Matrix influence on stability constants of 15-crown-5-alkali metal complexes measured by liquid secondary ion mass spectrometry

1994 ◽  
Vol 29 (4) ◽  
pp. 169-175 ◽  
Author(s):  
Denis Giraud ◽  
Olivier Laprévote ◽  
Bhupesh C. Das
Keyword(s):  
Mass Spectrometry ◽  
Alkali Metal ◽  
Metal Complexes ◽  
Stability Constants ◽  
Secondary Ion Mass Spectrometry ◽  
Ion Mass Spectrometry ◽  
Alkali Metal Complexes ◽  
Secondary Ion ◽  
Matrix Influence

High Mass Resolution Plasma Desorption and Secondary Ion Mass Spectrometry of Neutral Nickel Thiolate Complexes. Crystal Structure of [Ni6(SC3H7)12]

1992 ◽  
Vol 47 (7) ◽  
pp. 929-936 ◽  
Author(s):  
Herbert Feld ◽  
Angelika Leute ◽  
Derk Rading ◽  
Alfred Benninghoven ◽  
G. Henkel ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Metal Complexes ◽  
Secondary Ion Mass Spectrometry ◽  
Molecular Ions ◽  
Cluster Ions ◽  
High Mass ◽  
Plasma Desorption ◽  
Ion Mass Spectrometry ◽  
Thiolate Complexes ◽  
Secondary Ion

The use of mass spectrometry for the analysis of transition metal complexes is demonstrated by combined high resolution Plasma Desorption Mass Spectrometry (PDMS) and Secondary Ion Mass Spectrometry (SIMS) investigations of the neutral nickel thiolate complexes [Ni4(SC3H7)8] (1), [Ni4(SC6H11)8] (2), [Ni8(SCH2COOEt)16] (3) and [Ni6(SC3H7)12] (4). The positive spectra are dominated by three kinds of SI-species: (a) molecular ions, (b) fragment ions and (c) molecular ions with one or more substrate atoms attached. The negative spectra show mainly nickel sulfur cluster ions of the composition (NixSy)-. In contrast to many Fast Atom Bombardment (FAB) spectra of neutral metal complexes, SIMS and PDMS spectra provide molecular weight as well as fragment ion information. Both techniques are most powerful tools for the investigation of coordination compounds because the samples are easy to prepare and the spectra are independent of matrix conditions. Additionally crystallographic studies have been carried out for 4. The hexanuclear complex 4 with square planar Ni-S coordination sites crystallizes in the trigonal space group R 3̅ with Z = 3 and α = 18.537(5), c = 13.966(3) Å.

Applications of Time-OF-Flight Secondary Ion Mass Spectrometry (TOF-SIMS)

1990 ◽  
Vol 48 (2) ◽  
pp. 308-309
Author(s):  
Bruno Schueler ◽  
Robert W. Odom
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Structural Information ◽  
Time Of Flight ◽  
Biological Tissues ◽  
Polymer Surfaces ◽  
Tof Sims ◽  
Secondary Ions ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Time-of-flight secondary ion mass spectrometry (TOF-SIMS) provides unique capabilities for elemental and molecular compositional analysis of a wide variety of surfaces. This relatively new technique is finding increasing applications in analyses concerned with determining the chemical composition of various polymer surfaces, identifying the composition of organic and inorganic residues on surfaces and the localization of molecular or structurally significant secondary ions signals from biological tissues. TOF-SIMS analyses are typically performed under low primary ion dose (static SIMS) conditions and hence the secondary ions formed often contain significant structural information.This paper will present an overview of current TOF-SIMS instrumentation with particular emphasis on the stigmatic imaging ion microscope developed in the authors’ laboratory. This discussion will be followed by a presentation of several useful applications of the technique for the characterization of polymer surfaces and biological tissues specimens. Particular attention in these applications will focus on how the analytical problem impacts the performance requirements of the mass spectrometer and vice-versa.

Optics-Free Visualization of Proteins in Single Cells by Time of Flight-Secondary Ion Mass Spectrometry Coupled with Genetically Encoded Chemical Tags

2020 ◽  
Author(s):  
Feifei Jia ◽  
Jie Wang ◽  
Yanyan Zhang ◽  
Qun Luo ◽  
Luyu Qi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Single Cells ◽  
Time Of Flight ◽  
E Coli ◽  
Tof Sims ◽  
Ion Mass Spectrometry ◽  
Chemical Tags ◽  
Secondary Ion

<p></p><p><i>In situ</i> visualization of proteins of interest at single cell level is attractive in cell biology, molecular biology and biomedicine, which usually involves photon, electron or X-ray based imaging methods. Herein, we report an optics-free strategy that images a specific protein in single cells by time of flight-secondary ion mass spectrometry (ToF-SIMS) following genetic incorporation of fluorine-containing unnatural amino acids as a chemical tag into the protein via genetic code expansion technique. The method was developed and validated by imaging GFP in E. coli and human HeLa cancer cells, and then utilized to visualize the distribution of chemotaxis protein CheA in E. coli cells and the interaction between high mobility group box 1 protein and cisplatin damaged DNA in HeLa cells. The present work highlights the power of ToF-SIMS imaging combined with genetically encoded chemical tags for <i>in situ </i>visualization of proteins of interest as well as the interactions between proteins and drugs or drug damaged DNA in single cells.</p><p></p>

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