Characterization by mass spectrometry and IRMPD spectroscopy of the sulfoxide group in oxidized methionine and related compounds

Ignasiak, Marta T.; Scuderi, Debora; Oliveira, Pedro de; Pędziński, Tomasz; Rayah, Yamina; Levin, Chantal Houée

doi:10.1016/j.cplett.2010.12.012

Cited by 31 publications

(63 citation statements)

References 28 publications

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“…Second, in our previous work 6 we have shown that IRMPD provides a signature of the sulfoxide function with its IR band at around 1000 cm À1 in a non-congested region. Second, in our previous work 6 we have shown that IRMPD provides a signature of the sulfoxide function with its IR band at around 1000 cm À1 in a non-congested region.…”

Section: Discussionmentioning

confidence: 87%

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Tandem mass spectrometry and infrared spectroscopy as a tool to identify peptide oxidized residues

Scuderi

Ignasiak

Serfaty

et al. 2015

Phys. Chem. Chem. Phys.

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The final products obtained by the oxidation of small model peptides containing the thioether function, either methionine or S-methyl cysteine, have been characterized by tandem mass spectrometry and IR Multiple Photon Dissociation (IRMPD) spectroscopy. The modified positions have been clearly identified by the CID-MS(2) fragmentation mass spectra with or without loss of sulfenic acid, as well as by the vibrational signature of the sulfoxide bond at around 1000 cm(-1). The oxidation of the thioether function did not lead to the same products in these model peptides. The sulfoxide and sulfone (to a lesser extent) have been clearly identified as final products of the oxidation of S-methyl-glutathione (GS-Me). Decarboxylation or hydrogen loss are the major oxidation pathways in GS-Me, while they have not been observed in tryptophan-methionine and methionine-tryptophan (Trp-Met and Met-Trp). Interestingly, tryptophan is oxidized in the dipeptide Met-Trp, while that is not the case in the reverse sequence (Trp-Met).

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Section: Discussionmentioning

confidence: 87%

“…6 In methionine-containing dipeptides we have identified oxidized forms other than sulfoxide that appear after the oxidation of some peptides only. 6 In methionine-containing dipeptides we have identified oxidized forms other than sulfoxide that appear after the oxidation of some peptides only.…”

Section: And References Therein)mentioning

confidence: 96%

Tandem mass spectrometry and infrared spectroscopy as a tool to identify peptide oxidized residues

Scuderi

Ignasiak

Serfaty

et al. 2015

Phys. Chem. Chem. Phys.

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“…Importantly, the absence of fragmentation for oxidized ACTH 1–10 suggests that the presence of an oxidized methionine residue alone is not sufficient to enhance activation upon exposure to 10.6 μm IR light; congruent with studies that have shown oxidized methionine residues absorb light at approximately 9.5 μm, unless ion structure promotes S=O bond elongation. 40,50 …”

Section: Resultsmentioning

confidence: 99%

Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry

et al. 2017

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Protein S-sulfinylation (R-SO2−) and S-sulfonylation (R-SO3−) are irreversible oxidative post-translational modifications of cysteine residues. Greater than 5% of cysteines are reported to occupy these higher oxidation states, which effectively inactivate the corresponding thiols and alter the electronic and physical properties of modified proteins. Such higher oxidation states are reached after excessive exposure to cellular oxidants, and accumulate across different disease states. Despite widespread and functionally relevant cysteine oxidation across the proteome, there are currently no robust methods to profile higher order cysteine oxidation. Traditional data-dependent liquid chromatography/tandem mass spectrometry (LC/MS/MS) methods generally miss low occupancy modifications in complex analyses. Here, we present a data-independent acquisition (DIA) LC/MS-based approach, leveraging the high IR absorbance of sulfoxides at 10.6 μm, for selective dissociation and discovery of S-sulfonated peptides. Across peptide standards and protein digests, we demonstrate selective infrared multiphoton dissociation (IRMPD) of S-sulfonated peptides in the background of unmodified peptides. This selective DIA IRMPD LC/MS-based approach allows identification and annotation of S-sulfonated peptides across complex mixtures while providing sufficient sequence information to localize the modification site.

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“…[35]. It allowed us to confirm that the The peaks with their interpretation are collected in Table 2 173 (-CH 3 -CH 2 SO-CH 3 from parent ion) Table 2.…”

Section: What Are the Final Products Of Methionine Oxidation By  Oh mentioning

confidence: 49%

Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry

Scuderi

Bergès

Oliveira

et al. 2016

Radiation Physics and Chemistry

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Methionine is an essential amino acid, unfortunately prone to oxidation. The mechanism of its oxidation by • OH radicals has been studied for more than 40 years and still remains misunderstood. We have reinvestigated the oxidation of this residue in model peptides, aiming at i) improving the identification of free radicals by the use of more modern quantum chemistry methods; ii) reinvestigating the one-electron reduction potentials as a function of the position in the sequence; iii) identifying the final compounds, which were still unknown; iv) reinvestigating the intramolecular electron transfer (IET) involving this residue.

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Characterization by mass spectrometry and IRMPD spectroscopy of the sulfoxide group in oxidized methionine and related compounds

Cited by 31 publications

References 28 publications

Tandem mass spectrometry and infrared spectroscopy as a tool to identify peptide oxidized residues

Tandem mass spectrometry and infrared spectroscopy as a tool to identify peptide oxidized residues

Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry

Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry

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