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(Received for publication, June 3, 1997, and in revised form, July 14, 1997)
From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
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.
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