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Ligand O2-

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

non-pathway related

KEGG

Alzheimer disease, Amyotrophic lateral sclerosis, Central carbon metabolism in cancer, Chemical carcinogenesis - reactive oxygen species, Coronavirus disease - COVID-19, Diabetic cardiomyopathy, Fluid shear stress and atherosclerosis, Hepatocellular carcinoma, HIF-1 signaling pathway, Lipid and atherosclerosis, Longevity regulating pathway - worm, Neutrophil extracellular trap formation, Parkinson disease, Pathways in cancer, Pathways of neurodegeneration - multiple diseases, Plant-pathogen interaction, Prion disease, Type I diabetes mellitus more

MetaCyc

ethene biosynthesis III (microbes), protein S-nitrosylation and denitrosylation, reactive oxygen species degradation, superoxide radicals degradation

Show all BRENDA pathways known for O2-

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Natural Substrate (15 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.17

superoxide + Fe2+ = O2 + Fe3+

757128

-

1.13.11.52

L-tryptophan + O2- = N-formyl-L-kynurenine

395466

-

1.15.1.1

2 O2.- + 2 H+ + = O2 + H2O2

714933, 715677, 715260, 716197, 714989

-

1.15.1.1

2 O2.- + 2 H+ = O2 + H2O2

704979, 677652, 705498, 704820, 438185, 702845, 727297, 703778, 703779, 701534, 726922, 727097, 727639, 728111, 681370

-

1.15.1.1

2 superoxide + 2 H+ = O2 + H2O2

744500, 745523, 744390, 745763, 744281, 745093, 744963, 745015, 745088, 744564, 745137, 745653, 745059, 744464, 746277, 744591, 745116, 745228, 745226, 746055, 744601, 746564, 744066, 744065, 744746, 745774, 746334, 746337, 746336, 746551, 725344

-

1.15.1.1

O2- + H+ = O2 + H2O2

438096, 438097, 438110, 438185, 438109, 438171

-

1.15.1.1

O2.- + H+ = O2 + H2O2

685881, 685851, 688736, 685900, 687265, 690078, 688722, 688985, 684757, 685651, 688168, 688914, 688841, 684623, 685124, 688384, 688077, 685390, 689984, 687161, 685211, 687789, 685849, 687311, 686786, 673992, 685864, 684538, 684936, 684416, 688805, 688844, 686615, 685382, 687064

-

1.15.1.2

reduced desulforedoxin + superoxide + 2 H+ = desulforedoxin + H2O2

726902, 727313

-

1.15.1.2

reduced rubredoxin + superoxide + 2 H+ = rubredoxin + H2O2

727572, 714326, 726902, 727313, 726989, 714327, 715670, 723459, 721334, 727470

-

1.15.1.2

reduced rubredoxin + superoxide + H+ = oxidized rubredoxin + H2O2

390148, 390159, 390152

-

1.15.1.2

reduced rubredoxin + superoxide + H+ = rubredoxin + H2O2

686522, 686523, 685089, 687278, 674937, 684111, 686751, 687820, 687582

-

1.15.1.2

superoxide + reduced acceptor + 2 H+ = H2O2 + oxidized acceptor

744687, 746425, 743942

-

1.15.1.2

superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin

744022

-

1.15.1.1

5 entries

1.15.1.2

6 entries

1.17.1.4

hypoxanthine + NAD+ + H+ + O2- + H2O = xanthine + NADH + H2O2

644606, 644610, 644611, 644604, 644614, 644599, 644608, 644574, 644573, 644575, 644609, 644561

-

1.8.3.7

a [sulfatase]-L-cysteine + O(2) + a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O

741508, 742234

-

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.17

2 O2 + ubiquinol = 2 superoxide + ubiquinone + 2 H+

0

-

1.17.1.4

NADPH + O2 = NADP+ + O2- + H+

644566

-

1.17.1.4

xanthine + O2 + H2O = urate + O2- + 2 H+

644582, 644615, 644578, 644584, 644598, 644567, 644587, 644594, 644603, 644580, 644586, 644593, 644592, 644570, 644579, 644589, 644581, 644574, 644562, 644597, 644591, 644600, 644588

-

1.17.1.4

2 entries

1.6.3.1

NADPH + O2 = NADP+ + O2-

394275, 394273, 394274, 0

-

Substrate in Enzyme-catalyzed Reactions (30 results)

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Show Substrate (30 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.17

superoxide + Fe2+ = O2 + Fe3+

757128

-

1.10.3.17

superoxide + ubiquinone Q2 + H+ = O2 + ubiquinol Q2

757739

-

1.10.3.17

2 entries

1.11.2.2

serotonin + superoxide = tryptamine-4,5-dione + H2O

711135

-

1.13.11.52

3-indoleethanol + O2- = ?

