Tyrosine nitration as evidenced by IRMPD spectroscopy

Rajeev K. Sinha, Barbara Chiavarino, Maria Elisa Crestoni, Debora Scuderi, Simonetta Fornarini

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Protonated 3-nitrotyrosine ([nitroTyr + H] +) has been investigated by collision induced dissociation at variable energy and by IR multiple photon dissociation (IRMPD) spectroscopy in conjunction with quantum chemical calculations. Ultimately, this investigation is aimed at providing a diagnostic signature of protein tyrosine nitration, a post translational modification implied in pathological states. IRMPD spectroscopy of [nitroTyr + H] + ions has been examined in two different spectral regions, namely in the 1000-2000 cm -1 range, using the free electron laser beamline at the CLIO facility, and in the 3200-3700 cm -1 range, using a tabletop laser source. [nitroTyr + H] + ions have been assayed in parallel with intact [Tyr + H] + ions revealing characteristic bands at 1329 and 1540 cm -1. Mode assignments allowed by density functional theory calculations of the IR spectra of the most stable conformers indicate that these features are associated to vibrations of the nitro group and are endowed with enhanced activity. In the NH/OH stretching region, the remarkable difference between the IRMPD spectra is the strong absorption at 3641 cm -1 of the ring OH stretching of [Tyr + H] + which is absent in the nitrated ion due to a strong hydrogen bond engaging the ring OH and the ortho nitro group. These results suggest that IRMPD spectroscopy and tandem mass spectrometry may afford a selective method for the analysis and characterization of 3-nitrotyrosine, to be possibly extended to 3-nitrotyrosine-containing peptides.

Original languageEnglish
Pages (from-to)209-216
Number of pages8
JournalInternational Journal of Mass Spectrometry
Volume308
Issue number2-3
DOIs
Publication statusPublished - 01-12-2011

Fingerprint

nitration
Nitration
tyrosine
Tyrosine
Photons
Spectroscopy
dissociation
Ions
photons
spectroscopy
Stretching
ions
rings
Free electron lasers
free electron lasers
Peptides
peptides
Density functional theory
Mass spectrometry
Hydrogen bonds

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Condensed Matter Physics
  • Instrumentation

Cite this

Sinha, Rajeev K. ; Chiavarino, Barbara ; Crestoni, Maria Elisa ; Scuderi, Debora ; Fornarini, Simonetta. / Tyrosine nitration as evidenced by IRMPD spectroscopy. In: International Journal of Mass Spectrometry. 2011 ; Vol. 308, No. 2-3. pp. 209-216.
@article{592e34f59f164485adc2c8919813c016,
title = "Tyrosine nitration as evidenced by IRMPD spectroscopy",
abstract = "Protonated 3-nitrotyrosine ([nitroTyr + H] +) has been investigated by collision induced dissociation at variable energy and by IR multiple photon dissociation (IRMPD) spectroscopy in conjunction with quantum chemical calculations. Ultimately, this investigation is aimed at providing a diagnostic signature of protein tyrosine nitration, a post translational modification implied in pathological states. IRMPD spectroscopy of [nitroTyr + H] + ions has been examined in two different spectral regions, namely in the 1000-2000 cm -1 range, using the free electron laser beamline at the CLIO facility, and in the 3200-3700 cm -1 range, using a tabletop laser source. [nitroTyr + H] + ions have been assayed in parallel with intact [Tyr + H] + ions revealing characteristic bands at 1329 and 1540 cm -1. Mode assignments allowed by density functional theory calculations of the IR spectra of the most stable conformers indicate that these features are associated to vibrations of the nitro group and are endowed with enhanced activity. In the NH/OH stretching region, the remarkable difference between the IRMPD spectra is the strong absorption at 3641 cm -1 of the ring OH stretching of [Tyr + H] + which is absent in the nitrated ion due to a strong hydrogen bond engaging the ring OH and the ortho nitro group. These results suggest that IRMPD spectroscopy and tandem mass spectrometry may afford a selective method for the analysis and characterization of 3-nitrotyrosine, to be possibly extended to 3-nitrotyrosine-containing peptides.",
author = "Sinha, {Rajeev K.} and Barbara Chiavarino and Crestoni, {Maria Elisa} and Debora Scuderi and Simonetta Fornarini",
year = "2011",
month = "12",
day = "1",
doi = "10.1016/j.ijms.2011.07.012",
language = "English",
volume = "308",
pages = "209--216",
journal = "International Journal of Mass Spectrometry",
issn = "1387-3806",
publisher = "Elsevier",
number = "2-3",

