Mass spectrometry with ion sources operating at atmospheric pressure

Bruins, Andries P.

doi:10.1002/mas.1280100104

Cited by 301 publications

(193 citation statements)

References 106 publications

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“…Submillimeter glass and copper particles (approximately 50-60 mm in diameter) have been confined in the Kingdon trap to study orbital mechanics, with possible implications for understanding the dynamics of asteroids, galaxies, and planetary rings (Biewer et al, 1994;Robertson, 1995;Robertson & Alexander, 1995). Kingdon traps have also been used to study electron capture from neutral atoms by confined ions (Prior, Marrus, & Vane, 1983;Vane, Prior, & Marrus, 1981), measure rates of collisional quenching (Calamai & Johnson, 1990, 1991, 1992Prior, 1984) and to develop the orbitron ion pump (Douglas, Zabritski, & Herb, 1965).…”

Section: Orbital Trapping and Kingdon Trapsmentioning

confidence: 99%

“…Atmospheric pressure ionization (API) (Bruins, 1991;Carroll et al, 1974;Horning et al, 1973) sources such as ESI (Dole, Mack, & Hines, 1968;Fenn et al, 1989;Whitehouse et al, 1985;Yamashita & Fenn, 1984a,b) and atmospheric pressure chemical ionization (APCI) (Carroll et al, 1975;Horning et al, 1974a,b) coupled with mass spectrometers, especially high performance FIGURE 12. Schematic of an early prototype instrument that uses electrostatic acceleration lenses to inject ions produced by LD into the orbitrap.…”

Section: B Linear Quadrupole Ion Trapmentioning

confidence: 99%

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Orbitrap mass spectrometry: Instrumentation, ion motion and applications

Perry

Cooks

Noll

2008

Mass Spectrometry Reviews

406

290

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Since its introduction, the orbitrap has proven to be a robust mass analyzer that can routinely deliver high resolving power and mass accuracy. Unlike conventional ion traps such as the Paul and Penning traps, the orbitrap uses only electrostatic fields to confine and to analyze injected ion populations. In addition, its relatively low cost, simple design and high space‐charge capacity make it suitable for tackling complex scientific problems in which high performance is required. This review begins with a brief account of the set of inventions that led to the orbitrap, followed by a qualitative description of ion capture, ion motion in the trap and modes of detection. Various orbitrap instruments, including the commercially available linear ion trap–orbitrap hybrid mass spectrometers, are also discussed with emphasis on the different methods used to inject ions into the trap. Figures of merit such as resolving power, mass accuracy, dynamic range and sensitivity of each type of instrument are compared. In addition, experimental techniques that allow mass‐selective manipulation of the motion of confined ions and their potential application in tandem mass spectrometry in the orbitrap are described. Finally, some specific applications are reviewed to illustrate the performance and versatility of the orbitrap mass spectrometers. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 27: 661–699, 2008

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Section: Orbital Trapping and Kingdon Trapsmentioning

confidence: 99%

Section: B Linear Quadrupole Ion Trapmentioning

confidence: 99%

Orbitrap mass spectrometry: Instrumentation, ion motion and applications

Perry

Cooks

Noll

2008

Mass Spectrometry Reviews

406

290

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“…Mass Spectrometry-Electrospray (ES) mass spectrometry (MS) was performed on an API3000 mass spectrometer (Applied Biosystems/ MDS-SCIEX, Toronto, Canada), a triple quadrupole mass spectrometer supplied with an atmospheric pressure ionization source, and an ionspray interface (13). The spectra were scanned in the range between m/z 400 and 1600.…”

Section: Analysis Of Conformation By Circular Dichroismmentioning

confidence: 99%

Identification of the Catalytic Residues of α-Amino Acid Ester Hydrolase from Acetobacter turbidans by Labeling and Site-directed Mutagenesis

Polderman-Tijmes¹,

Jekel²,

Jeronimus-Stratingh³

et al. 2002

Journal of Biological Chemistry

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The ␣-amino acid ester hydrolase from Acetobacter turbidans ATCC 9325 is capable of hydrolyzing and synthesizing the side chain peptide bond in ␤-lactam antibiotics. Data base searches revealed that the enzyme contains an active site serine consensus sequence Gly-X-Ser-Tyr-X-Gly that is also found in X-prolyl dipeptidyl aminopeptidase. The serine hydrolase inhibitor p-nitrophenyl-p-guanidino-benzoate appeared to be an active site titrant and was used to label the ␣-amino acid ester hydrolase. Electrospray mass spectrometry and tandem mass spectrometry analysis of peptides from a to an alanine almost fully inactivated the enzyme, whereas mutation of the other residues did not seriously affect the enzyme activity. Circular dichroism measurements showed that the inactivation was not caused by drastic changes in the tertiary structure. Therefore, we conclude that the catalytic domain of the ␣-amino acid ester hydrolase has an ␣/␤-hydrolase fold structure with a catalytic triad of Ser 205 , Asp 338 , and His 370 . This distinguishes the ␣-amino acid ester hydrolase from the Ntnhydrolase family of ␤-lactam antibiotic acylases.

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“…While high-efficiency front-end separations are necessary to minimize ionization suppression and increase coverage of the detectable metabolome by LC-MS-based methods in biomarker discovery applications, of equal importance is the use of low LC flow rates in order to increase the ESI-MS efficiency (defined as the number of analyte ions recorded at the MS detector divided by the number of molecules delivered to the ESI emitter [119]) and, therefore, the overall sensitivity of the measurement [105,120,121]. The primary reason for increased ESI efficiency is the production of smaller charged droplets at lower flow rates [122,123], enabling more efficient solvent evaporation and requiring fewer Coulombic fission events to create gasphase ions.…”

Section: Miniaturization Of Ionization Sourcesmentioning

confidence: 99%

Future of Liquid Chromatography–Mass Spectrometry in Metabolic Profiling and Metabolomic Studies for Biomarker Discovery

et al. 2007

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SUMMARYThe future utility of liquid chromatography-mass spectrometry (LC-MS) in metabolic profiling and metabolomic studies for biomarker discover will be discussed, beginning with a brief description of the evolution of metabolomics and the utilization of the three most popular analytical platforms in such studies: NMR, GC-MS, and LC-MS. Emphasis is placed on recent developments in highefficiency LC separations, sensitive electrospray ionization approaches, and the benefits to incorporating both in LC-MS-based approaches. The advantages and disadvantages of various quantitative approaches are reviewed, followed by the current LC-MS-based tools available for candidate biomarker characterization and identification. Finally, a brief prediction on the future path of LC-MS-based methods in metabolic profiling and metabolomic studies is given.

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Mass spectrometry with ion sources operating at atmospheric pressure

Cited by 301 publications

References 106 publications

Orbitrap mass spectrometry: Instrumentation, ion motion and applications

Orbitrap mass spectrometry: Instrumentation, ion motion and applications

Identification of the Catalytic Residues of α-Amino Acid Ester Hydrolase from Acetobacter turbidans by Labeling and Site-directed Mutagenesis

Future of Liquid Chromatography–Mass Spectrometry in Metabolic Profiling and Metabolomic Studies for Biomarker Discovery

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