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Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase
Author(s) -
Ikeda-Saito Masao,
Argade Pramod V.,
Rousseau Denis L.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80651-7
Subject(s) - chemistry , ferric , heme , chloride , raman spectroscopy , resonance raman spectroscopy , myeloperoxidase , resonance (particle physics) , fluoride , hemeprotein , ligand (biochemistry) , photochemistry , enzyme , inorganic chemistry , biochemistry , organic chemistry , receptor , physics , particle physics , optics , inflammation , medicine
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.