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- W2052154783 abstract "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| 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|. 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." @default.
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- W2052154783 date "1980-03-01" @default.
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- W2052154783 title "The interaction of myeloperoxidase with ligands as studied by EPR" @default.
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- W2052154783 doi "https://doi.org/10.1016/0005-2744(80)90291-0" @default.
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