Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1174405 | Analytical Biochemistry | 2012 | 4 Pages |
Abstract
Investigation of the heme iron dynamics in cytochrome c with Mössbauer spectroscopy and especially nuclear resonance vibrational spectroscopy requires the replacement of the natural abundant heme iron with the 57Fe isotope. For demetallization, we use a safer and milder ferrous sulfate-hydrochloric acid method in addition to the harsher commonly used hydrofluoric acid-based procedure. The structural integrity of the 57Fe-reconstituted protein in both oxidation states is confirmed from absorption spectra and a detailed analysis of the rich resonance Raman spectra. These results reinforce the application of metal-substituted heme c proteins as reliable models for the native proteins.
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Authors
Bogdan M. Leu, Tom H. Ching, Cuong Tran, J. Timothy Sage,