Freezing induced change in ligand orientation in oxycobalt-myoglobin

Hiroshi Hori, Mássao Ikeda-saito, Takashi Yonetani

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

Abstract

Single crystals of oxycobalt-myoglobin were examined by electron paramagnetic resonance (EPR) spectroscopy at ambient and cryogenic temperatures. The principal values and eigenvectors of the g-tensor and the hyperfine coupling tensor were determined. The Co - O - O bond angle was estimated to be 125° at ambient temperature. The single crystal EPR data of oxycobalt myoglobin at 77 K showed two sets of the principal values for g and hyperfine coupling tensors and eigenvectors, indicating that the bound oxygen molecule takes two distinct orientations. The result has demonstrated for the first time that the well defined change in the molecular orientation is induced upon freezing the biological macromolecule.

Original languageEnglish
Pages (from-to)501-502
Number of pages2
JournalNature
Volume288
Issue number5790
DOIs
Publication statusPublished - 1980

ASJC Scopus subject areas

  • General

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