The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli
- PMID: 1311556
- PMCID: PMC1130916
- DOI: 10.1042/bj2820255
The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli
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.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources