Development of a Tandem Mass Spectrometry Instrument for Probing High-Energy Electron Transfer Dissociation

Nagao, Hirofumi; Hayakawa, Shigeo; Hashimoto, Mami; Iwamoto, Kaoru; Toyoda, Michisato; Shigeri, Yasushi; Jitosho, Mamiko; Awazu, Kunio

doi:10.5702/massspec.57.123

Cited by 2 publications

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“…The quadrupole lens doublet mounted between the JMS-HX110 and the collision cell improved the efficiency of ion transmission into the collision cell about 10 times. By applying 11 kV to the curved type conversion dynode, ion intensities of charge reduced fragment ions of both lower and higher masses than those of the precursor ions were significantly increased [46].…”

Section: Tandem Mass Spectrometry For High-energy Collision Induced Dmentioning

confidence: 98%

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High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

Hayakawa

Matsumoto

Hashimoto

et al. 2010

J. Am. Soc. Mass Spectrom.

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Post-translational modifications (PTMs) of proteins are important in the activation, localization, and regulation of protein function in vivo. The usefulness of electron capture dissociation (ECD) and electron-transfer dissociation (ETD) in tandem mass spectrometry (MS/MS) using low-energy (LE) trap type mass spectrometer is associated with no loss of a labile PTM group regarding peptide and protein sequencing. The experimental results of high-energy (HE) collision induced dissociation (CID) using the Xe and Cs targets and LE-ETD were compared for doubly-phosphorylated peptides TGFLT(p)EY(p)VATR (1). Although HE-CID using the Xe target did not provide information on the amino acid sequence, HE-CID using the Cs target provided all the z-type ions without loss of the phosphate groups as a result of HE-ETD process, while LE-ETD using fluoranthene anion gave only z-type ions from z 5 to z 11 . The difference in the results of HE-CID between the Xe and Cs targets demonstrated that HE-ETD process with the Cs target took place much more dominantly than collisional activation. The difference between HE-ETD using Cs targets and LE-ETD using the anion demonstrated that mass discrimination was much weaker in the high-energy process. HE-ETD was also applied to three other phosphopeptides YGGMHRQEX(p)VDC (2: X ϭ S, 3: X ϭ T, 4: X ϭ Y). The HE-CID spectra of the doubly-protonated phosphopeptides () of 2, 3, and 4 using the Cs target showed a very similar feature that the c-type ions from c 7 to c 11 and the z-type ions from z 7 to z 11 were formed via N-C␣ bond cleavage without a loss of the phosphate group. (J Am Soc Mass Spectrom 2010, 21, 1482-1489) © 2010 American Society for Mass Spectrometry P ost-translational modifications (PTMs) of proteins are important in vivo, especially, reversible protein phosphorylation, principally localized on serine, threonine, or tyrosine residues, is one of the most important and well-studied. Phosphorylations play crucial roles in the regulation of cellular processes such as cell cycle, cell growth, apoptosis, and signal transduction [1,2]. Although the mass analysis of phosphorylated proteins and peptides has become possible since the development of electrospray ionization (ESI) technique [3], the determination of phosphorylated positions has not yet been achieved by the most popular dissociation method, namely, a low-energy collisionally activated dissociation (LE-CAD) performed by using the tandem mass spectrometry (MS/ MS) [4]. Electron capture dissociation (ECD) using a Fourier transform ion cyclotron resonant mass spectrometer (FT-ICR-MS) [5][6][7][8] and electron-transfer dissociation (ETD) using a linear trap mass spectrometer [9,10] can provide information on c-and z-type ions [11,12] produced via N-C␣ backbone cleavage with no loss of labile PTM groups, such as phosphate and sulfate groups [13,14]. The N-C␣ backbone cleavage is different from other fragmentations brought about by collisional activation or infrared photoexcitation of closedshell cations [15]. The charge reduced p...

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Section: Tandem Mass Spectrometry For High-energy Collision Induced Dmentioning

confidence: 98%

“…In the present instrument, a quadrupole lens doublet was newly mounted and the conversion dynode of the detector was changed from the flat type used in the previous instrument [39,46] to a curved type. A schematic of the modified instrument is shown in Figure 1.…”

Section: Tandem Mass Spectrometry For High-energy Collision Induced Dmentioning

confidence: 99%

High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

Hayakawa

Matsumoto

Hashimoto

et al. 2010

J. Am. Soc. Mass Spectrom.

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Current literature in mass spectrometry

2010

J. Mass Spectrom.

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In order to keep subscribers up‐to‐date with the latest developments in their field, John Wiley & Sons are providing a current awareness service in each issue of the journal. The bibliography contains newly published material in the field of mass spectrometry. Each bibliography is divided into 11 sections: 1 Reviews; 2 Instrumental Techniques & Methods; 3 Gas Phase Ion Chemistry; 4 Biology/Biochemistry: Amino Acids, Peptides & Proteins; Carbohydrates; Lipids; Nucleic Acids; 5 Pharmacology/Toxicology; 6 Natural Products; 7 Analysis of Organic Compounds; 8 Analysis of Inorganics/Organometallics; 9 Surface Analysis; 10 Environmental Analysis; 11 Elemental Analysis. Within each section, articles are listed in alphabetical order with respect to author

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Development of a Tandem Mass Spectrometry Instrument for Probing High-Energy Electron Transfer Dissociation

Cited by 2 publications

References 23 publications

High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

Current literature in mass spectrometry

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