• Journal of Microbiology
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• v.39 no.3
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• pp.232-235
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• 2001

Electrophoretic resolution of superoxide dismutase (SOD) from the highly UV-resistant bacteria, Deinococcus species revealed multiple forms of superoxide dismutases (SODs) in D. radiodurans, D. grandis, and D. proteolyticus, as judged from electrophoretic properties and metal cofactors. A single SOD occurred in both D. radiophilus and D. radiopugnans. Deinococcal SODs were either MnSOD, FeSOD or cambialistic Mn/FeSOD. The unique SOD profile of each mesophilic Deinococcus species, multiplicity and metal cofactors would be valuable in identifying Deinococcus species.

• BMB Reports
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• v.33 no.5
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• pp.412-416
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• 2000

The obligate aerobic Deinococcus are highly resistant against lethal effect of UV-and ionizing-radiation. Only five mesophilic Deinococcus species, i. e. D. radiodurans, D. radiophilus, D. proteolyticus, D. radiopugnans, and D. grandis are known. Since an indispensable role of catalase has been suggested in protecting cells against oxidative stress and UV radiation, Deinococcal catalase activity of each species and electrophoretic profiles of catalases were investigated on gel. Total catalase activity was varied among the species in the aerobically grown culture at stationary phase. The occurrence of multiple forms of catalases with different molecular weights in four species of Deinococcus and of a single catalase in D. radiopugnans suggests that each species shows the unique catalase profiles on gel. Some Deinococcal catalases also exhibit peroxidase activity. Since Deinococcus spp. are less-distinct to each other in their morphology, biochemical and physiological properties, the catalase profiles on PAGE would be useful in identifying the species of Deinococcus.

• Journal of Microbiology
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• v.44 no.4
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• pp.461-465
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• 2006

The occurrence of thioredoxin reductase (NAD(P)H: oxidized-thioredoxin reductase, EC 1.6.4.5, TrxR) in five mesophilic species of Deinococcus was investigated by PAGE. Each species possessed a unique TrxR pattern, for example, a single TrxR characterized D. radiopugnans while multiple forms of TrxR occurred in other Deinococcal spp. Most of TrxRs occurring in Deinococcus showed dual cofactor specificity, active with either NADH or NADPH, although the NADPH specific-TrxR was observed in D. radiophilus and D. proteolytic us.