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Al3+
-
activates by 10% at 10 mM
Fe3+
activates the enzyme at 1 mM
Ca2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Ca2+
-
activates the enzyme
Ca2+
-
activates slightly by 10% at 5 mM
Co2+
-
Co(II) can substitute for zinc in erythrocytes
Co2+
-
the Co ion can stably substitute the native cofactor Mn ion
Co2+
-
Co2+ binds at zinc site
Co2+
-
27% stimulation of activity
copper
-
-
copper
-
peculiar axial geometry of copper active sitewith low accessibility to external chelating agents
copper
0.68 mol per mol of subunit
copper
recombinant enzyme, 0.9 mol per mol of subunit, native enzyme, 0.86 mol per mol of subunit
copper
-
coexpression with yeast copper chaperone, copper supplement of medium, about 1 atom per subunit
copper
-
wild-type, 0.98 atoms per subunit, mutant H43R, 1.42, mutant A4V, 1.06 atoms per subunit
copper
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
copper
-
1 atom per subunit
copper
Radix lethospermi
-
-
Cu
extracellular CuZnSOD
Cu
-
a Cu-Zn SOD, activates
Cu
-
a Cu/Zn superoxide dismutase
Cu
-
a Cu,Zn superoxide dismutase
Cu2+
a Cu/ZnSOD, highly conserved amino acid residues are involved in Cu/Zn binding
Cu2+
7 isozymes of CuZnSOD
Cu2+
a CuZn-superoxide dismutase
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
Cu2+
-
1.1 mol per mol of Cu,Zn-SOD
Cu2+
a CuZnSOD, Cherax quadricarinatus ecCuZnSOD contains a Cu signature from 59 to 69 (GFHVHEKGDLG), and four Cu binding sites (His 61,63, 78, and 137)
Cu2+
-
1 gatom per mol of enzyme
Cu2+
a CuZn-superoxide dismutase
Cu2+
-
an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His46, His48, His63, and His120 for Cu2+ binding
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1 gatom per mol of enzyme
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
-
a Cu,Zn-superoxide dismutase
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1.7 mol per mol of enzyme
Cu2+
-
extracellular EC-SOD with Cu,Zn-SOD activity
Cu2+
-
Cu,Zn-SOD mutant H63C
Cu2+
a Cu,ZnSOD with 1.07 Cu2+ per enzyme subunit, binding structure, position of Cu2+ in the Zn2+-deficient enzyme A chain active site, overview, physiologic function in Cu,Zn-SOD, overview
Cu2+
a CuZn-superoxide dismutase
Cu2+
required, enzyme-bound
Cu2+
a Cu/Zn-SOD, the enzyme contains 1.54 mg/l copper atoms, and 0.239 mol Cu2+ per mol of enzyme
Cu2+
isozyme Cu/Zn-SOD, the highly conserved histidine residues H47, H49, H64, H72, H81, and H121 are involved in the interaction with the metallic cofactors, which are essential for activity and folding in all the Sod1 enzymes, D84 is also involve in Cu2+ binding
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
a Cu,Zn-superoxide dismutase
Cu2+
a Cu,Zn-superoxide dismutase
Cu2+
a Cu,Zn-superoxide dismutase, residues H46, H48, H63, and H119 are involved in Cu2+ binding
Cu2+
-
mitochondrial cyanide-sensitive enzyme
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
a Cu/ZnSOD, the enzyme sequence harbors two Cu/ZnSOD signatures and seven metal liganding residues
Cu2+
a Cu/Zn-superoxide dismutase
Cu2+
-
a Cu/Zn-SOD, conserved amino acids required for binding copper and zinc
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
a CuZn-superoxide dismutase, the prosthetic copper and zinc are essential component of CuZn-SODs, 1.80-1.84 Cu2+ per enzyme dimer
Cu2+
-
a Cu/Zn-SOD. The isolated enzyme has 30% of its copper in the reduced state
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
activates the enzyme at 1 mM
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1.63-1.78 mol per mol of isoenzyme I
Cu2+
-
1.86-1.97 mol per mol of isoenzyme II
Cu2+
a CuZn-superoxide dismutase
Cu2+
-
activates slightly at 0.5-1.0 mM
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
Cu2+
Thermochaetoides thermophila
a CuZn-superoxide dismutase
Cu2+
-
activates by 16% at 10 mM
Cu2+
a Cu/Zn SOD, 0.83 ng atom Cu per mg protein
Cu2+
-
SOD-1, SOD-2 and SOD-4
Fe
-
cognate metal ions Mn, Fe, and Co can effectively occupy the metal site of superoxide dismutase, respectively. MnSOD exhibits the highest SOD activity of 8600 U/mg, while Fe-sub-MnSOD shows only 800 U/mg, and Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD
Fe
-
the recombinant SOD binds either Fe or Mn as a metal co-factor, with a consistent preference for Fe accommodation. But differently from the significant preference for Fe displays by the enzyme in the binding reaction, its Mn-form is 71fold more active compared to the Fe-form
Fe2+
a Fe-SOD, the enzyme is able to bind various bivalent metals in the active site
Fe2+
presence of 0.25 Fe atom and 0.01 Mn atom per monomer of protein
Fe2+
the SOD is active with Fe2+ and Mn2+, Fe2+ activates 6fold, binding structure, overview
Fe2+
the enzyme contains both Mn and Fe. It is cambialistic, i.e. active with either Fe2+ or Mn2+. The specific activities were 906 U/mg with Mn2+ and 175 U/mg with Fe2+
