Consecutive laser-induced photodissociation as a probe of ion structure

Bowers, William D.; Delbert, S.; McIver, Robert T.

doi:10.1021/ac00295a066

Cited by 54 publications

(17 citation statements)

References 27 publications

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“…Absorption of UV/vis photons by ions occurs by resonant photon absorption from the ground to an excited electronic state and commonly results in photodissociation of the excited ion. Photodissociation of peptides and small proteins has been achieved using 193 nm (6.42 eV) photons (Bowers et al, 1984;Bowers, Delbert, & McIver, 1986;Williams, Furlong, & McLafferty, 1990;Beu et al, 1993). However, photodissociation of larger proteins (ubiquitin ions, 8.6 kDa) resulted in formation of small, uninformative fragment ions (Beu et al, 1993).…”

Section: Multiphoton Dissociationmentioning

confidence: 99%

Activation of large lons in FT‐ICR mass spectrometry

Laskin

Futrell

2004

Mass Spectrometry Reviews

177

146

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The advent of soft ionization techniques, notably electrospray and laser desorption ionization methods, has enabled the extension of mass spectrometric methods to large molecules and molecular complexes. This both greatly extends the applications of mass spectrometry and makes the activation and dissociation of complex ions an integral part of these applications. This review emphasizes the most promising methods for activation and dissociation of complex ions and presents this discussion in the context of general knowledge of reaction kinetics and dynamics largely established for small ions. We then introduce the characteristic differences associated with the higher number of internal degrees of freedom and high density of states associated with molecular complexity. This is reflected primarily in the kinetics of unimolecular dissociation of complex ions, particularly their slow decay and the higher energy content required to induce decomposition-the kinetic shift (KS). The longer trapping time of Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) significantly reduces the KS, which presents several advantages over other methods for the investigation of dissociation of complex molecules. After discussing general principles of reaction dynamics related to collisional activation of ions, we describe conventional ways to achieve single-and multiple-collision activation in FT-ICR MS. Sustained off-resonance irradiation (SORI)-the simplest and most robust means of introducing the multiple collision activation process-is discussed in greatest detail. Details of implementation of this technique, required control of experimental parameters, limitations, and examples of very successful application of SORI-CID are described. The advantages of high mass resolving power and the ability to carry out several stages of mass selection and activation intrinsic to FT-ICR MS are demonstrated in several examples. Photodissociation of ions from small molecules can be effected using IR or UV/vis lasers and generally requires tuning lasers to specific wavelengths and/ or utilizing high flux, multiphoton excitation to match energy levels in the ion. Photodissociation of complex ions is much easier to accomplish from the basic physics perspective. The quasi-continuum of vibrational states at room temperature makes it very easy to pump relatively large amounts of energy into complex ions and infrared multiphoton dissociation (IRMPD) is a powerful technique for characterizing large ions, particularly biologically relevant molecules. Since both SORI-CID and IRMPD are slow activation methods they have many common characteristics. They are also distinctly different because SORI-CID is intrinsically selective (only ions that have a cyclotron frequency close to the frequency of the excitation field are excited), whereas IRMPD is not (all ions that reside on the optical path of the laser are excited). There are advantages and disadvantages to each technique and in many applications they complement each other. In contrast wi...

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Section: Multiphoton Dissociationmentioning

confidence: 99%

Activation of large lons in FT‐ICR mass spectrometry

Laskin

Futrell

2004

Mass Spectrometry Reviews

177

146

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“…promising for the sequencing of oligopeptides [4][5][6] and phospholipids [7). Among the instruments available for such MSIMS applications, the Fourier transform (FT) mass s p ectrometer [8][9][10][11][12][13][14][15] has the unusual capabilities of multichannel measurement of all stored ion s, the use of a single mass analyzer for multiple ma ss separations (M5 n ) sequential in time, unusually high resolution, and a high upper mass range, p rompting this further study of methods for dissociating ions mass-selected by FTMS.…”

Section: 1mentioning

confidence: 99%

Efficiency of collisionally-activated dissociation and 193-nm photodissociation of peptide ions in fourier transform mass spectrometry

Williams

Furlong

McLafferty

1990

J. Am. Soc. Mass Spectrom.

107

109

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For tandem mass spectrometry, the Fourier transform instrument exhibits advantages for the use of collisionally-activated dissociation (CAD). The CAD energy deposited in larger ions can be greatly increased by extending the collision time to as much as 120 s, and the efficiency of trapping and measuring CAD product ions is many times greater than that found for triple-quadrupole or magnetic sector instruments, although the increased pressure from the collision gas is an offsetting disadvantage. A novel system that uses the same laser for photodesorption of ions and their subsequent photodissociation can produce complete dissociation of larger oligopeptide ions and unusually abundant fragment ions. In comparison to CAD, much more internal energy can be deposited in the primary ions using 193-nm photons, sufficient to dissociate peptide ions of m/z > 2000. Mass spectra closely resembling ion photodissociation spectra can also be obtained by' neutral photodissociation (193-nm laser irradiation of the sample) followed by ion photodesorption.

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“…In particular, the possibility of modifying the relative yield of fragmentation in this channel by tuning the delay between pump and probe lasers in time‐resolved experiments,16 or by varying the laser wavelength,11 was demonstrated. As complements to these energy‐ and time‐resolved photodissociation experiments, multi‐stage mass spectrometry combined with photodissociation experiments (LID‐MS n ) has been used to determine fragment lineages and to obtain a better understanding of ion structures 11, 17…”

mentioning

confidence: 99%

Specific photodissociation of peptides with multi‐stage mass spectrometry

Tabarin

Antoine

Broyer

et al. 2005

Rapid Comm Mass Spectrometry

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We report collision-induced dissociation (CID) and laser-induced dissociation (LID) performed at different wavelengths between 220 and 280 nm of the peptides leucine-enkephalin (protonated) and gramicidin A (sodiated). Hydrogen-atom losses and side-chain cleavages were observed in LID experiments. These losses depend on the laser wavelength and lead to the formation of radical ions. The fragmentations of these radicals, which are not observed in CID experiments, were investigated in multi-stage mass spectrometry experiments.

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Consecutive laser-induced photodissociation as a probe of ion structure

Abstract: Resources Research Institute for financial assistance. press. 95.(2) Raghavan, S.; Unger, K. Trans. Insf. Min, Mete//. Sect. C 1983, 92, (3) Walker, G. T. Manuf. Chem. 1953, 24, 376. (4) Walker, 0. T.; Freeman, F. M. Manuf. Chem. 1955, 26, 13.

Cited by 54 publications

References 27 publications

Activation of large lons in FT‐ICR mass spectrometry

Activation of large lons in FT‐ICR mass spectrometry

Efficiency of collisionally-activated dissociation and 193-nm photodissociation of peptide ions in fourier transform mass spectrometry

Specific photodissociation of peptides with multi‐stage mass spectrometry

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