An Iron-containing Superoxide Dismutase from Escherichia coli
Year: 1973
Type: article
Abstract: Escherichia coli B contains two electrophoretically distinct superoxide dismutases, one of which was previously isolated and found to be a mangano-protein. We have now isolated the other superoxide dismutase present in this organism. It contains 1 atom of Fe3+ per molecule and exhibits spectral properties reminiscent of aconitase. Its molecular weight is 38,700 and it is composed of two subunits of equal size which are not covalently joined. The amino acid composition of this ferrisuperoxide dismutase is similar to that of the mangano-enzyme previously isolated from the same source.
Source: Journal of Biological Chemistry
Authors: Frederick J. Yost, Irwin Fridovich
Institution: Duke Medical Center
Language: English
Subfield: Inorganic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1576106895