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| Content Provider | Springer Nature Link |
|---|---|
| Author | Will, Joanna Kyas, Andreas Sheldrick, William S. Wolters, Dirk |
| Copyright Year | 2007 |
| Abstract | An automated multidimensional protein identification technology, which combines biphasic liquid chromatography with electrospray ionisation tandem mass spectrometry (MS/MS), was employed to analyse tryptic peptides from Escherichia coli cells treated with the antiproliferation agent [(η6-p-cymene)RuCl2(DMSO)], where DMSO is dimethyl sulfoxide. MS/MS spectra were recorded for molecular ions generated by neutral loss of p-cymene from intensive peptide ions coordinated by the (η6-p-cymene)RuII fragment. Matching of the MS/MS spectra of the ruthenated peptides to spectra of proteins in the E. coli database enabled the identification of five protein targets for [(η6-p-cymene)RuCl2(DMSO)]. One of these is the constitutive cold-shock protein cspC, which regulates the expression of genes encoding stress-response proteins, and three of the other targets, ppiD, osmY and sucC, are proteins of the latter type. The DNA damage-inducible helicase dinG was likewise established as a protein target. Aspartate carboxylate functions were identified as the probable Ru binding sites in cspC, ppiD and dinG, and threonine and lysine side chains in osmY and sucC, respectively. |
| Starting Page | 883 |
| Ending Page | 894 |
| Page Count | 12 |
| File Format | |
| ISSN | 09498257 |
| Journal | JBIC Journal of Biological Inorganic Chemistry |
| Volume Number | 12 |
| Issue Number | 6 |
| e-ISSN | 14321327 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2007-05-22 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Arene complexes Ruthenium(II) Protein targets Tandem mass spectrometry Escherichia coli Microbiology Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
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