665459

-

1.13.11.52

5-hydroxytryptophan + O2- = N-formyl-5-hydroxykynurenine

665454

-

1.13.11.52

alpha-methyl-DL-tryptophan + O2- = ?

665459

-

1.13.11.52

indole + O2- = ?

665459

-

1.13.11.52

L-tryptophan + O2- = N-formyl-L-kynurenine

395466, 665454, 665459

-

1.13.11.52

serotonin + O2- = ?

665454

-

1.13.11.52

tryptamine + O2- = ?

665454

-

1.15.1.1

2 O2.- + 2 H+ + = O2 + H2O2

714933, 715677, 715260, 716197, 714989

-

1.15.1.1

2 O2.- + 2 H+ = O2 + H2O2

704979, 677652, 705498, 704820, 438185, 702845, 727297, 719516, 703778, 703779, 701534, 726922, 727097, 727639, 728111, 681370

-

1.15.1.1

2 superoxide + 2 H+ = O2 + H2O2

744500, 745523, 744390, 745763, 744281, 745093, 744963, 745015, 745088, 744564, 745137, 725344, 745653, 745059, 744464, 746277, 744591, 745116, 745228, 745226, 746055, 744601, 746564, 744066, 744065, 744746, 745774, 746334, 746337, 746336, 746551

-

1.15.1.1

O2- + H+ = O2 + H2O2

438176, 438096, 438114, 438160, 438143, 438144, 438155, 438188, 438110, 438164, 438097, 438137, 438093, 438098, 438099, 438120, 438121, 438128, 438129, 438130, 438174, 438178, 438180, 438186, 673565, 675503, 438175, 438100, 438118, 438131, 438132, 438133, 438095, 438134, 438153, 438154, 438190, 438089, 438122, 438123, 438124, 438125, 438148, 438165, 438182, 438151, 438152, 438166, 438107, 438136, 438145, 438091, 438113, 438135, 438184, 438149, 438150, 438101, 438094, 438167, 438159, 438141, 438181, 438102, 438142, 438106, 438161, 438117, 438157, 438138, 438140, 438108, 438158, 438104, 438116, 438185, 672386, 438147, 438156, 438105, 438119, 438111, 438168, 659402, 438177, 438187, 674025, 438191, 438092, 438112, 438090, 658669, 658667, 659841, 438146, 438163, 438169, 438139, 438162, 660490, 438170, 438103, 438109, 438115, 438172, 438173, 438179, 672303, 659568, 659042, 676294, 673154, 673161, 676948, 438171, 438183, 438189, 672442, 438126, 438127

-

1.15.1.1

O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate = ?

684538

-

1.15.1.1

O2.- + H+ = O2 + H2O2

685849, 685864, 685881, 687789, 685382, 685851, 688736, 684936, 685900, 686615, 687064, 687161, 684416, 684538, 687265, 687311, 690078, 688722, 685390, 688985, 685211, 684757, 688844, 673992, 685651, 686786, 688168, 688914, 688805, 689984, 688841, 684623, 685124, 688384, 688077

-

1.15.1.2

reduced acceptor + superoxide + H+ = acceptor + H2O2

390151

-

1.15.1.2

reduced acceptor + superoxide = acceptor + H2O2 + O2

390151

-

1.15.1.2

reduced cytochrome c + superoxide + 2 H+ = oxidized cytochrome c + H2O2

727470

-

1.15.1.2

reduced cytochrome c + superoxide + H+ = cytochrome c + H2O2

390148, 390159, 390149, 390150

-

1.15.1.2

reduced desulforedoxin + superoxide + 2 H+ = desulforedoxin + H2O2

726902, 727313

-

1.15.1.2

reduced rubredoxin + superoxide + 2 H+ = oxidized rubredoxin + H2O2

727470

-

1.15.1.2

reduced rubredoxin + superoxide + 2 H+ = rubredoxin + H2O2

721334, 727572, 714326, 726902, 727313, 726989, 714327, 715670, 723459, 687582, 727470

