Inert Site in a Protein Zinc Cluster: Isotope Exchange by High Resolution Mass Spectrometry

Using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry, we show that one Zn2+ ion in the Zn4 cluster of cyanobacterial metallothionein is inert to exchange with 67Zn2+. We suggest that this is zinc in site A, which together with the surrounding α and β secondary st...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2003-03, Vol.125 (11), p.3226-3227
Main Authors: Blindauer, Claudia A, Polfer, Nick C, Keiper, Stella E, Harrison, Mark D, Robinson, Nigel J, Langridge-Smith, Pat R. R, Sadler, Peter J
Format: Article
Language:English
Subjects:
Analytical chemistry
Chemistry
Cyclotrons
Exact sciences and technology
Fourier Analysis
Mass Spectrometry - methods
Models, Molecular
Spectrometric and optical methods
Zinc - chemistry
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Summary:Using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry, we show that one Zn2+ ion in the Zn4 cluster of cyanobacterial metallothionein is inert to exchange with 67Zn2+. We suggest that this is zinc in site A, which together with the surrounding α and β secondary structure forms a zinc-finger fold.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0284409