A circular dichroism study of the proton-linked transition in the carbomonoxy derivative of the hemoglobin component IV from trout.
Near ultraviolet and visible circular dichroism spectra of the carbomonoxy derivative of the hemoglobin component IV from trout Salmo irideus are pH-dependent in the range 6.2-7.8, and are affected by the presence of inositol hexaphosphate at pH 6.2. On the basis of previous studies, the spectral changes observed can be associated to the pH-dependent R4 leads to T4 transition occurring in the liganded protein. The CD spectra above 500 nm at low pH can be interpreted as due to release of the heme asymmetry in the T liganded conformation, in agreement with the movement of the iron toward the proximal histidine.
D000494:Allosteric Regulation; D000818:Animals; D002263:Carboxyhemoglobin; D002942:Circular Dichroism; D006454:Hemoglobins; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D011522:Protons; D014337:Trout / Q000097:blood
D006454:Hemoglobins; D011522:Protons; D002263:Carboxyhemoglobin