The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli

W. J. Ingledew, R. A. Rothery, R. B. Gennis, J. C. Salerno

Research output: Contribution to journalArticle

Abstract

The Esherichia coli cytochrome bd complex incorporates three haems as prosthetic groups. In the ferric form these are a predominantly high-spin chlorin (haem d), a high-spin haem b (b595) and a low-spin haem b (b558). The orientations of these three haems have been determined by e.p.r. studies on oriented multilayer preparations of cytoplasmic membrane fragments. The low-spin haem b (b558) and the high-spin haem dare oriented with their haem planes perpendicular to the membrane plane. The high-spin haem b595 is oriented with its haem plane at approx. 55% to the membrane plane. A minor low-spill component, attributable to a low-spin subpopulation of the haem d, is also oriented with its haem plane perpendicular to the membrane plane.

Original languageEnglish (US)
Pages (from-to)255-259
Number of pages5
JournalBiochemical Journal
Volume282
Issue number1
DOIs
StatePublished - 1992

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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