Fe2+
the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Fe-reconstituted enzyme contains 0.79 atom of iron per subunit
Fe2+
-
the Fe ion can stably substitute the native cofactor Mn ion
Fe2+
all isozymes in the organism are FeSODs
Fe2+
-
Fe-SOD contains 1 Fe2+ per subunit
Fe2+
Fe-SOD, 0.41 atom of Fe per SOD subunit
Fe2+
-
a Fe,Mn-SOD, the purified enzyme contains 1.1 g-atom of Fe per mol enzyme
Fe2+
a cambialistic Fe/Mn-superoxide dismutase, 0.56 g-atom per mol of enzyme
Fe2+
-
the enzyme is an iron SOD with 0.9 Fe/subunit
Fe2+
-
a Fe-SOD, the dimeric enzyme contains one iron atom/subunit
Fe2+
the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95°C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity
Fe2+
native enzyme from aerobically-grown cells grown in standard medium contains 0.55 mol Fe2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with manganese contains less than 0.01 mol Fe2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with iron contains 0.01 mol Fe2+ per mol of subunit. Native enzyme from anaerobically-grown cells grown in standard medium contains 0.43 mol Fe2+ per mol of subunit. Recombinant apo-enzyme contains less than 0.01 mol Fe2+ per mol of subunit. Mn2+-reconstituted recombinant enzyme contains less than 0.01 mol Fe2+ per mol of subunit. Fe2+-reconstituted recombinant enzyme contains 0.76 mol Mn2+ per mol of subunit. The recombinant protein has little activity due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn2+ or Fe2+ yields a highly active protein
Fe2+
-
Fe-type SOD, helices alpha1 and alpha2 contribute one metal ligand each, i.e. His33 and His84, binding structure, the iron is ligated by Nepsilon2 of His33, His84 and His174, by Odelta1 of Asp170, and a solvent molecule forming a distorted trigonal bipyramidal coordination sphere, overview
Fe2+
-
the homodimeric enzyme contains 0.7 atom of iron per subunit
Fe2+
-
a Fe-SOD, all iron-binding sites (His 27, His 80, Asp 164 and His 168) of SaFe-SOD are conserved
Fe2+
-
activates the enzyme
Fe2+
-
activates slightly by 10% at 5 mM
Fe2+
-
bound by His33, His84, His174, and Asp170, coordination in the active site, overview
Fe2+
Fe/Mn-type SOD, the Fe-type enzyme contains Gln85
Fe2+
a cambialistic Mn/Fe-SOD
Fe2+
recombinant mutant H29A and H171A specificity
Iron
the enzyme is a tetramer with 4 iron centers, one iron per monomer
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.6 mol per mol of enzyme
Iron
0.4 mol per mol of mn-SOD
Iron
30% of the activity with manganese
Iron
0.5-1.0 atom Fe2+ per subunit
Iron
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
each Fe3+ ion has 2 coordination positions available for interaction with solute molecules but only 1 is necessary for catalysis
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
spectroscopic analysis of reduced and oxidized state of iron. In oxidized state, formation of a six-coordinate complex occurs. Two substrate analogues F- can bind to the oxidized enzymes active site
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
0.9 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
contains 0.95 atoms of Fe per monomer
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
Megalodesulfovibrio gigas
-
-
Iron
-
1.1 mol per mol of subunit
Iron
contains 1 mol iron per mol of enzyme, but no manganese
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1 atom per subunit
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
accepts iron and/or manganese as cofactor
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
0.75 atoms per subunit
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
iron-superoxide dismutase, FeSOD, encoded by gene sodB
Iron
-
when mitochondrial iron homeostasis is disrupted, iron accumulates in a reactive form and competes with manganese, inactivating the enzyme. The ability to control the iron pool within mitochondria is critical to maintaining enzyme activity
Iron
-
0.24 mol Fe2+ per mol of subunit
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
contains one iron atom per dimer, the protein contains a mononuclear iron center
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
Thermosynechococcus vestitus
-
no change in the geometry of the FeII site occurs over a wide pH range
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
0.35 mol per mol of subunit, required both for activity and stability of enzyme tetramer
Manganese
most effcient metal ion
Manganese
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Manganese
-
when the Deinococcus radiodurans Mn2+SOD reacts with a substoichiometric amount of superoxide, Deinococcus radiodurans Mn3+SOD is produced
Manganese
