Evidence for zinc ion sharing in metallothionein dimers provided by collision-induced dissociation

Details Evidence for zinc ion sharing in metallothionein dimers provided by collision-induced dissociation Evidence for zinc ion sharing in metallothionein dimers provided by collision-induced dissociation

2011-03-21

arxiv.org/abs/1103.4030v1

International Journal of Mass Spectrometry 231 (2004) 207-211

Biology

Quantitative Biology

Biomolecules

Scientific paper

10.1016/j.ijms.2003.10.007

Nanospray and collisionally-induced dissociation are used to evaluate the presence and absence of interstrand co-chelation of zinc ions in dimers of metallothionein. As was reported in a previous publication from this laboratory, co-chelation stabilizes the dimer to collisional activation, and facilitates asymmetrical zinc ion transfers during fragmentation. In the case of metallothionein, dimers of the holoprotein are found to share zinc ions, while dimers of metallothionein, in which one domain has been denatured, do not. Zinc ions are silent to most physicochemical probes, e.g., NMR and Mossbauer spectroscopies, and the capability of mass spectrometry to provide information on zinc complexes has widespread potential application in biochemistry.

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