiochem : a European journal of chemical biology · 2025Article
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5 authors.
Funding
Abstract
Cysteine sulfenyl iodides (Cys-SIs) have long been recognized as important intermediates in the oxidative modification of cysteine thiols since 1950s, implicated in pathways such as hydrolysis to cysteine sulfenic acid (Cys-SOH) and electrophilic aromatic substitution with an indole ring of tryptophan to form Cys-Trp thioether linkages. Despite their proposed significance in both biological and chemical contexts, direct examination of Cys-SIs has been precluded by their intrinsic instability. Herein, the first isolation of a small-molecule Cys-SI, stabilized using a nanosized molecular cradle at the N-terminus of cysteine, is reported. The structure of the isolable Cys-SI is determined by X-ray crystallography, and its reactivity is investigated with a range of nucleophiles. Hydrolysis to Cys-SOH and reaction with an indole derivative provide direct chemical evidence for long-standing mechanistic proposals. Furthermore, rapid formation of sulfenamides with amines and high-yield adduct formation with dimedone, a canonical sulfenic-acid probe, reveal that Cys-SI possesses even greater electrophilicity than Cys-SOH. These results deliver a structurally defined reference for Cys-SI and inform mechanisms of iodine-mediated protein oxidation and peptide modification.
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