Literature DB >> 1311556

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

W J Ingledew1, R A Rothery, R B Gennis, J C Salerno.   

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.

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Year:  1992        PMID: 1311556      PMCID: PMC1130916          DOI: 10.1042/bj2820255

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  20 in total

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

Authors:  J C Salerno; W J Ingledew
Journal:  Eur J Biochem       Date:  1991-06-15

2.  EPR studies of the cytochrome-d complex of Escherichia coli.

Authors:  S W Meinhardt; R B Gennis; T Ohnishi
Journal:  Biochim Biophys Acta       Date:  1989-06-23

3.  Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli.

Authors:  C W Rice; W P Hempfling
Journal:  J Bacteriol       Date:  1978-04       Impact factor: 3.490

4.  Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli.

Authors:  J C Salerno; B Bolgiano; R K Poole; R B Gennis; W J Ingledew
Journal:  J Biol Chem       Date:  1990-03-15       Impact factor: 5.157

5.  Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli.

Authors:  A Puustinen; M Finel; M Virkki; M Wikström
Journal:  FEBS Lett       Date:  1989-06-05       Impact factor: 4.124

6.  The cytochromes of anaerobically grown Escherichia coli. An electron-paramagnetic-resonance study of the cytochrome bd complex in situ.

Authors:  R A Rothery; W J Ingledew
Journal:  Biochem J       Date:  1989-07-15       Impact factor: 3.857

7.  Characterization and phenotypic control of the cytochrome content of Escherichia coli.

Authors:  G A Reid; W J Ingledew
Journal:  Biochem J       Date:  1979-08-15       Impact factor: 3.857

8.  The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli.

Authors:  M J Miller; R B Gennis
Journal:  J Biol Chem       Date:  1985-11-15       Impact factor: 5.157

9.  The light-reversible binding of carbon monoxide to cytochrome a1 in Escherichia coli K12.

Authors:  R K Poole; R I Scott; B Chance
Journal:  J Gen Microbiol       Date:  1981-08

10.  Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis.

Authors:  H Fang; R J Lin; R B Gennis
Journal:  J Biol Chem       Date:  1989-05-15       Impact factor: 5.157

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  5 in total

1.  Oxoferryl-porphyrin radical catalytic intermediate in cytochrome bd oxidases protects cells from formation of reactive oxygen species.

Authors:  Angela Paulus; Sebastiaan Gijsbertus Hendrik Rossius; Madelon Dijk; Simon de Vries
Journal:  J Biol Chem       Date:  2012-01-27       Impact factor: 5.157

Review 2.  The cytochrome bd respiratory oxygen reductases.

Authors:  Vitaliy B Borisov; Robert B Gennis; James Hemp; Michael I Verkhovsky
Journal:  Biochim Biophys Acta       Date:  2011-07-01

3.  Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?

Authors:  M H Vos; V B Borisov; U Liebl; J L Martin; A A Konstantinov
Journal:  Proc Natl Acad Sci U S A       Date:  2000-02-15       Impact factor: 11.205

4.  Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli.

Authors:  J J Hill; J O Alben; R B Gennis
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-15       Impact factor: 11.205

5.  Homologous bd oxidases share the same architecture but differ in mechanism.

Authors:  Alexander Theßeling; Tim Rasmussen; Sabrina Burschel; Daniel Wohlwend; Jan Kägi; Rolf Müller; Bettina Böttcher; Thorsten Friedrich
Journal:  Nat Commun       Date:  2019-11-13       Impact factor: 14.919

  5 in total

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