analysis of manganese(II) high-field electron paramagnetic resonance spectrum. In the -248°C to -73°C range, the zero-field interaction steadily decreases with increasing temperature. Above -33°C, a distinct six-line component is detected derived from a hexacoordinate Mn(II) center resulting from coordination of normally five-coordinate Mn(II) by a water molecule. comparison with Mn(II) centers in concanavalin A and R. spheroides photosynthetic center
Manganese
-
kinetic study on metal binding mechanism. Apo-enzyme metallation kinetics are gated, zero order in metal ion for both native Mn2+ and nonnative Co2+. Cobalt-binding reveals two exponential kinetic processes. Sensitivity of metallated protein to exogenously added chelator decreases with time, consistent with annealing of an initially formed metalloprotein complex
Manganese
-
less than 0.1 mol per mol of subunit
Manganese
-
manganese-superoxide dismutase, MnSOD, encoded by gene sodA
Manganese
-
mitochondrial localization is essential for insertion of manganese to protein. Insertion is only possible with a newly synthesized polypeptide and seems to be driven by the protein unfolding process associated with mitochondrial import
Manganese
putatively coordinated by H27, H81, D167, H171
Mg2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mg2+
-
up to 48% activation
Mg2+
-
73% stimulation of activity
Mn
manganese superoxide dismutase
Mn
-
cognate metal ions Mn, Fe, and Co can effectively occupy the metal site of superoxide dismutase, respectively. MnSOD exhibits the highest SOD activity of 8600 U/mg, while Fe-sub-MnSOD shows only 800 U/mg, and Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD
Mn
manganese superoxide dismutase
Mn
cytosolic MnSOD isozymes, Mn binding sequence is DVWHHAYY
Mn
mitochondrial MnSOD isozymes, Mn binding sequence is DVWHHAYY
Mn
manganese superoxide dismutase
Mn
-
the recombinant SOD binds either Fe or Mn as a metal co-factor, with a consistent preference for Fe accommodation. But differently from the significant preference for Fe displays by the enzyme in the binding reaction, its Mn-form is 71fold more active compared to the Fe-form
Mn
a manganese superoxide dismutase, contains 0.00246 mg Mn/mg protein, binding involves conserved residues H88, H136, D222, and H226
Mn2+
-
0.5 mol per mol of subunit
Mn2+
presence of 0.25 Fe atom and 0.01 Mn atom per monomer of protein
Mn2+
the SOD is active with Fe2+ and Mn2+, Mn2+ activates 20fold, binding structure, overview
Mn2+
the enzyme contains both Mn and Fe. It is cambialistic, i.e. active with either Fe2+ or Mn2+. The specific activities were 906 U/mg with Mn2+ and 175 U/mg with Fe2+
Mn2+
the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Mn-reconstituted enzyme contains 0.82 atom of manganese per subunit
Mn2+
isozyme MnSOD2, encoded by gene sodA-2
Mn2+
Mn-SOD isozyme MnSOD1, encoded by gene sodA-1, MnSOD1 is expressed at lower level compared to MnSOD2
Mn2+
a Mn-superoxide dismutase, conserved manganese-binding site residues are H28, H83, D165, and H169
Mn2+
-
1.1 mol per mol of enzyme
Mn2+
-
0.05 mol per mol of enzyme
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
Mn2+
0.9 Mn per mol of enzyme
Mn2+
-
0.89 mol per mol of liver Mn-SOD
Mn2+
-
1 atom per subunit
Mn2+
a MnSOD, Cherax quadricarinatus mtMnSOD contains a manganese superoxide dismutase domain (DVWEHAYY) from 180-187, and four conserved amino acids responsible for binding manganese (His48, His96, Asp180, and His184)
Mn2+
-
contains no manganese
Mn2+
-
the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
Mn2+
-
MnSOD, the Mn ion is the only metal cofactor, 0.57 atom per polypeptide chain
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
a Mn-SOD, Mn2+ activates, the manganese-binding site is formed by conserved residues His260, His308, Asp392, and His396
Mn2+
a Mn-SOD, Mn2+ activate the enzyme at 1 mM, the manganese-binding sites are conserved in the sequence involving residues His260, His308, Asp392, and His396
Mn2+
-
0.22 mol per mol of enzyme
Mn2+
-
2.2 mol per mol of enzyme
Mn2+
-
1.5 mol per mol of enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
a MnSOD, activates, binding sequence is DVWEHAYY
Mn2+
-
1 atom per subunit
Mn2+
-
less than 0.2 mol per mol of enzyme
Mn2+
-
a Fe,Mn-SOD, the purified enzyme contains 0.7 g-atom of Mn per mol enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
a cambialistic Fe/Mn-superoxide dismutase, 1.12 g-atom per mol of enzyme
Mn2+
-
1.7 mol per mol of enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
0.5 mol per mol of subunit
Mn2+
-
1.22 mol per mol of enzyme
Mn2+
a manganese-containing superoxide dismutase
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
a Mn-SOD, Mn2+ constitutes 0.13% of the enzyme, equivalent to one manganese atom per molecule of enzyme
Mn2+
-
accepts iron and/or manganese as cofactor
Mn2+
-
manganese-SOD variant
Mn2+
-
1.1 mol per mol of enzyme
Mn2+
the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95°C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity
Mn2+
