Literature DB >> 6378887

Cytochrome o as a terminal oxidase and receptor for aerotaxis in Salmonella typhimurium.

D J Laszlo, B L Fandrich, A Sivaram, B Chance, B L Taylor.   

Abstract

Cytochrome o was the only oxidase of the electron transport system that was present in exponentially growing Salmonella typhimurium ST1. Identification of cytochrome o was made by the (CO-reduced)-minus-(reduced) difference spectra and by the photochemical action spectrum of the relief, by light, of CO-inhibited respiration. Cytochrome o also functioned as the receptor for chemotaxis to oxygen (aerotaxis). The concentration of oxygen that elicits the maximum response for aerotaxis (0.7 microM) was similar to the Km for respiration (0.74 microM), and both aerotaxis and respiration were blocked 5 mM KCN.

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Year:  1984        PMID: 6378887      PMCID: PMC215695          DOI: 10.1128/jb.159.2.663-667.1984

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  24 in total

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Journal:  Annu Rev Biochem       Date:  1975       Impact factor: 23.643

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Journal:  J Biol Chem       Date:  1956-01       Impact factor: 5.157

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Journal:  Proc Natl Acad Sci U S A       Date:  1972-09       Impact factor: 11.205

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Journal:  J Biol Chem       Date:  1974-07-10       Impact factor: 5.157

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Authors:  A K Drabikowska
Journal:  Acta Biochim Pol       Date:  1970       Impact factor: 2.149

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Journal:  Biochim Biophys Acta       Date:  1966-03-07

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Authors:  J Adler
Journal:  Science       Date:  1969-12-26       Impact factor: 47.728

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Authors:  R M Daniel
Journal:  Biochim Biophys Acta       Date:  1970-09-01

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Authors:  D J Laszlo; B L Taylor
Journal:  J Bacteriol       Date:  1981-02       Impact factor: 3.490

10.  Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction.

Authors:  J Ruiz-Herrera; J A DeMoss
Journal:  J Bacteriol       Date:  1969-09       Impact factor: 3.490

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  10 in total

1.  Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxis.

Authors:  Jessica C Edwards; Mark S Johnson; Barry L Taylor
Journal:  Mol Microbiol       Date:  2006-09-21       Impact factor: 3.501

Review 2.  Nitrate respiration in relation to facultative metabolism in enterobacteria.

Authors:  V Stewart
Journal:  Microbiol Rev       Date:  1988-06

3.  Inversion of aerotactic response in Escherichia coli deficient in cheB protein methylesterase.

Authors:  C V Dang; M Niwano; J Ryu; B L Taylor
Journal:  J Bacteriol       Date:  1986-04       Impact factor: 3.490

4.  A signal transducer for aerotaxis in Escherichia coli.

Authors:  S I Bibikov; R Biran; K E Rudd; J S Parkinson
Journal:  J Bacteriol       Date:  1997-06       Impact factor: 3.490

5.  Oxygen as attractant and repellent in bacterial chemotaxis.

Authors:  J Shioi; C V Dang; B L Taylor
Journal:  J Bacteriol       Date:  1987-07       Impact factor: 3.490

6.  Signal transduction in chemotaxis to oxygen in Escherichia coli and Salmonella typhimurium.

Authors:  J Shioi; R C Tribhuwan; S T Berg; B L Taylor
Journal:  J Bacteriol       Date:  1988-12       Impact factor: 3.490

7.  Oxygen taxis and proton motive force in Azospirillum brasilense.

Authors:  I B Zhulin; V A Bespalov; M S Johnson; B L Taylor
Journal:  J Bacteriol       Date:  1996-09       Impact factor: 3.490

8.  Anaerobic electron acceptor chemotaxis in Shewanella putrefaciens.

Authors:  K H Nealson; D P Moser; D A Saffarini
Journal:  Appl Environ Microbiol       Date:  1995-04       Impact factor: 4.792

9.  Bacillus cereus electron transport and proton motive force during aerotaxis.

Authors:  D J Laszlo; M Niwano; W W Goral; B L Taylor
Journal:  J Bacteriol       Date:  1984-09       Impact factor: 3.490

10.  Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli.

Authors:  C Khosla; J E Bailey
Journal:  J Bacteriol       Date:  1989-11       Impact factor: 3.490

  10 in total

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