Proton magnetic resonance studies of peroxidases from turnip and horseradish.
Proton NMR spectra at 270 MHz have been measured for horseradish peroxidase and turnip peroxidase isoenzymes (P1, P2, P3 and P7) in both their high spin ferric native states and as the low spin ferric cyanide complexes. Resonances of amino acids near the heme have been identified and used to investigate variations in the structure of the heme crevice amongst the enzymes. Ligand proton resonances have been resolved in spectra of the cyanide complexes of the peroxidases and these provide information on the heme electronic structure. The electronic structure of the heme and the tertiary structure of the heme crevice are essentially the same in the acidic turnip isoenzymes, P1, P2 and, to a lesser extent, P3 but differ in the basic turnip enzyme, P7. The heme electronic structure and nature of the iron ligands in peroxidases are discussed. Further evidence is presented for histidine as the proximal ligand. A heme-linked ionizable group with a pK of 6.5 has been detected by NMR in the cyanide complex of horseradish peroxidase.
D001665:Binding Sites; D003201:Computers; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000032:analysis; D006735:Horseradish Peroxidase; D007527:Isoenzymes; D009682:Magnetic Resonance Spectroscopy; D010544:Peroxidases; D010944:Plants / Q000201:enzymology; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity
D007527:Isoenzymes; D006418:Heme; D006735:Horseradish Peroxidase; D010544:Peroxidases