native enzyme from aerobically-grown cells grown in standard medium contains 0.55 mol Mn2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with manganese contains 0.86 mol Mn2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with iron contains 0.68 mol Mn2+ per mol of subunit. Native enzyme from anaerobically-grown cells grown in standard medium contains 0.08 mol Mn2+ per mol of subunit. Recombinant apoenzyme contains less than 0.01 mol Mn2+ per m,ol of subunit. Mn2+-reconstituted recombinant enzyme contains 0.86 mol Mn2+ per mol of subunit. Fe2+-reconstituted recombinant enzyme contains less than 0.01 mol Mn2+ per mol of subunit.The recombinant protein has little activity due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn2+ or Fe2+ yields a highly active protein
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
Mn2+
-
3.69 mol per mol of enzyme
Mn2+
activates the enzyme at 1 mM
Mn2+
-
1 atom per subunit
Mn2+
-
4 mol per mol of enzyme
Mn2+
-
0.75 mol per mol of subunit
Mn2+
-
accepts iron and/or manganese as cofactor
Mn2+
-
isoform I, 1.85 atoms manganese per mol of enzyme
Mn2+
Fe/Mn-type SOD, the Mn-type enzyme contains Gly85
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
Thermochaetoides thermophila
-
0.00205 mg/mg of protein
Mn2+
Thermochaetoides thermophila
manganese superoxide dismutase
Mn2+
-
2 atoms of manganese per molecule
Mn2+
a cambialistic Mn/Fe-SOD
Mn2+
-
2 atoms of manganese per molecule
Mn2+
-
activates by 12% at 10 mM, Mn-containing superoxide dismutase
Mn2+
a Mn-SOD, wild-type specificity, and mutant H84A
Mn2+
-
isozyme SODI is a Mn-SOD
Mn2+
-
1.22 mol per mol of enzyme
Zinc
-
-
Zinc
1.02 mol per mol of subunit
Zinc
recombinant enzyme, 0.51 mol per mol of subunit, native enzyme, 1.01 mol per mol of subunit
Zinc
-
wild-type, 1.08 atoms per subunit, mutant H43R, 1.11, mutant A4V, 1.43 atoms per subunit
Zinc
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
Zinc
-
0.5 atoms per subunit
Zinc
Radix lethospermi
-
-
Zn
extracellular CuZnSOD
Zn
-
in solution, 1 mol per mol of protein. In crystal, a second Zn is bound at the interface between the two enzyme molecules leading to the formation of covalently bound enzyme dimers
Zn
-
a Cu/Zn superoxide dismutase
Zn
-
a Cu,Zn superoxide dismutase
Zn2+
a Cu/ZnSOD, highly conserved amino acid residues are involved in Cu/Zn binding
Zn2+
-
0.2 mol of Cu per mol of enzyme
Zn2+
-
0.6-0.7 mol per mol of enzyme
Zn2+
7 isozymes of CuZnSOD
Zn2+
a CuZn-superoxide dismutase
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
Zn2+
-
1.3 mol per mol of Cu,Zn-SOD
Zn2+
a CuZnSOD, Cherax quadricarinatus ecCuZnSOD contains a Zn signature from 155 to 166 (GNAGQRSGCGII) and four Zn binding sites (His 78, 86, and 95, and Asp 98)
Zn2+
-
1.0 gatom per mol of enzyme
Zn2+
a CuZn-superoxide dismutase
Zn2+
-
an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His63, His71, His80, and Asp83 for Zn2+ binding
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.85 mol per mol of enzyme
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
-
a Cu,Zn-superoxide dismutase
Zn2+
-
2.2 mol per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.5 mol per mol of enzyme
Zn2+
-
0.5 mol per mol of enzyme
Zn2+
-
1.6 mol per mol of enzyme
Zn2+
-
extracellular EC-SOD with Cu,Zn-SOD activity
Zn2+
a Cu,ZnSOD with 1.18 Zn2+ per enzyme subunit, binding structure, overview
Zn2+
a CuZn-superoxide dismutase
Zn2+
a Cu/Zn-SOD, the enzyme contains 1.71 mg/l zinc atoms, 0.258 mol Zn2+ per mol of enzyme
Zn2+
isozyme Cu/Zn-SOD, the highly conserved histidine residues H47, H49, H64, H72, H81, and H121 are involved in the interaction with the metallic cofactors, which are essential for activity and folding in all the Sod1 enzymes
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.2 mol of Cu per mol of enzyme
Zn2+
a Cu,Zn-superoxide dismutase
Zn2+
a Cu,Zn-superoxide dismutase
Zn2+
a Cu,Zn-superoxide dismutase, residues H63, H71, H80, and D83 are involved in Zn2+ binding
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
0.6-0.7 mol per mol of enzyme
Zn2+
-
mitochondrial cyanide-sensitive enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.2 mol per mol of enzyme
Zn2+
a Cu/ZnSOD, the enzyme sequence harbors two Cu/ZnSOD signatures and seven metal liganding residues
Zn2+
a Cu/Zn-superoxide dismutase
Zn2+
-
a Cu/Zn-SOD, conserved amino acids required for binding copper and zinc
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
a CuZn-superoxide dismutase, the prosthetic copper and zinc are essential component of CuZn-SODs, 1.6 Zn2+ per enzyme dimer
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
activates the enzyme at 1 mM
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
1.34-1.81 mol per mol of isoenzyme I
Zn2+
-
1.9-20.0 mol per mol of isoenzyme II
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
a CuZn-superoxide dismutase
Zn2+
-
