ArticleArchives of biochemistry and biophysics2008
Specific electrochemical iodination of horse heart myoglobin at tyrosine 103 as determined by Fourier transform ion cyclotron resonance mass spectrometry.
Article in Archives of biochemistry and biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Cyclopropanol can function as a caged dual-functional warhead for selective electrochemical bioconjugation.Nature chemistry · 2026Article
- Catalysis in Chemical Modification of Proteins.ChemCatChem · 2025Article
- Electrochemical labelling of hydroxyindoles with chemoselectivity for site-specific protein bioconjugation.Nature chemistry · 2024Article
- Electrochemical Late-Stage Functionalization.Chemical reviews · 2023Review
- A Multi-Sensor System for Sea Water Iodide Monitoring and Seafood Quality Assurance: Proof-of-Concept Study.Sensors (Basel, Switzerland) · 2021Article
- Laccase catalyzed synthesis of iodinated phenolic compounds with antifungal activity.PloS one · 2014Article
- New protein footprinting: fast photochemical iodination combined with top-down and bottom-up mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Top-down mass analysis of protein tyrosine nitration: comparison of electron capture dissociation with "slow-heating" tandem mass spectrometry methods.Analytical chemistry · 2010Article
- Retention of enzyme activity with a boron-doped diamond electrode in the electro-oxidative nitration of lysozyme.Enzyme and microbial technology · 2010Article
- Radical directed dissociation for facile identification of iodotyrosine residues using electrospray ionization mass spectrometry.Analytical chemistry · 2010Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The iodination of proteins remains a useful tool in biochemistry for radiolabelling. However, chemical or enzymatic iodination is difficult to control and can give deleterious polyiodination. Previously, we have shown that electrooxidation with nitrite is a rapid method for the selective nitration of tyrosine residues in proteins. In principle, it should be possible to substitute a number of electrooxidisable anions into the tyrosine phenol ring. Electrochemical iodination is more difficult to control than nitration because the rapid anodic oxidation of I(-) leads to persistent formation of the iodinating triiodide anion. However, application of pulsed electrooxidation and reduction cycles is shown to be an effective procedure for the selective mono and double-iodination of myoglobin, which may have general application to other proteins in controlling of the level of iodination. Mono- and double-iodination of myoglobin by this method was confirmed by electrospray FT-ICR mass spectrometry. Infrared multiphoton dissociation (IRMPD) enabled localization of the site of mono-iodination to be restricted to either His97 or Tyr103. More extensive sequence coverage was obtained with electron capture dissociation (ECD), allowing unambiguous assignment of the site of iodination to Tyr103.
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