A novel nickel-containing superoxide dismutase from Streptomyces spp

A novel type of superoxide dismutase (SOD) was purified to apparent homogeneity from the cytosolic fractions of Streptomyces sp. IMSNU-1 and Strep. coelicolor ATCC 10147 respectively. Both enzymes were composed of four identical subunits of 13.4 kDa, were stable at pH 4.0-8.0 and up to 70 degrees C,...

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Bibliographic Details
Published in:Biochemical journal 1996-09, Vol.318 ( Pt 3) (3), p.889-896
Main Authors: Youn, H D, Kim, E J, Roe, J H, Hah, Y C, Kang, S O
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Animals
Binding Sites
Cattle
Enzyme Inhibitors - pharmacology
Enzyme Stability
Erythrocytes - enzymology
Escherichia coli - enzymology
Hydrogen-Ion Concentration
Immunoblotting
Molecular Sequence Data
Molecular Structure
Molecular Weight
Nickel - analysis
Protein Conformation
Saccharomyces cerevisiae - enzymology
Streptomyces - enzymology
Streptomyces - genetics
Superoxide Dismutase - chemistry
Superoxide Dismutase - genetics
Superoxide Dismutase - isolation & purification
Temperature
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Summary:A novel type of superoxide dismutase (SOD) was purified to apparent homogeneity from the cytosolic fractions of Streptomyces sp. IMSNU-1 and Strep. coelicolor ATCC 10147 respectively. Both enzymes were composed of four identical subunits of 13.4 kDa, were stable at pH 4.0-8.0 and up to 70 degrees C, and were inhibited by cyanide and H2O2 but little inhibited by azide. The atomic absorption analyses revealed that both enzymes contain 0.74 g-atom of nickel per mol of subunit. Both enzymes were different from iron-containing SOD and manganese-containing SOD from Escherichia coli, and copper- and zinc-containing SODs from Saccharomyces cerevisiae and bovine erythrocytes, with respect to amino acid composition, N-terminal amino acid sequence and cross-reactivity against antibody. The absorption spectra of both enzymes were identical, exhibiting maxima at 276 and 378 nm, and a broad peak at 531 nm. The EPR spectra of both enzymes were almost identical with that of NiIII in a tetragonal symmetry of NiIII-oligopeptides especially containing histidine. The apoenzymes, lacking in nickel, had no ability to mediate the conversion of superoxide anion radical to hydrogen peroxide, strongly indicating that NiIII plays a main role in these enzymes.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3180889