Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction

Terrence G. Frey, Leslie A. Kuhn, John S. Leigh, M. J. Costello, Samuel H P Chan

Research output: Contribution to journalArticle

9 Scopus citations


Electron microscopic images of selectively contrasted cytochrome oxidase dimer crystals are interpreted in a manner consistent with the structure of monomers determined by Fuller et al. (J. Molec. Biol. 134, 305-327). The arms of the y-shaped monomers lie within and perpendicular to the lipid bilayer protruding approximately 25 Å on the matrix side of the membrane. The cytoplasmic-side tails of two monomers spread apart in a dimer forming a large cleft. Decoration of the exposed matrix side of vesicle crystals with antisubunit IV antibody fragments indicates that subunit IV lies along the a-crystal axis roughly 20 Å from the center of the dimer. A membrane propensity algorithm applied to the sequences of cytochrome oxidase subunits predicts a total of 19 transmembrane α-helices per monomer.

Original languageEnglish (US)
Pages (from-to)155-162
Number of pages8
JournalJournal of Inorganic Biochemistry
Issue number3-4
StatePublished - 1985


ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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