Stability of a highly charged noncovalent complex in the gas phase: holomyoglobin.
Gas phase holomyoglobin (hMb) ions in charge states +7 to +21 were formed by electrospray ionization in combination with a continuous-flow mixing apparatus. Collision cross section measurements show that the highly charged ions are somewhat unfolded in comparison to low charge states but still retain a considerable degree of folding. A new collision model is presented which calculates the relative energies transferred to complexes in tandem mass spectrometry. Tandem mass spectrometry and ion trapping experiments both show that the energies required to dissociate heme from the highly charged heme-protein complexes in the gas phase are similar to those of low charge states, previously shown in literature ion cyclotron resonance experiments to be 0.7-1.0 eV. These energies are comparable to those of the heme binding energy in solution. The results suggest that even for the highly charged hMb ions which have unfolded somewhat, the heme-protein interactions remain relatively unperturbed.
Department of Chemistry, University of British Columbia, Vancouver, Canada.
Y L
YL
Chen
J M
JM
Campbell
B A
BA
Collings
L
L
Konermann
D J
DJ
Douglas
D000818:Animals; D004735:Energy Transfer; D006418:Heme / Q000737:chemistry; D006736:Horses; D013058:Mass Spectrometry; D009211:Myoglobin / Q000737:chemistry*; D011485:Protein Binding; D012996:Solutions
D009211:Myoglobin; D012996:Solutions; D006418:Heme