activates slightly at 0.5-1.0 mM
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
Zn2+
Thermochaetoides thermophila
a CuZn-superoxide dismutase
Zn2+
-
1.0 gatom per mol of enzyme
Zn2+
-
activates by 48% at 10 mM
Zn2+
a Cu/Zn SOD, 0.41 ng atom Zn per mg protein
Zn2+
-
SOD-1, SOD-2 and SOD-4
additional information
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the native forms of SODAp and NTD-fused N-terminal domain ntdSODAp prefer binding Fe2+ over Mn2+ (about 10fold) but contain low ion amounts in each monomer, respectively
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enzyme affinities for copper, zinc, and nickel, overview
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enzyme affinities for copper, zinc, and nickel, overview
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presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals a 1/1 molar ratio (metal/protein) for Cu and Zn, without significant amounts of Fe, Mn or Ni
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presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals a 1/1 molar ratio (metal/protein) for Cu and Zn, without significant amounts of Fe, Mn or Ni
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presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals for SODI molar ratios (metal/protein) for Cu = 0.7 and Zn = 0.4, and for Mn = 0.16
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presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals for SODI molar ratios (metal/protein) for Cu = 0.7 and Zn = 0.4, and for Mn = 0.16
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
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the enzyme contains 7 metal binding sites
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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relevance of the zinc imidazolate bond to the redox properties
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overview: metal content
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role of copper and zinc in protein conformation and activity
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Cu2+ and Zn2+ binding sites are very close to each other
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Cu2+-binding site
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quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
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Mn-SOD contains as well Fe3+, but is only active with manganese
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Mn-SOD contains as well Fe3+, but is only active with manganese
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
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overview: metal content
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Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD
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the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion. Molecular mechanism and structural basis of the metal specificity, preparation of Mn-superoxide dismutase, Fe-Mn-superoxide dismutase, and Co-Mn-superoxide dismutase, the cognate metal characters tuned by the metal microenvironment dominate the metal specificity of the enzyme, overview. The H-bond between Gln178 and Tyr64 in Mn-superoxide dismutase is stronger than that in Fe-Mn-superoxide dismutase, while the coupling between Gln178 and the coordinated solvent of Mn-superoxide dismutase is weaker than that of Fe-Mn-superoxide dismutase. In the oxidized Fe-Mn-superoxide dismutase, tight coupling between Gln178 and the coordination hydroxyl may reduce its redox potential and thus impact its catalytic activity
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no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
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no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
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no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
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no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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overview: metal content
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overview: metal content
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no enzyme activity with Fe2+-reconstituted enzyme
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the Fe2+-reconstituted SOD is inactive
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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overview: metal content
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overview: metal content
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
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Cu2+ is not necessarily required
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
additional information
