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reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
blue non-heme iron enzyme that functions in anaerobic microbes as a defense mechanism against reactive oxygen species by catalyzing the reduction of superoxide to H2O2
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reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
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reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
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rubredoxin is assumed to be the physiological electron carrier
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reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
additional information
?
-
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
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?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
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-
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-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
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?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
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reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
functionally important residues are Glu14, Lys15, His16, His41, His51, His118, Ile49, and Cys111, mechanistic aspects of biological superoxide anion reduction, overview
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reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
SOR is a non-heme iron enzyme that reduces superoxide to peroxide at a diffusion-controlled rate, thiolate acts as a covalent anionic ligand. Replacing the thiolate with a neutral noncovalent ligand makes protonation very endothermic and greatly raises the reduction potential,overview
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reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
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reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
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?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
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?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
superoxide reductase mediates reduction of superoxide to hydrogen peroxide in an NADPH-dependent manner via a coupled reaction between NAD(P)H:rubredoxin oxidoreductase, rubredoxin, and superoxide reductase
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reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
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reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
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rubredoxin is assumed to be the physiological electron carrier
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?
additional information
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comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
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additional information
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structure-function relationship, overview
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additional information
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nitric oxide is used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus superoxide reductase through the use of EPR, resonance Raman, Fourier transform IR, UV-visible absorption, and variabletemperature variable-field magnetic CD spectroscopies
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additional information
?
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nitric oxide is used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus superoxide reductase through the use of EPR, resonance Raman, Fourier transform IR, UV-visible absorption, and variabletemperature variable-field magnetic CD spectroscopies
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Fe2+/Fe3+
each subunit contains a single mononuclear non-heme iron center
Iron
1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant. The electrostatic surface close to center II has a positive character, mainly due to the metal ion and to residue Lys 15 of 1Fe-SOR, metal site structure and mechanism, overview
Iron
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resonance Raman characterization of the mononuclear iron active-site
additional information
binding of synthetic iron ligand complexes, overview
Fe2+
1Fe SOR is a non-heme iron enzyme, iron binding and reaction mechanism, detailed overview
Fe2+
complex formation, kinetics, and electrochemistry, overview
Fe2+
the class II enzyme contains one iron-center, iron ligands Glu14, His47 and His114 in addition to adjacent residues Trp11, Ile39, Pro40, Pro42, Thr44 and Ile113, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+/Fe3+
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Fe2+/Fe3+
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in the oxidized state, the mononuclear ferric active site has a octahedral coordination with four equatorial histidyl ligands and axial cysteinate and monodentate glutamate ligands, in the reduced state the ferrous site has a square-pyramidal coordination geometry in frozen solution with four equatorial histidines and one axial cysteine
Fe2+/Fe3+
-
0.5 iron atoms/mol subunit
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Jenney, F.E., Jr.; Verhagen, M.F.J.M.; Cui, X.; Adams, M.W.W.
Anaerobic microbes: oxygen detoxification without superoxide dismutase
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1999
Pyrococcus furiosus
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Yeh, A.P.; Hu, Y.; Jenney, F.E., Jr.; Adams, M.W.W.; Rees, D.C.
Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states
Biochemistry
39
2499-2508
2000
Pyrococcus furiosus (P82385), Pyrococcus furiosus
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Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism
J. Am. Chem. Soc.
124
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2002
Pyrococcus furiosus
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Rusnak, F.; Ascenso, C.; Moura, I.; Moura, J.J.G.
Superoxide reductase activities of neelaredoxin and desulfoferrodoxin metalloproteins
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2002
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio vulgaris, Pyrococcus furiosus, Treponema pallidum
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Pyrococcus furiosus
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Pereira, A.S.; Tavares, P.; Folgosa, F.; Almeida, R.M.; Moura, I.; Moura, J.J.
Superoxide reductases
Eur. J. Inorg. Chem.
2007
2569-2581
2007
Archaeoglobus fulgidus (O29903), Desulfarculus baarsii (Q46495), Desulfovibrio desulfuricans, Desulfovibrio vulgaris (P20418), Megalodesulfovibrio gigas, Methanothermobacter thermautotrophicus, Pyrococcus furiosus (P82385), Thermotoga maritima (Q9WZC6), Treponema pallidum
-
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Brines, L.M.; Kovacs, J.A.
Understanding the mechanism of superoxide reductase promoted reduction of superoxide
Eur. J. Inorg. Chem.
2007
29-38
2007
Desulfovibrio desulfuricans, Treponema palladium, Pyrococcus furiosus (P82385), Desulfarculus baarsii (Q46495)
-
brenda
Dey, A.; Jenney, F.E.; Adams, M.W.; Johnson, M.K.; Hodgson, K.O.; Hedman, B.; Solomon, E.I.
Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on superoxide reductase: role of the axial thiolate in reactivity
J. Am. Chem. Soc.
129
12418-12431
2007
Pyrococcus furiosus (P82385), Pyrococcus furiosus
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Pinto, A.; Rodrigues, J.; Teixeira, M.
Reductive elimination of superoxide: Structure and mechanism of superoxide reductases
Biochim. Biophys. Acta
1804
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2010
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio desulfuricans (P22076), Desulfovibrio vulgaris, Megalodesulfovibrio gigas, Nanoarchaeum equitans, Pyrococcus furiosus (P82385), Pyrococcus horikoshii (O58810), Pyrococcus horikoshii OT-3 (O58810), Thermotoga maritima (Q9WZC6), Treponema pallidum
brenda
Grunden, A.M.; Jenney, F.E.; Ma, K.; Ji, M.; Weinberg, M.V.; Adams, M.W.
In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus
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71
1522-1530
2005
Pyrococcus furiosus
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Clay, M.D.; Jenney, F.E.; Noh, H.J.; Hagedoorn, P.L.; Adams, M.W.; Johnson, M.K.
Resonance Raman characterization of the mononuclear iron active-site vibrations and putative electron transport pathways in Pyrococcus furiosus superoxide reductase
Biochemistry
41
9833-9841
2002
Pyrococcus furiosus
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Im, Y.J.; Ji, M.; Lee, A.; Killens, R.; Grunden, A.M.; Boss, W.F.
Expression of Pyrococcus furiosus superoxide reductase in Arabidopsis enhances heat tolerance
Plant Physiol.
151
893-904
2009
Pyrococcus furiosus (P82385), Pyrococcus furiosus
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Clay, M.D.; Cosper, C.A.; Jenney, F.E.; Adams, M.W.; Johnson, M.K.
Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase
Proc. Natl. Acad. Sci. USA
100
3796-3801
2003
Pyrococcus furiosus (P82385), Pyrococcus furiosus
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Sheng, Y.; Abreu, I.; Cabelli, D.; Maroney, M.; Miller, A.; Teixeira, M.; Valentine, J.
Superoxide dismutases and superoxide reductases
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114
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Archaeoglobus fulgidus, Archaeoglobus fulgidus (O29903), Archaeoglobus fulgidus ATCC 49558 (O29903), Desulfarculus baarsii (Q46495), Desulfarculus baarsii ATCC 33931 (Q46495), Desulfovibrio desulfuricans, Desulfovibrio vulgaris, Dosidicus gigas, Ignicoccus hospitalis (A8AC72), Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 (A8AC72), Nanoarchaeum equitans (Q74MF3), Pyrococcus furiosus (P82385), Pyrococcus furiosus ATCC 43587 (P82385), Pyrococcus horikoshii (O58810), Thermotoga maritima (Q9WZC6), Thermotoga maritima ATCC 43589 (Q9WZC6), Treponema pallidum (O82795), Treponema pallidum Nichols (O82795)
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