}

Sinha, RK, Chiavarino, B, Crestoni, ME, Scuderi, D & Fornarini, S 2011, 'Tyrosine nitration as evidenced by IRMPD spectroscopy', International Journal of Mass Spectrometry, vol. 308, no. 2-3, pp. 209-216. https://doi.org/10.1016/j.ijms.2011.07.012

Tyrosine nitration as evidenced by IRMPD spectroscopy. / Sinha, Rajeev K.; Chiavarino, Barbara; Crestoni, Maria Elisa; Scuderi, Debora; Fornarini, Simonetta.

In: International Journal of Mass Spectrometry, Vol. 308, No. 2-3, 01.12.2011, p. 209-216.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Tyrosine nitration as evidenced by IRMPD spectroscopy

AU - Sinha, Rajeev K.

AU - Chiavarino, Barbara

AU - Crestoni, Maria Elisa

AU - Scuderi, Debora

AU - Fornarini, Simonetta

PY - 2011/12/1

Y1 - 2011/12/1

N2 - Protonated 3-nitrotyrosine ([nitroTyr + H] +) has been investigated by collision induced dissociation at variable energy and by IR multiple photon dissociation (IRMPD) spectroscopy in conjunction with quantum chemical calculations. Ultimately, this investigation is aimed at providing a diagnostic signature of protein tyrosine nitration, a post translational modification implied in pathological states. IRMPD spectroscopy of [nitroTyr + H] + ions has been examined in two different spectral regions, namely in the 1000-2000 cm -1 range, using the free electron laser beamline at the CLIO facility, and in the 3200-3700 cm -1 range, using a tabletop laser source. [nitroTyr + H] + ions have been assayed in parallel with intact [Tyr + H] + ions revealing characteristic bands at 1329 and 1540 cm -1. Mode assignments allowed by density functional theory calculations of the IR spectra of the most stable conformers indicate that these features are associated to vibrations of the nitro group and are endowed with enhanced activity. In the NH/OH stretching region, the remarkable difference between the IRMPD spectra is the strong absorption at 3641 cm -1 of the ring OH stretching of [Tyr + H] + which is absent in the nitrated ion due to a strong hydrogen bond engaging the ring OH and the ortho nitro group. These results suggest that IRMPD spectroscopy and tandem mass spectrometry may afford a selective method for the analysis and characterization of 3-nitrotyrosine, to be possibly extended to 3-nitrotyrosine-containing peptides.

AB - Protonated 3-nitrotyrosine ([nitroTyr + H] +) has been investigated by collision induced dissociation at variable energy and by IR multiple photon dissociation (IRMPD) spectroscopy in conjunction with quantum chemical calculations. Ultimately, this investigation is aimed at providing a diagnostic signature of protein tyrosine nitration, a post translational modification implied in pathological states. IRMPD spectroscopy of [nitroTyr + H] + ions has been examined in two different spectral regions, namely in the 1000-2000 cm -1 range, using the free electron laser beamline at the CLIO facility, and in the 3200-3700 cm -1 range, using a tabletop laser source. [nitroTyr + H] + ions have been assayed in parallel with intact [Tyr + H] + ions revealing characteristic bands at 1329 and 1540 cm -1. Mode assignments allowed by density functional theory calculations of the IR spectra of the most stable conformers indicate that these features are associated to vibrations of the nitro group and are endowed with enhanced activity. In the NH/OH stretching region, the remarkable difference between the IRMPD spectra is the strong absorption at 3641 cm -1 of the ring OH stretching of [Tyr + H] + which is absent in the nitrated ion due to a strong hydrogen bond engaging the ring OH and the ortho nitro group. These results suggest that IRMPD spectroscopy and tandem mass spectrometry may afford a selective method for the analysis and characterization of 3-nitrotyrosine, to be possibly extended to 3-nitrotyrosine-containing peptides.

UR - http://www.scopus.com/inward/record.url?scp=80955142874&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80955142874&partnerID=8YFLogxK

U2 - 10.1016/j.ijms.2011.07.012

DO - 10.1016/j.ijms.2011.07.012

M3 - Article

VL - 308

SP - 209

EP - 216

JO - International Journal of Mass Spectrometry

JF - International Journal of Mass Spectrometry

SN - 1387-3806

IS - 2-3

ER -