ArticleMawatari K, Matsukawa S, Yoneyama Y.
Biochim Biophys Acta. 1983 Jun 29;745(3):219-28.
Absorption and circular dichroism (CD) spectra of the Soret band, assigned as a pi-pi transition of the porphyrin pi-electron system, showed a great difference between alpha and beta subunits in the ferric state (alpha +, beta +). The nonequivalence of the spectra between alpha + and beta + subunits partly originates from the difference in the strength of the bond between heme iron and the proximal histidine. The peak positions for absorption and CD spectra of the ferric derivatives associated with F-, H2O, N-3 and CN- of the isolated subunits qualitatively correlate with the spin state of the ferric heme. The Soret absorption spectra obtained by simple addition of those for alpha + and beta + subunits are very similar to those for methemoglobin A (metHb A). On the other hand, the arithmetic means for the Soret CD spectra of alpha + and beta + subunits are different from those for metHb A. These differences were not observed between the Soret CD spectra of alpha 1 beta 1 dimer, which is predominantly present in metHb Hirose (beta 37Trp-Ser), and those of tetrameric metHb A. Therefore, the interaction between alpha 1 and beta 1 subunits to make the alpha 1 beta 1 dimer may strongly affect the CD spectral properties of alpha + and beta + subunits. The effect of the interaction between two homogeneous dimers, alpha 1 beta 1 and alpha 2 beta 2, forming a tetramer, on the Soret CD spectral properties, if any, is very small compared with that between alpha 1 and beta 1 subunits.