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FT-ICR Mass Spectrometry: History
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Contributor: Helena Kang

Ion cyclotron motion in a strong magnetic field, recorded as an image-current transient and converted by Fourier transformation into a frequency-domain mass spectrum, defines Fourier-transform ion-cyclotron-resonance (FT-ICR) mass spectrometry. Trapped ions orbit at a cyclotron frequency inversely proportional to their mass-to-charge ratio; broadband excitation and detection of that motion yield ultra-high mass resolving power and mass accuracy [1]. The same trapped-ion population can be activated by collisions or by electron capture, so that tandem spectra report connectivity without leaving the ICR cell [2]. Conceptual boundaries exclude quadrupole, time-of-flight, and Orbitrap Fourier-transform instruments that do not use cyclotron motion in a homogeneous magnet, although all Fourier-transform mass spectrometers share the time-to-frequency conversion step. Essential features are a high-field magnet, an ion trap that supports coherent cyclotron motion, and a Fourier-transform data system. Exact-composition assignment in complex mixtures and localization of noncovalent ligand sites are analytical consequences of the mass accuracy and tandem capabilities inherent in the ICR measurement principle [3]. An FT-ICR spectrum of dissolved organic matter is correspondingly interpreted as a catalogue of exact molecular compositions rather than as a chromatographic retention map [4].

  • FT-ICR
  • ion cyclotron resonance
  • Fourier transform
  • high-resolution mass spectrometry

Mass Spectrometry Techniques and Applications • Spectroscopy • Chemistry • Physical Sciences

References

  1. Stephen C. Brown; Gary Kruppa; Jean‐Louis Dasseux; Metabolomics applications of FT‐ICR mass spectrometry. Mass Spectrom. Rev. 2004, 24, 223-231, 10.1002/mas.20011.
  2. Julia Laskin; Jean H. Futrell; Collisional activation of peptide ions in FT‐ICR mass spectrometry. Mass Spectrom. Rev. 2003, 22, 158-181, 10.1002/mas.10041.
  3. Yongming Xie; Jennifer Zhang; Sheng Yin; Joseph A. Loo; Top-Down ESI-ECD-FT-ICR Mass Spectrometry Localizes Noncovalent Protein-Ligand Binding Sites. J. Am. Chem. Soc. 2006, 128, 14432-14433, 10.1021/ja063197p.
  4. Chen He; Yahe Zhang; Yunyun Li; Xiaocun Zhuo; Yuguo Li; Chuanlun Zhang; Quan Shi; In-House Standard Method for Molecular Characterization of Dissolved Organic Matter by FT-ICR Mass Spectrometry. ACS Omega 2020, 5, 11730-11736, 10.1021/acsomega.0c01055.
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