Orientation of the haems of the ubiquinol oxidase:O2 reductase, cytochrome bo of Escherichia coli.
The orientation of the two haems of the Escherichia coli ubiquinol oxidase:O2 reductase, cytochrome bo, has been determined by electron paramagnetic resonance studies on oriented multilayer preparations of cytoplasmic membrane fragments. The enzyme contains a low-spin b-like haem and a high-spin b-like haem, designated cytochromes b and o respectively. Both haems are oriented with their planes perpendicular to the membrane plane, further extending the catalogue of structural and functional similarities between this enzyme and the mammalian cytochrome c oxidase, cytochrome aa3.
Salerno
J C
JC
Department of Biochemistry and Microbiology, University of St. Andrews, Scotland.
Ingledew
W J
WJ
D003198:Computer Simulation; D003573:Cytochrome b Group; D003580:Cytochromes / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006418:Heme / Q000032:analysis*; D011487:Protein Conformation
D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; D006418:Heme; C017168:cytochrome bo, E coli; C038862:cytochrome o oxidase; D003576:Electron Transport Complex IV