Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase

Masao Ikeda-Saito, Pramod V. Argade, Denis L. Rousseau

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)


The resonance Raman spectra of ferric derivatives of myeloperoxidase at pH 8 show ligand-dependent differences. The data are consistent with the resting enzyme and the chloride and fluoride derivatives all having 6-coordinated high-spin configurations. At pH 4 we find that the resting enzyme is susceptible to photodegradation from our low power incident laser beam. Chloride binding inhibits this denaturation. Our data support direct binding of chloride to the enzyme under physiological conditions.

Original languageEnglish
Pages (from-to)52-55
Number of pages4
JournalFEBS Letters
Issue number1
Publication statusPublished - 1985 May 6


  • Myeloperoxidase
  • Raman spectrum

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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