Study on the intermediate ions formed by glutathione peroxidase mimic 2,2'-ditellurobis(2-deoxy-β-cyclodextrin) by electrospray ionization mass spectrometry
Article first published online: 13 DEC 2012
Copyright © 2012 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 27, Issue 2, pages 319–324, 30 January 2013
How to Cite
Jiao, A., Yang, N., Xu, X. and Jin, Z. (2013), Study on the intermediate ions formed by glutathione peroxidase mimic 2,2'-ditellurobis(2-deoxy-β-cyclodextrin) by electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom., 27: 319–324. doi: 10.1002/rcm.6455
- Issue published online: 13 DEC 2012
- Article first published online: 13 DEC 2012
- Manuscript Accepted: 25 OCT 2012
- Manuscript Revised: 18 OCT 2012
- Manuscript Received: 28 AUG 2012
2,2'-Ditellurobis(2-deoxy-β-cyclodextrin) (2-TeCD) is one of the most well-known glutathione peroxidase (GPx) mimics. However, because the critical reaction intermediates had not previously been isolated or directly detected due to its short lifetime, the catalytic mechanism of 2-TeCD is not very clear and further experiments are needed to characterize each of the intermediates in the catalytic cycle.
Using electrospray ionization mass (and tandem) spectrometry (ESI-MS and ESI-MS/MS) experiments, the decomposition of hydrogen peroxide at the expense of glutathione (GSH) catalyzed by 2-TeCD was monitored on-line.
The key intermediates were successfully intercepted and structurally characterized for the first time by coupling a microreactor on-line to the ESI ion source, which permitted the fast screening of intermediates directly from solution.
The catalytic mechanism of 2-TeCD catalysis has been elaborated based on mass spectrometric data and exerted its peroxidase activity via tellurol, tellurenic acid, and tellurosulfide, in analogy with natural GPX. Copyright © 2012 John Wiley & Sons, Ltd.