期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 402, 期 1, 页码 104-109出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(02)00065-6
关键词
manganese in Escherichia coli; superoxide scavenging by manganese; SOD mutants; complementation by Mn(II); aconitase; protection by Mn(II)
Escherichia coli, lacking cytoplasmic superoxide dismutases, exhibits a variety of oxygen-dependent phenotypic deficits. Enrichment of the growth medium with Mn(II) relieved those deficits. Extracts of cells grown on Mn(II)-rich medium exhibited superoxide dismutase-like activity that was due partially to low-molecular-weight and partially to high-molecular-weight complexes. The high-molecular-weight activity was sensitive to proteolysis. Hence this activity is likely associated with low-affinity binding of Mn to proteins. (C) 2002 Elsevier Science (USA). All rights reserved.
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