• chromium(III);
  • CID;
  • peptide;
  • metallopeptide;
  • chromodulin;
  • FT-ICR;
  • ESI


The complexes formed between chromium(III) and synthetic acidic peptides were studied by sustained off-resonance irradiation collision-induced dissociation (SORI-CID) in a Fourier transform ion-cyclotron resonance (FT-ICR) mass spectrometer equipped with electrospray ionization (ESI). Neutral peptides and peptides containing one, two, and multiple acidic residues were studied. Formation of [M + Cr − 2H]+ occurred for all peptides. Three noteworthy features were found in the CID spectra of [M + Cr − 2H]+. The first is that fewer fragment ions were produced from [M + Cr − 2H]+ than from [M + H]+. The reason may be that multiple coordination between chromium(III) and carboxylate or carbonyl groups hinders the production of fragment ions by continuing to bind pieces of the peptide to chromium(III) after cleavage of bonds within the peptide. The second feature is loss of CO from [M + Cr − 2H]+ and [yn + Cr − H]+. A mechanism involving coordination of chromium(III) with carboxylate groups is proposed to rationalize elimination of CO. The third feature is that chromium(III) is retained in all fragment ions, indicating strong binding of the metal ion to the peptides. The complex [M + 2Cr − 5H]+ is formed as the peptide chain length and number of acidic residues increases. Longer peptides have more sites to coordinate with chromium(III) and more conformational flexibility. In addition, formation of [M + Cr − 2H]+ from AGGAAAA-OCH3, which has no carboxylic acid groups, suggests that chromium(III) can coordinate with sites on the peptide backbone, albeit in low abundance. In the negative mode, [M + Cr − 4H] was only found for peptides containing four or more carboxylic acid groups. This is consistent with deprotonated carboxylic acid groups being involved in chromium(III) coordination and with chromium existing in the 3 + state in the gas-phase ions. Copyright © 2008 John Wiley & Sons, Ltd.