Metal electronic effects on myoglobin conformational stability.
The first quantitative measurements of the effect of metal substitution on (myo)globin conformational stability are reported. Metallomyoglobins examined include Fe(III), Cr(III), Rh(III), Mn(III), Fe(II), Zn(II), Cu(II), and Ru(II). It is shown that the protein denaturant interaction is not altered, in general, by metal substitution. Therefore reversible denaturation provides a means to assess the dependence of myoglobin conformational energy on metal electronic state. A simple relationship was found between the conformational free energy of trivalent metal derivatives (delta delta G0u) and the metal imidazole bond strength (delta Gim) of that derivative. Clear differences are observed between the divalent and trivalent metal derivatives, independent of delta Gim.
D000818:Animals; D002857:Chromium; D003300:Copper; D006146:Guanidines; D007501:Iron; D008345:Manganese; D008670:Metals; D009211:Myoglobin; D011485:Protein Binding; D011487:Protein Conformation; D012238:Rhodium; D012428:Ruthenium; D014907:Whales; D015032:Zinc
D006146:Guanidines; D008670:Metals; D009211:Myoglobin; D002857:Chromium; D008345:Manganese; D003300:Copper; D012428:Ruthenium; D012238:Rhodium; D007501:Iron; D015032:Zinc