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dc.contributor.authorSmith, MA.en_US
dc.contributor.authorFinel, M.en_US
dc.contributor.authorKorolik, Victoriaen_US
dc.contributor.authorMendz, GL.en_US
dc.date.accessioned2017-05-03T13:44:16Z
dc.date.available2017-05-03T13:44:16Z
dc.date.issued2000en_US
dc.date.modified2010-07-26T06:49:57Z
dc.identifier.issn03028933en_US
dc.identifier.doi10.1007/s002030000174en_AU
dc.identifier.urihttp://hdl.handle.net/10072/3438
dc.description.abstractThe 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.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherSpringer Verlagen_US
dc.publisher.placeGermanyen_US
dc.relation.ispartofpagefrom1en_US
dc.relation.ispartofpageto10en_US
dc.relation.ispartofjournalArchives of Microbiologyen_US
dc.relation.ispartofvolume174en_US
dc.subject.fieldofresearchcode320000en_US
dc.titleCharacteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobacter pylorien_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2000
gro.hasfulltextNo Full Text


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