Plasma desorption mass spectrometry: coming of age

Cotter, Robert J.

doi:10.1021/ac00164a002

Cited by 67 publications

(7 citation statements)

References 65 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Given the amino acid composition of the Wavelength (nrn) peptide, we should conclude that this value may represent a dimeric form of the peptide Val-Ala-Pro-Cys (chromophore). This conclusion is also supported by the general observation for PDMS spectra of small peptides that the M + 2H+/2 mass values are smaller than the MH+ values (Cotter, 1988). We have no idea, however, how such a dimer would be formed.…”

Section: Proteinase K Digestsupporting

confidence: 61%

“…The uncertainty about the latter part of the protein was taken away by measuring the precise mass of peptide H7, the C-terminal peptide of the protein obtained after the partial acid hydrolysis cleavage. For this measurement we used the technique of PDMS, known to have a mass accuracy of 0.1% (Cotter, 1988;Loo et al, 1990). We found a mass of 1,185.1 Da, which is only 1.7 Da different from the calculated value of 1,183.4 Da, assuming that the peptide contains only three valine residues.…”

Section: Mass Analysesmentioning

confidence: 99%

See 1 more Smart Citation

Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore

Beeumen¹,

Devreese²,

Bun³

et al. 1993

Protein Science

108

View full text Add to dashboard Cite

The complete amino acid sequence of the 125-residue photoactive yellow protein (PYP) from Ectothiorhodospiru halophila has been determined to be MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKEVIGKNFFKDVAP CTDSPEFYGKFKEGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWVFVKRV.This is the first sequence to be reported for this class of proteins. There is no obvious sequence homology to any other protein, although the crystal structure, known at 2.4 A resolution (McRee, D.E., et al., 1989, Proc. Nutl. Acud. Sci. USA 86,6533-6537), indicates a relationship to the similarly sized fatty acid binding protein (FABP), a representative of a family of eukaryotic proteins that bind hydrophobic molecules. The amino acid sequence exhibits no greater similarity between PYP and FABP than for proteins chosen at random (8%).The photoactive yellow protein contains an unidentified chromophore that is bleached by light but recovers within a second. Here we demonstrate that the chromophore is bound covalently to Cys 69 instead of Lys 11 1 as deduced from the crystal structure analysis. The partially exposed side chains of Tyr 76, 94, and 118, plus Trp 119 appear to be arranged in a cluster and probably become more exposed due to a conformational change of the protein resulting from light-induced chromophore bleaching. The charged residues are not uniformly distributed on the protein surface but are arranged in positive and negative clusters on opposite sides of the protein.The exact chemical nature of the chromophore remains undetermined, but we here propose a possible structure based on precise mass analysis of a chromophore-binding peptide by electrospray ionization mass spectrometry and on the fact that the chromophore can be cleaved off the apoprotein upon reduction with a thiol reagent.The molecular mass of the chromophore, including an SH group, is 147.6 Da (k0.5 Da); the cysteine residue to which it is bound is at sequence position 69.

show abstract

Section: Proteinase K Digestsupporting

confidence: 61%

Section: Mass Analysesmentioning

confidence: 99%

Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore

Beeumen¹,

Devreese²,

Bun³

et al. 1993

Protein Science

108

View full text Add to dashboard Cite

show abstract

“…Simultaneously, the molecules are highly excited vibrationally and ionized [24,25]. UV-MALDI ionization is a laser desorption/ ionization assisted by a "matrix" that is a compound with an absorption band at the ionization laser frequency [26,27].…”

Section: Collisional Cooling Of Excited Analyte Molecular Ions In Uv-mentioning

confidence: 99%

A comparative study of the fragmentation of neutral lactooligosaccharides in negative-ion mode by UV-MALDI-TOF and UV-MALDI ion-trap/TOF mass spectrometry

