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. 1992 Feb 15;282(Pt 1):255–259. doi: 10.1042/bj2820255

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

W J Ingledew 1, R A Rothery 1, R B Gennis 1, J C Salerno 1
PMCID: PMC1130916  PMID: 1311556

Abstract

The Escherichia 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 d are oriented with their haem planes perpendicular to the membrane plane. The high-spin haem b595 is oriented with its haem plane at approx. 55 degrees to the membrane plane. A minor low-spin component, attributable to a low-spin subpopulation of the haem d, is also oriented with its haem plane perpendicular to the membrane plane.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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