» Articles » PMID: 16099166

Does Double Electron Capture Lead to the Formation of Biradicals? An ECD-SORI-CID Study on Lacticin 481

Overview
Specialty Chemistry
Date 2005 Aug 16
PMID 16099166
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

We studied lacticin 481, a small lantibiotic with three lanthionine bridges, by electron capture dissociation (ECD) in a Fourier transform ion cyclotron resonance (FTICR) mass spectrometer. Following electron capture, very little fragmentation was observed, but species formed by nondissociative single and multiple electron capture were abundant. Ions formed by double electron capture were subjected to sustained off resonance irradiation collision induced dissociation (SORI-CID) to determine whether stable biradicals were formed. In the SORI-CID spectra of the ions formed by double electron capture, some, but minor, H* radical loss was observed, which was not observed at all for regularly protonated ions. A small part of the ions formed by double electron capture are thus long-lived biradicals. Apart from the observed H* loss, the SORI-CID spectra of ions that captured two electrons was similar to that of regularly protonated ions and quite different from the SORI-CID spectra of radical ions formed by single electron capture. This implies that recombination of the two radical sites is the dominant process in biradical lacticin 481 ions, at least on the time scale of our SORI-CID experiments.

Citing Articles

Where Does the Electron Go? Stable and Metastable Peptide Cation Radicals Formed by Electron Transfer.

Pepin R, Layton E, Liu Y, Afonso C, Turecek F J Am Soc Mass Spectrom. 2016; 28(1):164-181.

PMID: 27709510 DOI: 10.1007/s13361-016-1512-z.


Capturing Polyradical Protein Cations after an Electron Capture Event: Evidence for their Stable Distonic Structures in the Gas Phase.

Baba T, Campbell J J Am Soc Mass Spectrom. 2015; 26(10):1695-701.

PMID: 26231348 DOI: 10.1007/s13361-015-1207-x.


Electron capture dissociation of hydrogen-deficient peptide radical cations.

Kalli A, Hess S J Am Soc Mass Spectrom. 2012; 23(10):1729-40.

PMID: 22855421 DOI: 10.1007/s13361-012-0433-8.


Distributive and directional behavior of lantibiotic synthetases revealed by high-resolution tandem mass spectrometry.

Lee M, Ihnken L, You Y, McClerren A, van der Donk W, Kelleher N J Am Chem Soc. 2009; 131(34):12258-64.

PMID: 19663480 PMC: 2738757. DOI: 10.1021/ja9033507.


Activated Ion Electron Capture Dissociation (AI ECD) of proteins: synchronization of infrared and electron irradiation with ion magnetron motion.

Mikhailov V, Cooper H J Am Soc Mass Spectrom. 2009; 20(5):763-71.

PMID: 19200749 PMC: 2674148. DOI: 10.1016/j.jasms.2008.12.015.


References
1.
Horn D, Ge Y, McLafferty F . Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins. Anal Chem. 2000; 72(20):4778-84. DOI: 10.1021/ac000494i. View

2.
Kleinnijenhuis A, Duursma M, Breukink E, Heeren R, Heck A . Localization of intramolecular monosulfide bridges in lantibiotics determined with electron capture induced dissociation. Anal Chem. 2003; 75(13):3219-25. DOI: 10.1021/ac0263770. View

3.
EDMAN P, Begg G . A protein sequenator. Eur J Biochem. 1967; 1(1):80-91. DOI: 10.1007/978-3-662-25813-2_14. View

4.
Mirgorodskaya E, Roepstorff P, Zubarev R . Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer. Anal Chem. 1999; 71(20):4431-6. DOI: 10.1021/ac990578v. View

5.
Mirgorodskaya O, Haselmann K, Kjeldsen F, Zubarev R, Roepstorff P . Towards the standard-module approach to disulfide-linked polypeptide nanostructures. I. Methodological prerequisites and mass spectrometric characterization of the test two-loop structure. Eur J Mass Spectrom (Chichester). 2003; 9(2):139-48. DOI: 10.1255/ejms.539. View