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Journal of Bacteriology, January 2001, p. 101-108, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.101-108.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Rubrerythrin and Rubredoxin Oxidoreductase in Desulfovibrio vulgaris: a Novel Oxidative Stress Protection System

Heather L. Lumppio,1,2 Neeta V. Shenvi,2,3 Anne O. Summers,1,2 Gerrit Voordouw,4 and Donald M. Kurtz Jr.2,3,*

Departments of Chemistry3 and Microbiology1 and Center for Metalloenzyme Studies,2 University of Georgia, Athens, Georgia 30602, and Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada4

Received 15 June 2000/Accepted 11 October 2000

Evidence is presented for an alternative to the superoxide dismutase (SOD)-catalase oxidative stress defense system in Desulfovibrio vulgaris (strain Hildenborough). This alternative system consists of the nonheme iron proteins, rubrerythrin (Rbr) and rubredoxin oxidoreductase (Rbo), the product of the rbo gene (also called desulfoferrodoxin). A Delta rbo strain of D. vulgaris was found to be more sensitive to internal superoxide exposure than was the wild type. Unlike Rbo, expression of plasmid-borne Rbr failed to restore the aerobic growth of a SOD-deficient strain of Escherichia coli. Conversely, plasmid-borne expression of two different Rbrs from D. vulgaris increased the viability of a catalase-deficient strain of E. coli that had been exposed to hydrogen peroxide whereas Rbo actually decreased the viability. A previously undescribed D. vulgaris gene was found to encode a protein having 50% sequence identity to that of E. coli Fe-SOD. This gene also encoded an extended N-terminal sequence with high homologies to export signal peptides of periplasmic redox proteins. The SOD activity of D. vulgaris is not affected by the absence of Rbo and is concentrated in the periplasmic fraction of cell extracts. These results are consistent with a superoxide reductase rather than SOD activity of Rbo and with a peroxidase activity of Rbr. A joint role for Rbo and Rbr as a novel cytoplasmic oxidative stress protection system in D. vulgaris and other anaerobic microorganisms is proposed.

* Corresponding author. Mailing address: Department of Chemistry, University of Georgia, Athens, GA 30602. Phone: (706) 542-2016. Fax: (706) 542-9454. E-mail: kurtz{at}sunchem.chem.uga.edu.

Journal of Bacteriology, January 2001, p. 101-108, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.101-108.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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