Determination of Relative Ordering of Activation Energies for Gas-Phase Ion Unimolecular Dissociation by Infrared Radiation for Gaseous Multiphoton Energy Transfer

Freitas, Michael A.; Hendrickson, and Christopher L.; Marshall, Alan G.

doi:10.1021/ja9925397

Cited by 39 publications

(76 citation statements)

References 71 publications

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“…There is an excellent agreement between master equation modeling (open symbols) and the blackbody curve (line). There is a slight deviation between the actual IED for (Ala-Gly) 8 ions excited by cw laser (dashed line) and blackbody irradiation (solid line) as shown in Figure 16 (Freitas, Hendrickson, & Marshall, 2000).…”

Section: Internal Energy Distributionmentioning

confidence: 98%

“…This correction decreases rapidly with increase in the size of the molecule and is expected to be negligibly small for large molecules. For example, Marshall and co-workers found that for (AlaGly) 8 H þ there is an almost perfect overlap between the IEDs of ions with and without dissociation (Freitas, Hendrickson, & Marshall, 2000), implying that the reactive depletion correction for this size system is close to zero. The corresponding correction for excited n-butylbenzene ions is 0.05 eV (Uechi & Dunbar, 1992).…”

Section: Kinetics Of Irmpdmentioning

confidence: 99%

“…If ion dissociation is fast relative to ion activation the thermal distribution is depleted. Similarly to BIRD depletion of the thermal distribution by IRMPD has been modeled using master equation modeling (Dunbar, 1991;Uechi & Dunbar, 1992;Dunbar & Zaniewski, 1992;Jockusch, Paech, & Williams, 2000;Freitas, Hendrickson, & Marshall, 2000;Paech, Jockusch, & Williams, 2002). In master equation modeling, the entire internal energy range is divided in small bins.…”

Section: Internal Energy Distributionmentioning

confidence: 99%

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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: Internal Energy Distributionmentioning

confidence: 98%

Section: Kinetics Of Irmpdmentioning

confidence: 99%

Section: Internal Energy Distributionmentioning

confidence: 99%

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Activation of large lons in FT‐ICR mass spectrometry

Laskin

Futrell

2004

Mass Spectrometry Reviews

177

146

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“…Similarly, IRMPD can be used for the determination of the activation energy, E a , for gas-phase unimolecular dissociation reactions. This approach was first introduced for small molecules (Ͻ50 atoms) by Dunbar [38,39], and later extended to large biomolecules (Ͼ50 atoms) by Marshall and coworkers [40,41]. These authors renamed the technique as focused radiation for gaseous multiphoton energy-transfer (FRAGMENT).…”

mentioning

confidence: 99%

“…In addition, to study the effect of Fe(III) binding on the unimolecular kinetics and relative activation energies for the dissociation of enterobactin in the gas phase, time-resolved IRMPD experiments were carried out on ent and ent-Fe(III). The FRAGMENT method [40,41]üwasüemployedüto determine relative dissociation energetics.…”

mentioning

confidence: 99%

Infrared multiphoton dissociation of the siderophore enterobactin and its Fe(III) complex. Influence of Fe(III) binding on dissociation kinetics and relative energetics

Leslie

Daneshfar

Volmer

2007

J. Am. Soc. Mass Spectrom.

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The dissociation pathways of the siderophore enterobactin and its complex with Fe(III) were examined using infrared multiphoton dissociation (IRMPD). Under experimental conditions (pH ϭ 3.5), both compounds' electrospray spectra exhibited exclusively singly-charged anions. The compositions of the dissociation products were characterized by accurate mass measurements using Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS). The primary dissociation channel for both species was determined to be the loss of one serine group from the precursor molecules. To further investigate the influence of Fe(III) binding on the intramolecular interactions, dissociation kinetics and relative energetics for the loss of this serine group were determined using the focused radiation for gaseous multiphoton energytransfer (FRAGMENT) method. From the kinetic data, it was found that enterobactin was ϳseven times more reactive than its Fe(III) complex over the range of laser intensities investigated. The relative activation energies, however, exhibited similar values, ϳ7 kcal · mol Ϫ1 . These results suggest that at pH ϭ 3.5, Fe(III) interacts with only two of the three serine groups. The results from the present work are believed to be valuable for the characterization of novel siderophores as well as their associated metabolites and synthetic analogues. (J Am Soc Mass Spectrom 2007, 18, 632-641)

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Ion Dissociation Methods in Proteomics

Rathore

Aboufazeli

Huang

et al. 2015

Encyclopedia of Analytical Chemistry

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This article serves as a review of polypeptide ion dissociation methods in the context of mass spectrometry (MS)‐based proteomic analysis. Given the many tandem mass spectrometry (MS/MS) instrument types and ion fragmentation approaches presently in use, the proteomic analyst is confronted with numerous methodological considerations in selecting and implementing an ion fragmentation technique for primary structure determination of polypeptides. Because the physical and chemical bases for a given mode of dissociation largely dictate the outcome of an MS/MS experiment, the underlying fundamental principles and the manner of executing each fragmentation approach must inform any subsequent spectral interpretation. Here, we endeavor to encapsulate the current state of the art in peptide and protein ion fragmentation methods, including methods in widespread use for proteomic analysis and maturing but less commonly applied approaches with significant potential in the field of proteomics. A general overview of MS/MS and polypeptide ion fragmentation is followed by a discussion of the fundamental basis for several ion dissociation approaches and how each technique is implemented in various MS/MS hardware configurations. Representative examples from the literature are also highlighted, with emphasis on the unique features and specific strengths of each dissociation method. Finally, several proposed peptide ion fragmentation mechanisms and fragment ion structures are presented.

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Determination of Relative Ordering of Activation Energies for Gas-Phase Ion Unimolecular Dissociation by Infrared Radiation for Gaseous Multiphoton Energy Transfer

Cited by 39 publications

References 71 publications

Activation of large lons in FT‐ICR mass spectrometry

Activation of large lons in FT‐ICR mass spectrometry

Infrared multiphoton dissociation of the siderophore enterobactin and its Fe(III) complex. Influence of Fe(III) binding on dissociation kinetics and relative energetics

Ion Dissociation Methods in Proteomics

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