Studying metal integration in native and recombinant copper proteins by hyphenated ICP-DRC-MS and ESI-TOF-MS capabilities and limitations of the complementary techniques

Obinger, Christian; Stingeder, Gerhard; Paumann, Martina; Furtmüller, Paul G.; Koellensperger, Gunda

doi:10.1039/b604974p

Cited by 36 publications

(26 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4). We nevertheless recommend always combining ESI-MS with a suitable atomic spectroscopy; if ICP-OES or state-of-theart ICP-MS (including reaction/collision cell technology) [108] are used, measurement of sulfur concentration can conveniently be used for absolute protein quantification, if some precautions are taken into consideration [109].…”

Section: Immobilised Metal-affinity Chromatographymentioning

confidence: 99%

Protein fractionation and detection for metalloproteomics: challenges and approaches

2012

View full text Add to dashboard Cite

At least one third of all proteins are thought to require a metal ion co-factor for their function. Recognition of the importance of metals in biological systems and major advances in analytical instrumentation and technology have led to the emergence of the new research area of metalloproteomics in recent years. Despite this progress, the experimental determination of in-vivo metal cofactors has remained challenging, because this requires elucidation of protein interactions with non-covalently bound metal ions. This critical review highlights current methodological approaches, focusing, in particular, on issues relating to the fractionation and separation of the metalloproteome, including recent experience with metalloproteomics for marine cyanobacteria in our laboratory. Metalloproteomics promises to deliver novel insights into fundamental biological processes in the future, but it is clear that further methodological advances are necessary to exploit the full potential of this emerging research area.

show abstract

Section: Immobilised Metal-affinity Chromatographymentioning

confidence: 99%

Protein fractionation and detection for metalloproteomics: challenges and approaches

2012

View full text Add to dashboard Cite

show abstract

“…LC-ESI-MS and LC-ICP-MS were complementarily used for the characterization of bacterial copper proteins. ESI-TOF-MS confirmed both the stoichiometry of ligation and the oxidation state of the metal center in plastocyanin and the CuA domain of cytochrome c oxidase from the cyanobacterium Synechocystis (Hann et al 2006).…”

Section: Electrospray Ionization Mass Spectrometry (Esi-ms)supporting

confidence: 64%

A Glossary of Microanalytical Tools to Assess the Metallome

Wesenberg

Bleuel

Krauss

Molecular Microbiology of Heavy Metals

View full text Add to dashboard Cite

“…Anion exchange is by far the most popular [36,39,[53][54][55][56]58,59]. It was successfully combined with SEC for the bidimensional fractionation of complex samples [54][55][56], the study of interactions of a metal-based anticancer drug with plasma proteins [75] or even more extensive fractionation schemes [53].…”

Section: Ion Exchangementioning

confidence: 99%

Separative techniques for metalloproteomics require balance between separation and perturbation

Hagège¹,

Huynh²,

Hébrant³

2015

TrAC Trends in Analytical Chemistry

View full text Add to dashboard Cite

Studying metal integration in native and recombinant copper proteins by hyphenated ICP-DRC-MS and ESI-TOF-MS capabilities and limitations of the complementary techniques

Cited by 36 publications

References 45 publications

Protein fractionation and detection for metalloproteomics: challenges and approaches

Protein fractionation and detection for metalloproteomics: challenges and approaches

A Glossary of Microanalytical Tools to Assess the Metallome

Separative techniques for metalloproteomics require balance between separation and perturbation

Contact Info

Product

Resources

About