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 Citations (Scopus)

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

Fingerprint

Heme
Peroxidase
Chlorides
Iron
Enzymes
Derivatives
Denaturation
Photolysis
Photodegradation
Fluorides
Laser beams
Raman scattering
Lasers
Ligands

Keywords

  • Myeloperoxidase
  • Raman spectrum

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase. / Ikeda-Saito, Masao; Argade, Pramod V.; Rousseau, Denis L.

In: FEBS Letters, Vol. 184, No. 1, 06.05.1985, p. 52-55.

Research output: Contribution to journalArticle

Ikeda-Saito, Masao ; Argade, Pramod V. ; Rousseau, Denis L. / Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase. In: FEBS Letters. 1985 ; Vol. 184, No. 1. pp. 52-55.
@article{ccf5581d671c4945856943c7272cc961,
title = "Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase",
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.",
keywords = "Myeloperoxidase, Raman spectrum",
author = "Masao Ikeda-Saito and Argade, {Pramod V.} and Rousseau, {Denis L.}",
year = "1985",
month = "5",
day = "6",
doi = "10.1016/0014-5793(85)80651-7",
language = "English (US)",
volume = "184",
pages = "52--55",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase

AU - Ikeda-Saito, Masao

AU - Argade, Pramod V.

AU - Rousseau, Denis L.

PY - 1985/5/6

Y1 - 1985/5/6

N2 - 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.

AB - 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.

KW - Myeloperoxidase

KW - Raman spectrum

UR - http://www.scopus.com/inward/record.url?scp=0021792132&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021792132&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(85)80651-7

DO - 10.1016/0014-5793(85)80651-7

M3 - Article

C2 - 2985447

AN - SCOPUS:0021792132

VL - 184

SP - 52

EP - 55

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -