Effects of solvent on the absorption maxima of five-coordinate heme complexes and carbon monoxide-heme complexes as models for the differential spectral properties of hemoglobins and myoglobins.
Absorption spectra were recorded for 5- and 6-coordinate model ferrous heme complexes of hindered and unhindered ligands in aqueous, and detergent solutions. Heme complexes exhibited differences in absorption maxima up to 6 nm which were correlated with the polarity of the heme environment. Increasing polarity of the solvent resulted in a general blue shift of absorption maxima of both deoxy- and (carbon monoxy)heme complexes. The differences in absorption maxima of heme complexes with different heme environments are offered as a possible explanation for some of the differences in absorption maxima among hemoproteins such as hemoglobin, myoglobin, and leghemoglobin.
D002248:Carbon Monoxide; D003902:Detergents; D006418:Heme; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009211:Myoglobin; D012997:Solvents; D013057:Spectrum Analysis
D003902:Detergents; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D009211:Myoglobin; D012997:Solvents; D006418:Heme; D002248:Carbon Monoxide