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Superoxide Dismutase from Escherichia coli B

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Keele, Bernard B., McCord, J.M., Fridovich, I.·1970·Journal of Biological Chemistry

Abstract

Superoxide dismutase, which catalyzes the disproportionation of univalently reduced oxygen (O2.- + O2.- + 2H+ → O2 + H2O2) and which has previously been demonstrated in a variety of mammalian sources, has now been purified from Escherichia coli. Whereas the mammalian enzyme is blue and contains copper and zinc, the bacterial superoxide dismutase is red-purple and was found to contain manganese. The molecular weight of the E. coli enzyme was found to be 39,500 by sedimentation equilibrium and was shown, by gel electrophoresis in the presence of sodium dodecyl sulfate, to be composed of two subunits of equal size. Electron paramagnetic resonance spectrometry and chemical analysis demonstrated between 1.6 and 1.8 atoms of manganese per molecule of enzyme. The enzyme contains no significant amounts of copper or zinc. The ultraviolet and visible absorption spectra of the enzyme are presented, as are the results of amino acid analysis.

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Metadata

Authors
Keele, B. B., McCord, J. M., & Fridovich, I.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1970-11
Volume
245
Issue
22
Pages
6176-6181
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1514186391
Cited by
559
References
0
FWCI
17.92
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Superoxide Dismutase from Escherichia coli B. https://app.cochat.ai/papers/10.1016/s0021-9258(18)62675-4
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Keele, B. B., McCord, J. M., & Fridovich, I. (1970). Superoxide Dismutase from Escherichia coli B. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)62675-4

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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