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• W1542542441 abstract "Superoxide dismutase of Propionibacterium shermanii, an anaerobic that produces an iron superoxide dismutase, was purified from cells grown in iron-free conditions. The enzyme isolated was found to contain manganese and to have spectral and catalytic properties very similar to those of typical Mn-superoxide dismutases. Its electrophoretic mobility, molecular weight, and subunit size were identical with those of the Fe-enzyme. Amino acid compositions were practically indistinguishable in either case. The NH2-terminal sequence was found to be identical. The catalytic activity of an apoprotein sample prepared from the purified holoenzyme was restored by adding either Mn(II) or Fe(II). Only the metal/protein ratio varied from approximately 1 per subunit in the case of the Fe-enzyme to approximately 2 for the Mn-enzyme. It is concluded that this bacterium can accommodate either Fe or Mn on identical, or very slightly dissimilar, proteins forming active sites with the properties found in specific metallodismutases." @default.
• W1542542441 created "2016-06-24" @default.
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• W1542542441 date "1982-12-01" @default.
• W1542542441 modified "2023-09-29" @default.
• W1542542441 title "Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied." @default.
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• W1542542441 doi "https://doi.org/10.1016/s0021-9258(19)45329-5" @default.
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