1.15.1.2: superoxide reductase
This is an abbreviated version!
For detailed information about superoxide reductase, go to the full flat file.
Word Map on EC 1.15.1.2
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1.15.1.2
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desulfovibrio
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non-heme
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gigas
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desulfoarculus
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baarsii
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sulfate-reducing
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high-spin
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radiolysis
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rubrerythrin
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hildenborough
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hydroperoxo
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peroxo
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square-pyramidal
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ferric-hydroperoxo
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thiolate-ligated
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rubredoxin-like
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feiii-ooh
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agriculture
- 1.15.1.2
- desulfovibrio
-
non-heme
- gigas
- desulfoarculus
- baarsii
-
sulfate-reducing
-
high-spin
-
radiolysis
- rubrerythrin
- hildenborough
-
hydroperoxo
-
peroxo
-
square-pyramidal
-
ferric-hydroperoxo
-
thiolate-ligated
-
rubredoxin-like
-
feiii-ooh
- agriculture
Reaction
Synonyms
1Fe SOR, 1Fe-SOR, 1Fe-superoxide reductase, 2Fe-SOR, class I SOR, class I superoxide reductase, class II SOR, cytochrome c–superoxide oxidoreductase, desulfoferrodoxin, desulforedoxin, Dfx, EC 1.18.96.1, Fe-SOR, GiSOR, MM_0632, More, neelaredoxin, neelaredoxin-type SOR, Nlr, PfSOR, rubredoxin oxidoreductase, SOR, superoxide reductase, TM0658, two-iron superoxide reductase, Zn/Fe-SOR
ECTree
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KM Value
KM Value on EC 1.15.1.2 - superoxide reductase
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additional information
Megalodesulfovibrio gigas
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steady-state kinetics
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additional information
additional information
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detailed kinetic analysis and comparison of mechanism with 1Fe-SOR isoform neelaredoxin. UV/Vis and EPR-spectral analysis
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additional information
additional information
detailed kinetic analysis and comparison of mechanism with 1Fe-SOR isoform neelaredoxin. UV/Vis and EPR-spectral analysis
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additional information
additional information
Megalodesulfovibrio gigas
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steady-state kinetics, overview
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additional information
additional information
kinetic analysis, binding parameters, and electrochemic parameters of the enzyme and Fe2+ complexes, overview
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additional information
additional information
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kinetic analysis, binding parameters, and electrochemic parameters of the enzyme and Fe2+ complexes, overview
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additional information
additional information
kinetics, resonance Raman spectroscopy
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additional information
additional information
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kinetics, resonance Raman spectroscopy
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additional information
additional information
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rapid kinetics measurements and pH-dependence, stopped-flow kinetics of electron transfer between rubredoxin and desulfoferrodoxin, overview
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additional information
additional information
rapid kinetics measurements and pH-dependence, stopped-flow kinetics of electron transfer between rubredoxin and desulfoferrodoxin, overview
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additional information
additional information
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solvent deuterium isotope effects, stopped-flow kinetics of wild-type and mutant enzymes at different pH in different buffer systems, overview
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additional information
additional information
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the reaction with superoxide proceeds via formation of an intermediate with a second-order rate constant
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additional information
additional information
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kinetic analysis, e.g. kinetics of the formation of the first reaction intermediate T1 adjusted with a biexponential model, overview
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additional information
additional information
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stopped-flow kinetic analysis, overview
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additional information
additional information
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enzyme redox potentials, and stopped-flow kinetics of the reduction of superoxide reductase-Zn(II)-Fe(III) and superoxide reductase-Fe(III)-Fe(III), overview. Smaller reaction rate constants are observed for the superoxide reductase-Fe(III)-Fe(III) and oxidized superoxide reductase-Zn(II)-Fe(III) forms, in both cases centre II has to be reduced prior to the reaction with superoxide radical, leading to a slower initial reaction rate
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