Characteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobacter pylori

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Title Characteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobacter pylori
Author Smith, MA.; Finel, M.; Korolik, Victoria; Mendz, GL.
Journal Name Archives of Microbiology
Year Published 2000
Place of publication Germany
Publisher Springer Verlag
Abstract The respiratory chain enzymes of microaerophilic bacteria should play a major role in their adaptation to growth at low oxygen tensions. The genes encoding the putative NADH:quinone reductases (NDH-1), the ubiquinol:cytochrome c oxidoreductases (bc1 complex) and the terminal oxidases of the microaerophiles Campylobacter jejuni and Helicobacter pylori were analysed to identify structural elements that may be required for their unique energy metabolism. The gene clusters encoding NDH-1 in both C. jejuni and H. pylori lacked nuoE and nuoF, and in their place were genes encoding two unknown proteins. The NuoG subunit in these microaerophilic bacteria appeared to have an additional Fe-S cluster that is not present in NDH-1 from other organisms; but C. jejuni and H. pylori differed from each other in a cysteine-rich segment in this subunit, which is present in some but not all NDH-1. Both organisms lacked genes orthologous to those encoding NDH-2. The subunits of the bc1 complex of both bacteria were similar, and the Rieske Fe-S and cytochrome b subunits had significant similarity to those of Paracoccus denitrificans and Rhodobacter capsulatus, well-studied bacterial bc1 complexes. The composition of the terminal oxidases of C. jejuni and H. pylori was different; both bacteria had cytochrome cbb3 oxidases, but C. jejuni also contained a bd-type quinol oxidase. The primary structures of the major subunits of the cbb3-type (terminal) oxidase of C. jejuni and H. pylori indicated that they form a separate group within the cbb3 protein family. The implications of the results for the function of the enzymes and their adaptation to microaerophilic growth are discussed.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1007/s002030000174
Volume 174
Page from 1
Page to 10
ISSN 0302-8933
Date Accessioned 2001-01-01
Date Available 2010-07-26T06:49:57Z
Language en_AU
Research Centre Institute for Glycomics
Faculty Griffith Health Faculty
Subject PRE2009-Medical & Health Sciences
URI http://hdl.handle.net/10072/3438
Publication Type Article in Scholarly Refereed Journal
Publication Type Code c1

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