Literature DB >> 1646721

Orientation of the haems of the ubiquinol oxidase:O2 reductase, cytochrome bo of Escherichia coli.

J C Salerno1, W J Ingledew.   

Abstract

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.

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Year:  1991        PMID: 1646721     DOI: 10.1111/j.1432-1033.1991.tb16082.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

1.  Angular dependences of perpendicular and parallel mode electron paramagnetic resonance of oxidized beef heart cytochrome c oxidase.

Authors:  D J Hunter; V S Oganesyan; J C Salerno; C S Butler; W J Ingledew; A J Thomson
Journal:  Biophys J       Date:  2000-01       Impact factor: 4.033

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

Authors:  W J Ingledew; R A Rothery; R B Gennis; J C Salerno
Journal:  Biochem J       Date:  1992-02-15       Impact factor: 3.857

  2 in total

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