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Journal of Bacteriology, November 2004, p. 7821-7825, Vol. 186, No. 22
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.22.7821-7825.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Humboldt-Universität zu Berlin, Institut für Biologie/Mikrobiologie, 10115 Berlin, Germany
Received 9 July 2004/ Accepted 16 August 2004
Metal-dependent superoxide dismutases (SODs) with a specific requirement for a manganese or iron ion for catalytic activity and copper- and zinc-dependent enzymes are essential for detoxification of superoxide anion radicals. Genome sequence analyses predict the existence of a nickel-dependent enzyme (NiSOD) as the unique SOD in oxygen-evolving marine cyanobacteria. NiSOD activity was observed in Escherichia coli when sodN and sodX (encoding a putative peptidase) from Prochlorococcus marinus MIT9313 were coexpressed.
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