S-nitrosation of cysteine as evidenced by IRMPD spectroscopy

Lanucara, Francesco; Chiavarino, Barbara; Crestoni, Maria Elisa; Scuderi, Debora; Sinha, Rajeev K.; Maı̂tre, Philippe; Fornarini, Simonetta

doi:10.1016/j.ijms.2012.07.003

Cited by 31 publications

(52 citation statements)

References 63 publications

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“…A different fragment ion, namely, HS − at m / z 33, was previously reported for native deprotonated cysteine, [cys−H] − , under both IRMPD and CID assay …”

Section: Resultsmentioning

confidence: 93%

“…The unambiguous and detailed characterization of the structural and dynamic behavior of these transient intermediates in isolated environments, in which external interferences are absent, will help to reveal intrinsic properties relevant to their biological activity. The inherent bonding and conformational features of cysteine in its (de)protonated, nitrosated, and metal‐tagged forms have been previously interrogated both in the free amino acid and in the residue embodied in the glutathione peptide by a joint computational and experimental infrared multiple photon dissociation (IRMPD) assay. IRMPD spectroscopy, coupled with ESI tandem mass spectrometry (MS/MS), is a pivotal tool to provide direct structural clues about gaseous (bio)molecular ions, including (de)protonation site, metal‐binding patterns, and local intramolecular interactions in both native and modified amino acids and peptides, DNA/RNA bases and nucleotides, cluster ions, and fragmentation products …”

Section: Introductionmentioning

confidence: 99%

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Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Scuderi

Bodo

Chiavarino

et al. 2016

Chemistry A European J

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The redox activity of cysteine sulfur allows numerous post-translational protein modifications involved in the oxidative regulation of metabolism, in metal binding, and in signal transduction. A combined approach based on infrared multiple photon dissociation spectroscopy at the Centre Laser Infrarouge d'Orsay (CLIO) free electron laser facility, calculations of IR frequencies, and finite temperature ab initio molecular dynamics simulations has been employed to characterize the gas-phase structures of deprotonated cysteine sulfenic, sulfinic, and sulfonic acids, [cysSO ] (x=1, 2, 3, representing the number of S-bound oxygen atoms), which are key intermediates in the redox-switching chemistry of proteins. The ions show different structural motifs owing to preferential binding of the proton to either the carboxylate or sulfur-containing group. Due to the decreasing basicity of the sulfenic, sulfinic, and sulfonic terminals, the proton bound to SO in [cysSO] migrates to the carboxylate in [cysSO ] , whereas it turns out to be shared in [cysSO ] . Evidence is gathered that a mixture of close-lying low-energy conformers is sampled for each cysteine oxo form in a Paul ion trap at room temperature.

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“…A different fragment ion, namely, HS − at m / z 33, was previously reported for native deprotonated cysteine, [cys−H] − , under both IRMPD and CID assay …”

Section: Resultsmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Scuderi

Bodo

Chiavarino

et al. 2016

Chemistry A European J

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“…IRMPD spectroscopy thus serves as a direct structural probe of gas-phase ions and can be used for structural elucidation of said ions, especially when combined with theoretical infrared (IR) frequency calculations and/or comparison to experimental spectra of synthetic standards. This technique has proven successful in many areas, including the study of PTMs [18][19][20][21] and of the fragmentation chemistry of peptides [22][23][24][25] and remains promising for many additional future applications.…”

Section: Introductionmentioning

confidence: 99%

Insights into the fragmentation pathways of gas-phase protonated sulfoserine

Patrick

Stedwell

Schindler

et al. 2015

International Journal of Mass Spectrometry

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“…34–38 Other reports have demonstrated the use of gas-phase IR spectroscopic signatures as a means to identify the presence of phosphorylation, nitrosation, and oxidative-based PTMs. 39–41 Despite the fact that sulfoxides absorb at a similar wavelength as phosphates, the application of infrared multiphoton dissociation (IRMPD) to sulfoxide-containing peptides has been limited. 42–45 In fact, this methodology has, to our knowledge, not previously been applied to peptides containing cysteine-based oxidative modifications.…”

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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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S-nitrosation of cysteine as evidenced by IRMPD spectroscopy

Cited by 31 publications

References 63 publications

Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Insights into the fragmentation pathways of gas-phase protonated sulfoserine

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

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