The Transmembrane Helices of Beef Heart Cytochrome Oxidase

M. Lundeen, B. Chance, L. Powers

Research output: Contribution to journalLetter

7 Scopus citations

Abstract

The locations of the transmembrane helices in the 12 subunits of beef heart cytochrome oxidase were predicted with a modified form of the von Heijne-Blomberg hydrophobicity scale. Based on ∼20 residues per transmembrane helix, about 480 of the estimated 660 helical residues (36.8% of 1,793 total residues) are expected to be in transmembrane helices that have their axes tilted by a small angle α from the normal to the plane of the membrane. This angle is calculated to be ∼30°, based on the observed overall tilt angle θ of 39° obtained from circular dichroism (CD) measurements on multilamellar films, or about 25°, based on the observed tilt angle θ of 36° obtained from the infrared linear dichroism of films. For 21 residues per transmembrane helix, the calculated values of α become 32° and 28°, respectively, depending upon the value of θ used. Thus, a transmembrane helical tilt angle of ∼30° accounts for the predicted transmembrane stretches in cytochrome oxidase if 20–21 residues are sufficient to span the membrane. Additional helical residues in the lipid head region may deviate by a larger angle from the normal to the plane of the membrane in cytochrome oxidase.

Original languageEnglish (US)
Pages (from-to)693-695
Number of pages3
JournalBiophysical Journal
Volume51
Issue number4
DOIs
StatePublished - Jan 1 1987
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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