Reaction of copper-zinc superoxide dismutase with diethyldithiocarbamate.
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چکیده
منابع مشابه
Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutase.
The reaction of the copper of (Cu,Zn)-superoxide dismutase with diethyldithiocarbamate was studied at pH = 7.4 and the results obtained led to a reaction scheme basically different from the conclusion of a previous study (Misra, H. P. (1979) J. Biol. Chem. 254, 11623-11628). The analysis of optical and ESR spectra at 9 and 35 GHz, at different ligand/protein ratios and reaction times, showed th...
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The rate constants of the reactions between pulse radiolytically produced superoxide radicals and the Cu(II) chelate of diethyldithiocarbamate were determined at pH 7.0. It was found that diethyldithiocarbamate forms a copper complex, which as no dismutating activity. The removal of the protein bound copper in superoxide dismutase by diethyldithiocarbamate yields the same effect as coordination...
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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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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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)86530-4