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

Abstract : An itroxide carryingapeptides pecific to the bindingp ocket of the serine proteasesc hymotrypsin and cathepsin Gi sp repared. This peptidei sa ttached as an enol ester to the nitroxide. Upon enzymatic hydrolysis of the peptide, the enol ester moiety is transformed into a ketone moiety.T his transformation affords ad ifference of 5G in phosphorus hyperfine couplingc onstant between the electronic paramagnetic resonance (EPR) signals of each nitroxide.T his property is used to monitor the enzymatic activity of chymotrypsin and cathepsin Gb yE PR. Michaelis constants were determined and match those reported for conventional opticalprobes.
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Submitted on : Tuesday, February 11, 2020 - 11:06:30 AM
Last modification on : Tuesday, October 13, 2020 - 3:11:03 AM

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Indranil Duttagupta, Natacha Jugniot, Gérard Audran, Jean-Michel Franconi, Sylvain R.A. Marque, et al.. Selective On/Off-Nitroxides as Radical Probes to Investigate Non-radical Enzymatic Activity by Electron Paramagnetic Resonance. Chemistry - A European Journal, Wiley-VCH Verlag, 2018, 24 (30), pp.7615-7619. ⟨10.1002/chem.201800866⟩. ⟨hal-02421099⟩

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