Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH

• Published in: Archives of biochemistry and biophysics Vol. 489; no. 1; pp. 68 - 75
• Main Authors: Droghetti, Enrica, Sumithran, Suganya, Sono, Masanori, Antalík, Marián, Fedurco, Milan, Dawson, John H., Smulevich, Giulietta
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2009
• Subjects: Acetic Acid - chemistry; Animals; Cattle; Electronic absorption spectroscopy; Heme - chemistry; Horses; Hydrogen-Ion Concentration; Iron - chemistry; Magnetic circular dichroism spectroscopy; Molecular Structure; Myoglobin; Myoglobin - chemistry; Protein Denaturation; Resonance Raman spectroscopy; Unfolding process; Urea; Urea - chemistry; Myoglobin; Urea; Unfolding process; Electronic absorption spectroscopy; Magnetic circular dichroism spectroscopy; Resonance Raman spectroscopy
• ISSN: 0003-9861; 1096-0384
• DOI: 10.1016/j.abb.2009.07.008

The heme iron coordination of ferric myoglobin (Mb) in the presence of 9.0 M urea and 8.0 M acetic acid at acidic pH values has been probed by electronic absorption, magnetic circular dichroism and resonance Raman spectroscopic techniques. Unlike Mb at pH 2.0, where heme is not released from the protein despite the acid denaturation and the loss of the axial ligand, upon increasing the concentration of either urea or acetic acid, a spin state change is observed, and a novel, non-native six-coordinated high-spin species prevails, where heme is released from the protein.