1. Spectroscopic characterization of (57)Fe-enriched cytochrome c.
- Author
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Leu BM, Ching TH, Tran C, and Sage JT
- Subjects
- Cytochromes c metabolism, Ferrous Compounds chemistry, Heme chemistry, Hydrochloric Acid chemistry, Iron Isotopes chemistry, Models, Molecular, Oxidation-Reduction, Spectrum Analysis, Raman, Vibration, Cytochromes c chemistry, Spectroscopy, Mossbauer
- 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 (57)Fe 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 (57)Fe-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., (Published by Elsevier Inc.)
- Published
- 2012
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