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Resonance Raman characterization of the heme prosthetic group in eosinophil peroxidase

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
189
Issue
2
Identifiers
DOI: 10.1016/0014-5793(85)81038-3
Keywords
  • Chlorin
  • Eosinophil
  • Enzme Mechanism
  • Peroxidase
  • Protoheme
  • Roman Spectroscopy
Disciplines
  • Biology

Abstract

Abstract The resonance-enhanced Raman spectrum of eosinophil peroxidase (EPO) from horse and human eosinophils is reported. Based upon the spectral energies, distribution and depolarization ratios of the high-frequency skeletal modes and upon the presence of weak bands assignable to vinyl substituent groups, we conclude that the heme prosthetic group is high-spin, 6 coordinate protoporphyrin. The Raman spectrum reveals clear differences from lactoperoxidase (LPO), an enzyme which appears nearly structurally isomorphous by other physical techniques; the data indicate a stronger axial 6th ligand in EPO. Mechanistic implications are discussed in relation to LPO and myeloperoxidase, an enzyme present in neutrophils and monocytes which contains a unique functional active-site chlorin.

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