EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide. Halide-dependent spectral changes are found at acidic pH. The electronic structure of the low-spin ferric iron in cyanide complex appears to be modulated by halide binding to a protonated amino acid in the distal heme cavity. These findings suggest halide substrates can interact with ferryl oxygen in compound I during enzyme catalysis to form hypohalous acid.
|ジャーナル||Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular|
|出版ステータス||Published - 1991 1 29|
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