Myoglobin thermodynamic parameters

Jmol-1K-1) in the reverse direction. Free energy, entropy as well as volume profiles were presented. The thermodynamic parameters were similar to those found for binding of CO to myoglobin. 

A variety of physical methods has been used to ascertain whether or not surface ruthenation alters the structure of a protein. UV/vis, CD, EPR, and resonance Raman spectroscopies have demonstrated that myoglobin (30, 89), cytochrome c (74, 164, 193, 194), and azurin (113) are not perturbed structurally by the attachment of a ruthenium complex to a surface histidine. The reduction potential of the metal redox center of a protein and its temperature dependence are indicators of protein structure as well. Cyclic voltammetry (113, 193), differential pulse polarography (30, 31, 140), and spectroelectrochemistry (30, 31,194) are commonly used for the determination of the ruthenium and protein redox center potentials in modified proteins. The reduction potential and thermodynamic parameters... 

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