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Ca2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Co2+
-
Co(II) can substitute for zinc in erythrocytes
Mg2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Cu2+
-
-
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
heart: 1.64 mol of Cu per mol of enzyme, erythrocyte: 1.84 mol of Cu per mol of enzyme
Cu2+
-
the concentration of enzyme bound Cu2+ is 1.63 mg/l, the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], replacement of natural cofactor Cu2+ by isotopically enriched 65Cu, method, overview
Mn2+
-
contains no manganese
Mn2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Zn2+
-
-
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
the concentration of enzyme bound Zn2+ is 1.68 mg/l, the Zn ion plays a structural role, replacement of natural cofactor Zn2+ by isotopically enriched 68Zn, method, overview
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
relevance of the zinc imidazolate bond to the redox properties
additional information
-
overview: metal content
additional information
-
role of copper and zinc in protein conformation and activity
additional information
-
Cu2+ and Zn2+ binding sites are very close to each other
additional information
-
Cu2+-binding site
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
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Keele, B.B.; McCord, J.M.; Fridovich, I.
Further characterization of bovine superoxide dismutase and its isolation from bovine heart
J. Biol. Chem.
246
2875-2880
1971
Bos taurus
brenda
Cass, A.E.G.
Superoxide dismutases
Top. Mol. Struct. Biol.
6
121-156
1985
Geobacillus stearothermophilus, Bos taurus, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Photobacterium leiognathi, Propionibacterium freudenreichii subsp. shermanii, Bos taurus CuZn-SOD, Photobacterium leiognathi CuZn-SOD, Caulobacter vibrioides CuZn-SOD, Caulobacter vibrioides CB15, Escherichia coli Mn-SOD, Escherichia coli Fe-SOD, Saccharomyces cerevisiae CuZn-SOD, Geobacillus stearothermophilus Mn-SOD, Saccharomyces cerevisiae Mn-SOD
-
brenda
Flohe, L.; tting, F.
Superoxide dismutase assays
Methods Enzymol.
105
93-104
1984
Bos taurus, Homo sapiens, Homo sapiens CuZn-SOD
brenda
Munkres, K.D.
Purification of exocellular superoxide dismutases
Methods Enzymol.
186
249-260
1990
Bacillus subtilis, Bos taurus, Escherichia coli, Saccharomyces cerevisiae, Triticum aestivum
brenda
Rigo, A.; Viglino, P.; Rotilio, G.
Kinetic study of o2-dismutation by bovine superoxide dismutase. Evidence for saturation of the catalytic sites by O-2
Biochem. Biophys. Res. Commun.
63
1013-1018
1975
Bos taurus, Bos taurus CuZn-SOD
brenda
Rigo, A.; Terenzi, M.; Viglino, P.; Calabrese, L.; Cocco, D.; Rotilio, G.
The binding of copper ions to copper-free bovine superoxide dismutase. Properties of the protein recombined with increasing amounts of copper ions
Biochem. J.
161
31-35
1977
Bos taurus
brenda
Morpurgo, L.; Mavelli, I.; Calabrese, L.; Agro, A.F.; Rotilio, G.
A ferrocyanide charge-transfer complex of bovine superoxide dismutase. Relevance of the zinc imidazolate bond to the redox properties of the enzyme
Biochem. Biophys. Res. Commun.
70
607-614
1976
Bos taurus, Bos taurus CuZn-SOD
brenda
Fee, J.A.; DeCorleto, P.E.
Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase
Biochemistry
12
4893-4899
1973
Bos taurus, Bos taurus CuZn-SOD
brenda
Rotilio, G.; Calabrese, L.; Bossa, F.; Barra, D.; Agro, A.F.; Mondovi, B.
Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase
Biochemistry
11
2182-2187
1972
Bos taurus, Bos taurus CuZn-SOD
brenda
Weser, U.; Prinz, R.; Schallies, A.; Fretzdorff, A.; Krauss, P.; Voelter, W.; Voetsch, W.
Microbial and hepatic cuprein (superoxide dismutase). Isolation and characterisation of cuprein (superoxide dismutase) from Saccharomyces cerevisiae and bovine liver
Hoppe-Seyler's Z. Physiol. Chem.
353
1821-1831
1972
Bos taurus, Saccharomyces cerevisiae, Bos taurus CuZn-SOD, Saccharomyces cerevisiae CuZn-SOD
brenda
Calabrese, L.; Rotilio, G.; Mondovi, B.
Cobalt erythrocuprein: preparation and properties
Biochim. Biophys. Acta
263
827-829
1972
Bos taurus, Bos taurus CuZn-SOD
brenda
Michel, E.; Nauser, T.; Sutter, B.; Bounds, P.L.; Koppenol, W.H.
Kinetics properties of Cu,Zn-superoxide dismutase as a function of metal content
Arch. Biochem. Biophys.
439
234-240
2005
Bos taurus
brenda
Agbas, A.; Hui, D.; Wang, X.; Tek, V.; Zaidi, A.; Michaelis, E.K.
Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo
Biochem. J.
405
51-59
2007
Bos taurus, Homo sapiens
brenda
Ye, M.; English, A.M.
Binding of polyaminocarboxylate chelators to the active-site copper inhibits the GSNO-reductase activity but not the superoxide dismutase activity of Cu,Zn-superoxide dismutase
Biochemistry
45
12723-12732
2006
Bos taurus
brenda
Goldstein, S.; Fridovich, I.; Czapski, G.
Kinetic properties of Cu,Zn-superoxide dismutase as a function of metal content-order restored
Free Radic. Biol. Med.
41
937-941
2006
Bos taurus
brenda
Jiang, W.; Shen, T.; Han, Y.; Pan, Q.; Liu, C.
Divalent-metal-dependent nucleolytic activity of Cu, Zn superoxide dismutase
J. Biol. Inorg. Chem.
11
835-848
2006
Bos taurus (P00442), Bos taurus
brenda
Jiang, W.; Han, Y.; Pan, Q.; Shen, T.; Liu, C.
Roles of exogenous divalent metals in the nucleolytic activity of Cu,Zn superoxide dismutase
J. Inorg. Biochem.
101
667-677
2007
Bos taurus
brenda
Deitrich, C.L.; Raab, A.; Pioselli, B.; Thomas-Oates, J.E.; Feldmann, J.
Chemical preparation of an isotopically enriched superoxide dismutase and its characterization as a standard for species-specific isotope dilution analysis
Anal. Chem.
79
8381-8390
2007
Bos taurus
brenda
Zhan, Z.J.; Zhou, Z.G.; Shan, W.G.
Preparation and characterization of Cu,Zn-superoxide dismutase covalently modified by polyunsaturated fatty acids
Biochemistry (Moscow)
74
1266-1269
2009
Bos taurus
brenda
Ramasarma, T.; Rao, A.V.; Devi, M.M.; Omkumar, R.V.; Bhagyashree, K.S.; Bhat, S.V.
New insights of superoxide dismutase inhibition of pyrogallol autoxidation
Mol. Cell. Biochem.
400
277-285
2015
Bos taurus
brenda