PMID:1311556
| Citation |
Ingledew, WJ, Rothery, RA, Gennis, RB and Salerno, JC (1992) The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli. Biochem. J. 282 ( Pt 1):255-9 |
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| 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. |
| Links | |
| Keywords |
Binding Sites; Cell Membrane/enzymology; Cytochromes/chemistry; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli/enzymology; Escherichia coli Proteins; Heme/analysis; Oxidoreductases/chemistry; Protein Conformation |
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