Selective On/Off‐Nitroxides as Radical Probes to Investigate Non‐radical Enzymatic Activity by Electron Paramagnetic Resonance | Zendy

Duttagupta Indranil | Zendy; Jugniot Natacha | Zendy; Audran Gérard | Zendy; Franconi JeanMichel | Zendy; Marque Sylvain R. A. | Zendy; Massot Philippe | Zendy; Mellet Philippe | Zendy; Parzy Elodie | Zendy; Thiaudière Eric | Zendy; Vanthuyne Nicolas | Zendy

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Selective On/Off‐Nitroxides as Radical Probes to Investigate Non‐radical Enzymatic Activity by Electron Paramagnetic Resonance

Author(s) -

Duttagupta Indranil,

Jugniot Natacha,

Audran Gérard,

Franconi JeanMichel,

Marque Sylvain R. A.,

Massot Philippe,

Mellet Philippe,

Parzy Elodie,

Thiaudière Eric,

Vanthuyne Nicolas

Publication year - 2018

Publication title -

chemistry – a european journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.687

H-Index - 242

eISSN - 1521-3765

pISSN - 0947-6539

DOI - 10.1002/chem.201800866

Subject(s) - nitroxide mediated radical polymerization , chemistry , electron paramagnetic resonance , moiety , photochemistry , stereochemistry , organic chemistry , nuclear magnetic resonance , radical polymerization , physics , copolymer , polymer

A nitroxide carrying a peptide specific to the binding pocket of the serine proteases chymotrypsin and cathepsin G is prepared. This peptide is attached as an enol ester to the nitroxide. Upon enzymatic hydrolysis of the peptide, the enol ester moiety is transformed into a ketone moiety. This transformation affords a difference of 5 G in phosphorus hyperfine coupling constant between the electronic paramagnetic resonance (EPR) signals of each nitroxide. This property is used to monitor the enzymatic activity of chymotrypsin and cathepsin G by EPR. Michaelis constants were determined and match those reported for conventional optical probes.

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