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
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the enzyme contains no iron
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added Zn2+ and Cu2+ do not affect the enzyme activity or structure
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added Zn2+ and Cu2+ do not affect the enzyme activity or structure
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the enzyme contains 6 metal binding sites
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the enzyme contains no copper, zinc, or manganese
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the enzyme contains no copper, zinc, or manganese
additional information
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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overview: metal content
additional information
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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overview: metal content
additional information
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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overview: metal content
additional information
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
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overview: metal content
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overview: metal content
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no evidence for the presence of either iron or copper/zinc SODs in Phytophthora cinnamomi
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measurement of Cu and Zn content of PschSOD by ICP-MS, zincon, and bathocuproeine protocols
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measurement of Cu and Zn content of PschSOD by ICP-MS, zincon, and bathocuproeine protocols
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exposure to a pH of 3.8 in the presence of 8.0 M urea labilizes the manganese and allows the preparation of a colorless and inactive apoenzyme, that can be reconstituted by subsequent treatment with MnCl2
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metal content of the enzyme depends on the growth condition: anaerobic culture condition promote a higher Fe-content, aerobic conditions promote a higher Mn-content
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protein contains no manganese
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protein contains no manganese
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no effect: Cu2+, Co2+, Ca2+
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metal content analysis of the recombinant enzyme
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metal content analysis of the recombinant enzyme
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
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no effect: Cu2+, Ca2+
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no effect on enzyme activity by Cu2+ at 0.1-5 mM
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different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD
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Thermochaetoides thermophila
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the purified enzyme contains no Fe
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enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
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overview: metal content
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Zn, Ni, and Fe contents of the His29Ala enzyme mutant are 180, 76, and 300 ng/mg, respectively, and the amount of Fe is almost twice that of Zn and fourtimes that of Ni, suggesting that His29Ala mainly is a Fe-SOD. Metal binding trutcure involving residues His29 and His171, overview
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iron, manganese, and nickel contents are below the detection level
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iron, manganese, and nickel contents are below the detection level
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binding ligands: His27, His74, Asp157 and His161 in SodB
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binding ligands: His27, His74, Asp157 and His161 in SodB
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binding ligands: His27, His74, Asp157 and His161 in SodB
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binding ligands: His27, His74, Asp157 and His161 in SodB
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binding ligands: His27, His82, Asp169 and His173 in SodA
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binding ligands: His27, His82, Asp169 and His173 in SodA
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binding ligands: His27, His82, Asp169 and His173 in SodA
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binding ligands: His27, His82, Asp169 and His173 in SodA