Ligand orientation of oxyproto- and oxymesocobalt porphyrin-substituted myoglobin by single crystal EPR spectroscopy.

H. Hori, M. Ikeda-Saito, T. Yonetani

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

Single crystals of oxyproto- and oxymesocobalt myoglobin have been examined by electron paramagnetic resonance spectroscopy at ambient and cryogenic temperatures in order to determine the principal values and eigenvectors of g tensors and the hyperfine coupling tensors. The Co--O--O bond angle was determined to be 125 degrees +/- 5 degrees for oxyprotocobalt myoglobin, and 153 degrees +/- 5 degrees for oxymesocobalt myoglobin at ambient temperature. This result suggests that differences in stereochemical interactions of the modified 2,4-side chains of porphyrin with protein contribute to the ligand orientations as well as the altered ligand-binding behavior in these hemoproteins. Upon freezing, two unequivalent orientations of the O--O axis (species I and II) were found in both oxycobalt myoglobin single crystals. Shifts of the resonance spectra of these species were observed below the freezing point of the crystals. The signal intensities of two paramagnetic species in oxyprotocobalt myoglobin were approximately equivalent (I congruent to II), whereas those in oxymesocobalt myoglobin were quite different (I greater than II) at 77 K. The present electron paramagnetic resonance studies demonstrate that changes in the bonding structure of Co--O2 are induced upon freezing the biological macromolecule, including the movement of the residues of the heme environment.

Original languageEnglish
Pages (from-to)3636-3642
Number of pages7
JournalJournal of Biological Chemistry
Volume257
Issue number7
Publication statusPublished - 1982 Apr 10

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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