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J. Bacteriol., 11 1995, 6330-6337, Vol 177, No. 22
Copyright © 1995, American Society for Microbiology

Pseudomonas aeruginosa sodA and sodB mutants defective in manganese- and iron-cofactored superoxide dismutase activity demonstrate the importance of the iron-cofactored form in aerobic metabolism

DJ Hassett, HP Schweizer and DE Ohman
Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Ohio 45257-0524, USA.

The consumption of molecular oxygen by Pseudomonas aeruginosa can lead to the production of reduced oxygen species, including superoxide, hydrogen peroxide, and the hydroxyl radical. As a first line of defense against potentially toxic levels of endogenous superoxide, P. aeruginosa possesses an iron- and manganese-cofactored superoxide dismutase (SOD) to limit the damage evoked by this radical. In this study, we have generated mutants which possess an interrupted sodA (encoding manganese SOD) or sodB (encoding iron SOD) gene and a sodA sodB double mutant. Mutagenesis of sodA did not significantly alter the aerobic growth rate in rich medium (Luria broth) or in glucose minimal medium in comparison with that of wild-type bacteria. In addition, total SOD activity in the sodA mutant was decreased only 15% relative to that of wild-type bacteria. In contrast, sodB mutants grew much more slowly than the sodA mutant or wild-type bacteria in both media, and sodB mutants possessed only 13% of the SOD activity of wild-type bacteria. There was also a progressive decrease in catalase activity in each of the mutants, with the sodA sodB double mutant possessing only 40% of the activity of wild-type bacteria. The sodA sodB double mutant grew very slowly in rich medium and required approximately 48 h to attain saturated growth in minimal medium. There was no difference in growth of either strain under anaerobic conditions. Accordingly, the sodB but not the sodA mutant demonstrated marked sensitivity to paraquat, a superoxide-generating agent.(ABSTRACT TRUNCATED AT 250 WORDS)

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