Article ID Journal Published Year Pages File Type
1926284 Archives of Biochemistry and Biophysics 2009 8 Pages PDF
Abstract

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.

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