The Bordetella pertussis gene sodB, encoding superoxide dismutase (SOD), was cloned by complementation of an Escherichia coli sonAsodB double mutant. The nucleotide sequence of sodB predicted a 21-kDa protein with homology to manganese- and iron-containing SODs from other organisms. Examination of SOD activity on gels suggests that B. pel tussis extracts have a single SOD containing Fe3+ as a prosthetic group. A SOD-deficient mutant was obtained by insertional inactivation of sodB in B. pel tussis, confirming that there is only one SOD in this organism.