Assignment of the axial ligands of the haem in milk lactoperoxidase using magnetic circular dichroism spectroscopy.
The absorption and MCD spectra of ferric lactoperoxidase from milk and its cyanide and fluoride derivatives have been measured in the near infrared and visible wavelength regions both at room temperature and at 4.2 K. By comparison with the MCD spectra of haemoproteins of known axial ligation, which also contain protohaem IX, it has been possible to arrive at suggestions for the axial ligation in lactoperoxidase. At room temperature oxidized lactoperoxidase has the haem iron in the high-spin state, and the results indicate that the proximal ligand of the haem iron is a histidine imidazole and that the sixth ligand is probably a carboxylate ion. At 4.2 K oxidized lactoperoxidase converts almost totally to a low-spin form, changing the sixth ligand to a histidine imidazole, which is in the imidazolate form.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D005260:Female; D006418:Heme; D007784:Lactoperoxidase; D008024:Ligands; D008892:Milk / Q000201:enzymology*; D010544:Peroxidases; D013055:Spectrophotometry, Infrared
D008024:Ligands; D006418:Heme; D007784:Lactoperoxidase; D010544:Peroxidases