Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I

H. Caroline Lee, Karla S. Booth, Winslow S. Caughey, Masao Ikeda-Saito

研究成果: Article査読

15 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)317-320
ページ数4
ジャーナルBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
1076
2
DOI
出版ステータスPublished - 1991 1 29

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学

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