The interaction of myeloperoxidase with ligands as studied by EPR.
1. The reaction of myeloperoxidase with fluoride, chloride and azide has been studied by EPR. 2. Fluoride decreases the rhombicity of the high-spin heme signal of myeloperoxidase and the nuclear spin of the fluoride atom induces a splitting in g parallel of 35 G. This observation demonstrates that fluoride binds as an axial ligand to the heme iron of the enzyme. 3. Addition of chloride to the fluoride-treated enzyme increases the rhombicity of the high-spin heme signal and brings about a disappearance of the splitting at g parallel. The addition of azide to the fluoride-treated enzyme changes the spin state of the heme iron from a high-to a low-spin state (gx = 2.68, gy = 2.22 and gz = 1.80). 4. Upon addition of chloride or fluoride to low-spin azido-myeloperoxidase this compound is converted into the high-spin chlorido- or fluorido-myeloperoxidase. These observations demonstrate that these ligands compete for a binding site at or close to the heme iron of myeloperoxidase.
D001386:Azides / Q000378:metabolism*; D002712:Chlorides / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D005459:Fluorides / Q000378:metabolism*; D006801:Humans; D007962:Leukocytes / Q000201:enzymology; D009195:Peroxidase / Q000097:blood*; D010544:Peroxidases / Q000097:blood*
D001386:Azides; D002712:Chlorides; D010544:Peroxidases; D009195:Peroxidase; D005459:Fluorides