-

1.15.1.2

reduced rubredoxin + superoxide + H+ = oxidized rubredoxin + H2O2

390148, 390159, 390152

-

1.15.1.2

reduced rubredoxin + superoxide + H+ = rubredoxin + H2O2

686522, 390159, 686523, 390154, 685089, 687820, 687278, 674937, 684111, 390148, 657785, 686751, 687582

-

1.15.1.2

superoxide + reduced acceptor + 2 H+ = H2O2 + oxidized acceptor

744687, 746425, 743942

-

1.15.1.2

superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin

744022

-

1.13.11.52

7 entries

1.15.1.1

6 entries

1.15.1.2

11 entries

1.17.1.4

hypoxanthine + NAD+ + H+ + O2- + H2O = xanthine + NADH + H2O2

644606, 644610, 644611, 674374, 644604, 644614, 644599, 644608, 644574, 644573, 644575, 644609, 644561, 659210, 659314

-

1.7.2.1

O2-. + H+ = H2O2 + O2

644779

-

1.8.3.7

a [sulfatase]-L-cysteine + O(2) + a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O

741508, 742234

-

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.2.3

L-lactate + O2 = ? + superoxide anion

0

-

1.10.3.17

2 O2 + ubiquinol = 2 superoxide + ubiquinone + 2 H+

0

-

1.17.1.4

hypoxanthine + O2 + H2O = xanthine + O2-

0

-

1.17.1.4

NADH + O2 + H+ = NAD+ + O2- + H2O2

0

-

1.17.1.4

NADPH + O2 = NADP+ + O2- + H+

644566

-

1.17.1.4

xanthine + O2 + H2O = urate + O2- + 2 H+

644582, 644615, 644578, 644584, 644598, 644567, 644587, 644594, 644603, 644580, 644586, 0, 644593, 644592, 644570, 644579, 644589, 644581, 644574, 644562, 644597, 644591, 644600, 644588

-

1.17.1.4

4 entries

1.17.3.2

xanthine + H2O + O2 = superoxide + urate + ?

0

-

1.2.3.14

NADH + O2 = NAD+ + O2-

0

-

1.6.2.4

NADPH + O2 = NADP+ + O2-

288558, 288572

-

1.6.3.1

NADPH + O2 = NADP+ + O2-

394275, 394273, 394274, 0

-

1.8.1.9

paraquat radical + O2 = paraquat + O2-

0

-

7.1.1.2

NADH + O2 = NAD+ + superoxide radical

0, 392696

-

Activator in Enzyme-catalyzed Reactions (4 results)

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Show Activating Compound (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.9

stimulation of O2 uptake

389879

-

1.13.11.11

activation of the enzyme is stimulated by superoxide and H2O2

743358

-

1.13.11.52

-

665204, 395466, 395458

-

1.13.11.52

the enzyme is inactive unless superoxide anion is present, the native ferric form of the enzyme binds to the superoxide anion to form the oxygenated enzyme

395461

-

1.13.11.52

2 entries

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.9

-

396627

-

1.15.1.1

substrate inhibition for mutant C140S/Q143A

673565

-

1.97.1.12

superoxide generated in the chloroplast stroma causes photoinhibition of photosystem I, superoxide accelerates photoinhibition of PSI

745984

-

2.5.1.18

generated by a Fe3+/ascorbate system, inhibits cytosolic GSTs and microsomal GSTs by 30% and 65%, respectively. Addition of 2 mM DTT fails to completely reverse microsomal GST inhibition elicited by Fe3+/ascorbate, recovering only about 10% of this activity, but it completely reverses the inhibitory effect of Fe3+/ascorbate on cytosolic GST activity

702529

-

2.5.1.54

displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide. Superoxide stress promotes the mismetallation of DAHP synthase

738530

-

3.4.22.36

superoxide production decreases the cellular redox potential and specifically inhibites caspase-1 by reversible oxidation and glutathionylation of the redox-sensitive cysteine residues Cys397 and Cys362

