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 journalArticle

44 Scopus citations

Abstract

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 (US)
Pages (from-to)52-55
Number of pages4
JournalFEBS Letters
Volume184
Issue number1
DOIs
StatePublished - May 6 1985
Externally publishedYes

Keywords

  • Myeloperoxidase
  • Raman spectrum

ASJC Scopus subject areas

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

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