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Journal of Bacteriology, August 2003, p. 4345-4353, Vol. 185, No. 15
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.15.4345-4353.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Gene Expression Analysis of Energy Metabolism Mutants of Desulfovibrio vulgaris Hildenborough Indicates an Important Role for Alcohol Dehydrogenase

Shelley A. Haveman,1 Véronique Brunelle,1 Johanna K. Voordouw,1 Gerrit Voordouw,1* John F. Heidelberg,2 and Ralf Rabus3

Department of Biological Sciences, University of Calgary, Calgary, Alberta, T2N 1N4, Canada,1 The Institute for Genomic Research, Rockville, Maryland, 20850,2 Max-Planck Institute for Marine Microbiology, D-28359 Bremen, Germany3

Received 26 February 2003/ Accepted 13 May 2003

Comparison of the proteomes of the wild-type and Fe-only hydrogenase mutant strains of Desulfovibrio vulgaris Hildenborough, grown in lactate-sulfate (LS) medium, indicated the near absence of open reading frame 2977 (ORF2977)-coded alcohol dehydrogenase in the hyd mutant. Hybridization of labeled cDNA to a macroarray of 145 PCR-amplified D. vulgaris genes encoding proteins active in energy metabolism indicated that the adh gene was among the most highly expressed in wild-type cells grown in LS medium. Relative to the wild type, expression of the adh gene was strongly downregulated in the hyd mutant, in agreement with the proteomic data. Expression was upregulated in ethanol-grown wild-type cells. An adh mutant was constructed and found to be incapable of growth in media in which ethanol was both the carbon source and electron donor for sulfate reduction or was only the carbon source, with hydrogen serving as electron donor. The hyd mutant also grew poorly on ethanol, in agreement with its low level of adh gene expression. The adh mutant grew to a lower final cell density on LS medium than the wild type. These results, as well as the high level of expression of adh in wild-type cells on media in which lactate, pyruvate, formate, or hydrogen served as the sole electron donor for sulfate reduction, indicate that ORF2977 Adh contributes to the energy metabolism of D. vulgaris under a wide variety of metabolic conditions. A hydrogen cycling mechanism is proposed in which protons and electrons originating from cytoplasmic ethanol oxidation by ORF2977 Adh are converted to hydrogen or hydrogen equivalents, possibly by a putative H2-heterodisulfide oxidoreductase complex, which is then oxidized by periplasmic Fe-only hydrogenase to generate a proton gradient.

* 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, August 2003, p. 4345-4353, Vol. 185, No. 15
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.15.4345-4353.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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