Periplasmic copper-zinc superoxide dismutase protects Haemophilus ducreyi from exogenous superoxide
نویسندگان
چکیده
منابع مشابه
Total reconstitution of copper-zinc superoxide dismutase.
The total reconstitution of copper-zinc superoxide dismutase by stoichiometric addition of the metals to completely metal-free apoprotein is described. Reconstitution has been monitored by electron paramagnetic resonance (EPR) and absorption spectroscopy, enzymic activity, and acrylamide gel el%ctrophoresis. Under the same conditions, it has been possible to prepare highly active enzymes with c...
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We have isolated the cytosolic form of Cu-Zn superoxide dismutase (SOD) from the marine yeast Debaryomyces hansenii. This enzyme has a subunit mass of 18 kDa. The preparation was found to be heterogeneous by IF electrophoresis with two pI ranges: 5.14-4.0 and 1.6-1.8. The enzyme preparation had a remarkably strong stability at pH 6.0-7.0, surviving boiling for 10 min without losing more than 60...
متن کاملPrimary structure of copper-zinc superoxide dismutase from Neurospora crassa.
The complete amino acid sequence of copper-zinc superoxide dismutase from Neurospora crassa is reported. The subunit consists of 153 amino acids and has a Mr of 15,850. The primary structure was determined by automated and manual sequence analysis of peptides obtained by digestions of the carboxymethylated and aminoethylated enzyme with trypsin and thermolysin. The protein is devoid of tryptoph...
متن کاملHuman copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants.
An Escherichia coli double mutant, sodAsodB, that is deficient in both bacterial superoxide dismutases (Mn superoxide dismutase and iron superoxide dismutase) is unable to grow on minimal medium in the presence of oxygen and exhibits increased sensitivity to paraquat and hydrogen peroxide. Expression of the evolutionarily unrelated eukaryotic CuZn superoxide dismutase in the sodAsodB E. coli mu...
متن کاملPeriplasmic superoxide dismutase in meningococcal pathogenicity.
Meningococcal sodC encodes periplasmic copper- and zinc-cofactored superoxide dismutase (Cu,Zn SOD) which catalyzes the conversion of the superoxide radical anion to hydrogen peroxide, preventing a sequence of reactions leading to production of toxic hydroxyl free radicals. From its periplasmic location, Cu,Zn SOD was inferred to acquire its substrate from outside the bacterial cell and was spe...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 1998
ISSN: 0950-382X,1365-2958
DOI: 10.1046/j.1365-2958.1998.00687.x