Journal articles
Selective On/Off-Nitroxides as Radical Probes to Investigate Non-radical Enzymatic Activity by Electron Paramagnetic Resonance
Abstract : 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 5G 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.
Cited literature [35 references]
https://hal-amu.archives-ouvertes.fr/hal-02091903
Contributor : Didier Gigmes <>
Submitted on : Sunday, April 7, 2019 - 6:35:30 AM
Last modification on : Tuesday, October 13, 2020 - 3:10:54 AM
Contributor : Didier Gigmes <>
Submitted on : Sunday, April 7, 2019 - 6:35:30 AM
Last modification on : Tuesday, October 13, 2020 - 3:10:54 AM
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