Yamagaki

Suzuki

Tachibana

2006

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

Structure analyses of underivatized neutral lacto oligosaccharides are systematically performed by ultraviolet matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (UV-MALDI TOF MS) and UV-MALDI ion-trap time-of-flight mass spectrometry (ion-trap/TOF MS) acquired in negative-ion mode. Interestingly, their fragmentation significantly differ each other. In postsource decay (PSD) in UV-MALDI TOF MS, cross-ring cleavage at the reducing terminal predominates. On the other hand, glycosyl bond cleavage (C-type fragmentation) takes place preferentially in collision induced dissociation (CID) in UV-MALDI ion-trap/TOF MS. The cross-ring cleavage in PSD similar to that in in-source decay occurs via a prompt reaction path characteristic of the UV-MALDI process itself. The product ion spectra of UV-MALDI ion-trap/ TOF MS are similar to the electrospray ionization (ESI) ion-trap or quadrupole/TOF CID product ion spectra. During ion-trap/TOF MS experiments, the deprotonated molecular ions survive for several tens of milliseconds after CID event because the high internal energy chlorinated precursor ions are cooled by collisional cooling in the ion trap. The results obtained suggest that the PSD from the chlorinated precursor ion in UV-MALDI TOF MS might proceed as a two-step reaction; in the first, a high internal energy deprotonated molecular ion is generated as a reaction intermediate during the flight in the drift tube, and in the second, the rapid decomposition from the deprotonated molecular ion takes place. . In UV matrix-assisted laser desorption/ionization mass spectrometry (UV-MALDI MS) of neutral oligosaccharides, positively charged ions are detected as cation adduct ions rather than as protonated ions. Under common measurement conditions, employing a matrix of 2,5-dihydroxybenzoic acid (DHBA), a sodiated molecular ion [M ϩ Na] ϩ is preferentially observed in positive-ion UV-MALDI mass spectra of neutral oligosaccharides [3].Conventionally, UV-MALDI is combined with time-offlight mass spectrometry (TOF-MS); a structural analysis can be performed using postsource decay (PSD) ions produced by spontaneous decay during the time of flight of metastable ions generated by laser irradiation [4]. In the PSD of oligosaccharides, glycosyl bond cleavage ions (Yand B-type fragment; Domon and Costello nomenclature [5]) are generally observed from a sodiated precursor ion [M ϩ Na] ϩ in the positive-ion UV-MALDI PSD spectra[6]. Cross-ring cleavage ions are observed, however, and their relative abundance tends to be low [7,8]. In our previous study, these ions were generated from ␤1-4 linked N-acetyl glucosamine residue (GlcNAc) at the reducing terminal in Lewis X trisaccharide, but they were not generated from the terminal glucose (Glc) in 3-fucosyl lactose [9]. Positive-ion UV-MALDI TOF MS measurements yield information about molecular weights and sugar sequences. In electrospray ionization MS analysis of positively charged ion detection, Y-and B-type fragment ions are predominant in the low-energy colli...

show abstract

“…However, the highest m/z value reproducibly attainable in the commonest pyrolysis MS instruments is very small (typically Ͻm/z 200), moreover, due to the in vacuo thermal degradation step essentially all information on the structure or identity of the molecules producing the pyrolysate is lost. Later, the application of desorption techniques, such as plasma desorption [7] and fast atom bombardment (FAB) [8,9], allowed the analysis of involatile fractions and extended the measurable mass range. The advent of "soft" ionization techniques, such as matrix-assisted laser desorption ionization (MALDI), and electrospray ionization (ESI) has enabled the mass spectrometric analysis of both large molecular weight compounds, such as proteins and nucleic acids [10,11], and low molecular weight metabolites [12], giving the potential for rapid characterization of microorganisms with greater accuracy, selectivity, and sensitivity for better discrimination.…”

mentioning

confidence: 99%

Flow-injection electrospray ionization mass spectrometry of crude cell extracts for high-throughput bacterial identification

Vaidyanathan

Kell

Goodacre

2002

J. Am. Soc. Mass Spectrom.

101

View full text Add to dashboard Cite

Flow-injection electrospray ionization mass spectrometry (FI-ESI-MS) of unfractionated cellfree extracts obtained from bacterial cells suspended in a solvent mixture was investigated as a rapid analytical method for reproducible, high-throughput bacterial identification. Five bacterial strains (two Escherichia coli, two Bacillus spp. and one Brevibacillus laterosporus) were studied in this investigation. Axenically grown bacterial cells were suspended in an acidic organic solvent and the cell-free extract was sequentially injected into a solvent flow stream that was sprayed into the ionization chamber of the ESI-MS. The spectra produced contained reproducible information, which was useful for discriminating between the bacteria. Tandem mass spectrometry was used to characterize further the peaks, and at least three classes of macromolecules, namely phospholipids, glycolipids, and proteins, were found to contribute most to the spectral information. Bacterial extracts stored under different conditions gave very similar mass spectra for each of the five bacterial strains, indicating that the extracts were stable even at room temperature for up to 24 h, with no loss of information content, which has obvious implications for automated high-throughput analysis. An analysis of the components of the extracting solvent mixture and their effects on the spectral information showed that acetonitrile contributes most significantly to the extraction process and hence to the information content of the spectra. (J Am Soc Mass Spectrom 2002, 13, 118 -128)

show abstract

Plasma desorption mass spectrometry: coming of age

Abstract: Plasma desorption mass spectrometry (PDMS) uses the high-energy fragments emitted from the spontaneous fission of <)|2Cf to desorb and ionize large and nonvolatile molecules for mass analysis. The method is also known as fission fragment induced desorption (FFID). Much of the develop-

Cited by 67 publications

References 65 publications

Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore

Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore

A comparative study of the fragmentation of neutral lactooligosaccharides in negative-ion mode by UV-MALDI-TOF and UV-MALDI ion-trap/TOF mass spectrometry

Flow-injection electrospray ionization mass spectrometry of crude cell extracts for high-throughput bacterial identification

Contact Info

Product

Resources

About