Proton magnetic resonance of the bovine spleen green heme-protein

Masao Ikeda-Saito, Toshiro Inubushi

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

The ferric spleen green heme-protein exhibits hyperfine-shifted proton resonances between 90 and 20 ppm for the high-spin resting form and the chloride complex, and between 46 and -9.4 ppm for the low-spin nitrite complex. The proton NMR spectral profile of the enzyme is similar to that of lactoperoxidase, but different from those of common heme-proteins. The appearance of a resonance at 76 ppm in the ferrous enzyme shows the presence of a proximal histidine residue linked to the iron. The proton relaxation rates of bulk water indicate that chloride binds to the sixth position of the iron in the chloride complex of the enzyme.

Original languageEnglish
Pages (from-to)111-116
Number of pages6
JournalFEBS Letters
Volume214
Issue number1
DOIs
Publication statusPublished - 1987 Apr 6

Keywords

  • (Bovine spleen)
  • Heme-protein
  • Myeloperoxidase
  • NMR

ASJC Scopus subject areas

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

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