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Journal of Bacteriology, February 2002, p. 679-686, Vol. 184, No. 3
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.3.679-686.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Effects of Deletion of Genes Encoding Fe-Only Hydrogenase of Desulfovibrio vulgaris Hildenborough on Hydrogen and Lactate Metabolism

Brant K. J. Pohorelic,1 Johanna K. Voordouw,1 Elisabeth Lojou,2 Alain Dolla,2 Jens Harder,3 and Gerrit Voordouw1,2,3*

Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada,1 BIP-IBSM-CNRS 13402 Marseilles Cedex 20, France,2 Max Planck Institute for Marine Microbiology, D-28359 Bremen, Germany3

Received 25 June 2001/ Accepted 31 October 2001

The physiological properties of a hyd mutant of Desulfovibrio vulgaris Hildenborough, lacking periplasmic Fe-only hydrogenase, have been compared with those of the wild-type strain. Fe-only hydrogenase is the main hydrogenase of D. vulgaris Hildenborough, which also has periplasmic NiFe- and NiFeSe-hydrogenases. The hyd mutant grew less well than the wild-type strain in media with sulfate as the electron acceptor and H2 as the sole electron donor, especially at a high sulfate concentration. Although the hyd mutation had little effect on growth with lactate as the electron donor for sulfate reduction when H2 was also present, growth in lactate- and sulfate-containing media lacking H2 was less efficient. The hyd mutant produced, transiently, significant amounts of H2 under these conditions, which were eventually all used for sulfate reduction. The results do not confirm the essential role proposed elsewhere for Fe-only hydrogenase as a hydrogen-producing enzyme in lactate metabolism (W. A. M. van den Berg, W. M. A. M. van Dongen, and C. Veeger, J. Bacteriol. 173:3688–3694, 1991). This role is more likely played by a membrane-bound, cytoplasmic Ech-hydrogenase homolog, which is indicated by the D. vulgaris genome sequence. The physiological role of periplasmic Fe-only hydrogenase is hydrogen uptake, both when hydrogen is and when lactate is the electron donor for sulfate reduction.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Calgary, 2500 University Dr. NW, Calgary, Alberta T2N 1N4, Canada. Phone: (403) 220-6388. Fax: (403) 289-9311. E-mail: voordouw{at}ucalgary.ca.

Journal of Bacteriology, February 2002, p. 679-686, Vol. 184, No. 3
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.3.679-686.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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