Literature DB >> 2843510

The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli.

G N Green1, H Fang, R J Lin, G Newton, M Mather, C D Georgiou, R B Gennis.   

Abstract

The cytochrome d terminal oxidase complex is one of two terminal oxidases in the aerobic respiratory chain of Escherichia coli. The enzyme is located in the cytoplasmic membrane where it oxidizes ubiquinol-8 in the bilayer and reduces oxygen to water. Enzyme turnover is coupled to the generation of a proton-motive force, resulting in electrogenic translocation across the membrane of one proton per electron passing through the system. The enzyme is an alpha beta heterodimer containing four hemes. The cyd locus, encoding both subunits, has previously been genetically mapped and cloned. This work describes an insertion and deletion analysis of cyd which indicates the direction of transcription, defines the coding regions, and suggests that cyd is an operon. In addition, the complete DNA sequence of the cyd gene is reported. Two open reading frames, separated by 18 base pairs, encode the two subunits of the oxidase complex. Hydropathy profiles of the deduced protein sequence indicate that subunits I and II are each likely to have multiple transmembrane elements. There are only 10 histidines in both subunits, several of which are likely to serve as heme axial ligands.

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Year:  1988        PMID: 2843510

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  41 in total

Review 1.  Sodium ion cycle in bacterial pathogens: evidence from cross-genome comparisons.

Authors:  C C Häse; N D Fedorova; M Y Galperin; P A Dibrov
Journal:  Microbiol Mol Biol Rev       Date:  2001-09       Impact factor: 11.056

2.  Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection.

Authors:  S Endley; D McMurray; T A Ficht
Journal:  J Bacteriol       Date:  2001-04       Impact factor: 3.490

3.  Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy.

Authors:  Fabrice Rappaport; Jie Zhang; Marten H Vos; Robert B Gennis; Vitaliy B Borisov
Journal:  Biochim Biophys Acta       Date:  2010-05-28

Review 4.  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

5.  Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica.

Authors:  Amaresh Das; Radu Silaghi-Dumitrescu; Lars G Ljungdahl; Donald M Kurtz
Journal:  J Bacteriol       Date:  2005-03       Impact factor: 3.490

6.  Essential role of cytochrome bd-related oxidase in cyanide resistance of Pseudomonas pseudoalcaligenes CECT5344.

Authors:  Alberto Quesada; M Isabel Guijo; Faustino Merchán; Blas Blázquez; M Isabel Igeño; Rafael Blasco
Journal:  Appl Environ Microbiol       Date:  2007-06-15       Impact factor: 4.792

7.  Mode of bactericidal action of silver zeolite and its comparison with that of silver nitrate.

Authors:  Yoshinobu Matsumura; Kuniaki Yoshikata; Shin-ichi Kunisaki; Tetsuaki Tsuchido
Journal:  Appl Environ Microbiol       Date:  2003-07       Impact factor: 4.792

8.  Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain.

Authors:  M W Calhoun; K L Oden; R B Gennis; M J de Mattos; O M Neijssel
Journal:  J Bacteriol       Date:  1993-05       Impact factor: 3.490

9.  E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli.

Authors:  M W Calhoun; G Newton; R B Gennis
Journal:  J Bacteriol       Date:  1991-03       Impact factor: 3.490

10.  Azorhizobium caulinodans respires with at least four terminal oxidases.

Authors:  C L Kitts; R A Ludwig
Journal:  J Bacteriol       Date:  1994-02       Impact factor: 3.490

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