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

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)317-320
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1076
Issue number2
DOIs
Publication statusPublished - 1991 Jan 29

Keywords

  • Cyanide complex
  • EPR
  • Enzyme catalysis
  • Halide
  • Myeloperoxidase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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