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

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

doi:10.1016/0014-5793(85)80651-7

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 journal › Article › peer-review

49 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 language	English (US)
Pages (from-to)	52-55
Number of pages	4
Journal	FEBS Letters
Volume	184
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(85)80651-7
State	Published - May 6 1985
Externally published	Yes

Keywords

Myeloperoxidase
Raman spectrum

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(85)80651-7

Cite this

@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.}",

note = "Funding Information: We thank the Penn-Jersey Regional Red Cross Blood Services,P hiladelphia for their supply of the out-dated granulocyte concentrates,D r T. Yonetani for his support,a nd Dr D. Safer for electrophoresis.M .I.-S. wishest o thank Dr K.-G. Paul of the University of Umea, Umea, Swedenf or his kind support at the initial stageo f this investigation. We thank Dr Y. Ozaki for sendingu s his un-publishedr esults.T he portion of this work carried out at the University of Pennsylvaniaw as supported by researchg rant AI-20463 from the National Institute for Allergy and Infectious Diseases.",

year = "1985",

month = may,

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.

N1 - Funding Information: We thank the Penn-Jersey Regional Red Cross Blood Services,P hiladelphia for their supply of the out-dated granulocyte concentrates,D r T. Yonetani for his support,a nd Dr D. Safer for electrophoresis.M .I.-S. wishest o thank Dr K.-G. Paul of the University of Umea, Umea, Swedenf or his kind support at the initial stageo f this investigation. We thank Dr Y. Ozaki for sendingu s his un-publishedr esults.T he portion of this work carried out at the University of Pennsylvaniaw as supported by researchg rant AI-20463 from the National Institute for Allergy and Infectious Diseases.

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

SN - 0014-5793

VL - 184

SP - 52

EP - 55

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this