A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (desulfoferrodoxin) from Desulfoarculus baarsii.
Overexpression of rbo in Escherichia coli prevents the inactivation of the [4Fe-4S]-containing fumarases that otherwise occurs in the sodA sodB strain. It similarly protects against the increased sensitivity toward H2O2, which is imposed by the lack of SOD A and SOD B. These results would be explained on the basis of scavenging of O-2 within the cells by RBO. This interpretation was supported by measurements of intracellular scavenging of O-2 by the lucigenin luminescence method. Since SOD activity could not be detected in dilute extracts, of the RBO-overexpressing sodA sodB strain, we propose that RBO catalyzes the reduction of O-2 at the expense of cellular reductants such as NAD(P)H. A similar mechanism may apply to other instances of complementation of SOD defects by non-SOD genes.
Liochev
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Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Fridovich
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D000166:Acridines / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003901:Desulfovibrio / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli; D005288:Ferredoxins / Q000235:genetics / Q000378:metabolism*; D016166:Free Radical Scavengers / Q000378:metabolism; D005649:Fumarate Hydratase / Q000378:metabolism; D005816:Genetic Complementation Test; D006861:Hydrogen Peroxide / Q000378:metabolism; D008163:Luminescent Measurements; D010100:Oxygen / Q000378:metabolism; D010641:Phenotype; D013482:Superoxide Dismutase / Q000235:genetics / Q000378:metabolism*
D000166:Acridines; D001426:Bacterial Proteins; D005288:Ferredoxins; D016166:Free Radical Scavengers; C066602:desulfoferrodoxin; C033472:10,10'-dimethyl-9,9'-biacridinium; D006861:Hydrogen Peroxide; C095500:SodA protein, Bacteria; C087504:SodB protein, Bacteria; D013482:Superoxide Dismutase; D005649:Fumarate Hydratase; D010100:Oxygen