Send to

Choose Destination
See comment in PubMed Commons below
Microb Pathog. 2009 Jul;47(1):8-15. doi: 10.1016/j.micpath.2009.04.009. Epub 2009 May 3.

The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology.

Author information

Department of Microbiology, North Carolina State University, Raleigh, NC 27695, USA.


The human pathogen Campylobacter jejuni utilizes oxidative phosphorylation to meet all of its energy demands. The genome sequence of this bacterium encodes a number of respiratory enzymes in a branched electron transport chain that predicts the utilization of a number of electron transport chain donor and acceptor molecules. Three of these electron donor enzymes: hydrogenase, formate dehydrogenase, and 2-oxoglutarate:acceptor oxidoreductase (OOR), oxidize hydrogen, formate and alpha-ketoglutarate as electron donors, respectively. Mutations were created in these donor enzymes to isolate mutants in hydrogenase (HydB::CM), formate dehydrogenase (Fdh::CM), and OOR (OorB::CM), as well as a strain with insertions in both hydrogenase and formate dehydrogenase (Hyd::Fdh). These mutants are deficient in their respective enzyme activities and do not reduce the components of the electron transport chain when provided with their respective substrates. The presence of either hydrogen or formate in the media stimulated the growth of wild type (WT) C. jejuni (but not the associated mutant strains) and at least one of these alternative substrates is required for growth of the OOR mutant strain OorB::CM. Finally, the importance of hydrogenase, formate dehydrogenase and OOR as well as the complex I of C. jejuni are elucidated by chicken colonization assays, where the double mutant Hyd::Fdh, OorB::CM and nuo mutants are severely impaired in host colonization.

[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center