Iron electronic structure in oxyhemoglobin and carboxypeptidase digested derivatives.
Mössbauer experiments were performed on the oxy- derivatives of human hemoglobin and its products of digestion with carboxypeptidases. The hemoglobins were chemically enriched to 95% in 57Fe, and were free from hemochrome impurities. Spectra were taken at low temperatures in the presence and absence of a 5.0 T magnetic field. It was observed that the enzymatic digestions which remove residues at least 16 A from the iron of the nearest heme appear to modify the electronic environment of the metal.
D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000378:metabolism; D043422:Carboxypeptidases A; D007501:Iron; D010108:Oxyhemoglobins; D013053:Spectrophotometry
D010108:Oxyhemoglobins; D007501:Iron; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D043424:Carboxypeptidase B