Growth in Iron-enriched Medium Partially Compensates Escherichia coli for the Lack of Manganese and Iron Superoxide Dismutase
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چکیده
منابع مشابه
Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.
The crystal structure of dimeric Fe(III) superoxide dismutase (SOD) from Escherichia coli (3006 protein atoms, 2 irons, and 281 solvents) has been refined to an R of 0.184 using all observed data between 40.0 and 1.85 A (34,879 reflections). Features of this structure are compared with the refined structure of MnSOD from Thermus thermophilus. The coordination geometry at the Fe site is distorte...
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Mutants of Escherichia coli that lack cytoplasmic superoxide dismutase (SOD) exhibit auxotrophies for sulfur-containing, branched-chain, and aromatic amino acids and cannot catabolize nonfermentable carbon sources. A secondary-site mutation substantially relieved all of these growth defects. The requirement for fermentable carbon and the branched-chain auxotrophy occur because superoxide (O2-) ...
متن کاملOxygen toxicity in Streptococcus mutans: manganese, iron, and superoxide dismutase.
When cultured anaerobically in a chemically defined medium that was treated with Chelex-100 to lower its trace metal content, Streptococcus mutans OMZ176 had no apparent requirement for manganese or iron. Manganese or iron was necessary for aerobic cultivation in deep static cultures. During continuous aerobic cultivation in a stirred chemostat, iron did not support the growth rate achieved wit...
متن کاملFur positive regulation of iron superoxide dismutase in Escherichia coli: functional analysis of the sodB promoter.
In Escherichia coli, the expression of sodB, which encodes iron superoxide dismutase, has been suggested to be activated by Fur, the iron-responsive global regulator initially characterized as a transcriptional repressor. We investigated sodB regulation by functional analysis of the sodB promoter using sodB-lac fusions with various truncated and mutated promoters. Several cis- and trans-acting ...
متن کاملSpectroscopic measurement of a long-predicted active site pK in iron-superoxide dismutase from Escherichia coli.
The accepted mechanism of Fe-containing superoxide dismutase (Fe-SOD) activity and inhibition by anions implies the existence of a group with a pK of 8.6-9.0 in the active site of reduced Fe-SOD [Bull, C. & Fee, J. A. (1985) J. Am. Chem. Soc. 107, 3295-3304]. We have performed pH titrations of reduced Fe-SOD by NMR spectroscopy and observe a pK of 8.5 at 30 degrees C which is the only pK affect...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.17.10313