The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli.
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.
Ingledew
W J
WJ
Department of Biochemistry and Microbiology, University of St. Andrews, Fife, Scotland, U.K.
Rothery
R A
RA
Gennis
R B
RB
Salerno
J C
JC
D001665:Binding Sites; D002462:Cell Membrane / Q000201:enzymology; D003573:Cytochrome b Group; D003580:Cytochromes / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D045222:Electron Transport Chain Complex Proteins; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006418:Heme / Q000032:analysis*; D010088:Oxidoreductases / Q000737:chemistry*; D011487:Protein Conformation
D003573:Cytochrome b Group; D003580:Cytochromes; D045222:Electron Transport Chain Complex Proteins; D029968:Escherichia coli Proteins; D006418:Heme; D010088:Oxidoreductases; C040077:cytochrome bd terminal oxidase complex, E coli