700365

-

3.6.1.6

GDPase activity significantly decreases at high concentrations

756751

-

4.2.1.12

-

33652

-

4.2.1.12

the O2--sensitive target site is proposed to be an iron-sulfur cluster which is readily destroyed by oxidation

33658

-

4.2.1.12

2 entries

4.2.1.130

sensitivity of glyoxalase III is special and might relate to the thiol group that is essential for its activity and possibly to the binding of iron adjacent to the active site thiol

715449

-

4.2.1.3

-

696168

-

4.6.1.2

-

34862, 691656

-

7.2.2.13

-

675473

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

7.1.1.9

7au3, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.15.1.1

1100

-

pH 7.5, 25°C, mutant Y34F with fluorinated Tyr-residues

675503

1.15.1.1

3300

-

pH 7.5, 25°C, mutant Y34F

675503

1.15.1.1

4600

-

pH 7.5, 25°C, wild-type with fluorinated Tyr-residues

675503

1.15.1.1

40000

-

pH 7.5, 25°C, wild-type

675503

1.15.1.1

100000

-

-

438122

1.15.1.1

107000

-

pH 8.2, 22°C

745088

1.15.1.1

6 entries

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.15.1.1

0.0115

-

pH 8.2, 22°C

745088

1.15.1.1

0.355

-

-

438122

1.15.1.1

2 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.15.1.1

0.06

-

mutant C140S/Q143A, pH 9.0, 25°C

673565

References & Links

Literature References (308)

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Show Reference (308 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

33652

8728108

6-Phosphogluconate dehydratase from Zymomonas mobilis: an iron-sulfur-manganese enzyme

1996

Rodriguez, M.; Wedd, A.G.; Scopes, R.K.

Biochem. Mol. Biol. Int.

39

783-789

33658

1846355

Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase

1991

Gardner, P.R.; Fridovich, I.

J. Biol. Chem.

266

1478-1483

34862

1976516

Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion

1990

Bruene, B.; Schmidt, K.U.; Ullrich, V.

Eur. J. Biochem.

192

683-688

288558

6094521

Purification and characterization of a membrane-bound NADPH-cytochrome c reductase capable of catalyzing menadione-dependent O2- formation in guinea pig polymorphonuclear leukocytes

1984

Sakane, F.; Takahashi, K.; Koyama, J.

J. Biochem.

96

671-678

288572

14931

Studies on the microsomal electron-transport system of anaerobically grown yeast. V. Purification and characterization of NADPH-cytochrome c reductase

1977

Kubota, S.; Yoshida, Y.; Kumaoka, H.; Furumichi, A.

J. Biochem.

81

197-205

389879

-

Trivalent copper, superoxide, and galactose oxidase

1978

Hamilton, G.A.; Adolf, P.K.; de Jersey, J.; DuBois, G.C.; Dyrkacz, G.R.; Libby, R.D.

J. Am. Chem. Soc.

100

1899-1912

390148

10514376

Anaerobic microbes: oxygen detoxification without superoxide dismutase

1999

Jenney, F.E., Jr.; Verhagen, M.F.J.M.; Cui, X.; Adams, M.W.W.

Science

286

306-309

390149

10874033

Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase

2000

Jovanovic, T.; Ascenso, C.; Hazlett, K.R.O.; Sikkink, R.; Krebs, C.; Litwiller, R.; Benson, L.M.; Moura, I.; Moura, J.J.G.; Radolf, J.D.; Huynh, B.H.; Naylor, S.; Rusnak, F.

J. Biol. Chem.

275

28439-28448

390150

10617593

Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity

2000

Lombard, M.; Fontecave, M.; Touati, D.; Niviere, V.

J. Biol. Chem.

275

115-121

390151

11069658

Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by Neelaredoxin

2000

Abreu, I.A.; Saraiva, L.M.; Carita, J.; Huber, H.; Stetter, K.O.; Cabelli, D.; Teixeira, M.

Mol. Microbiol.

38

322-334

390152

10704199

Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states

2000

Yeh, A.P.; Hu, Y.; Jenney, F.E., Jr.; Adams, M.W.W.; Rees, D.C.

Biochemistry

39

2499-2508

390154

11566030

A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase

2001

Coulter, E.D.; Kurtz, D.M., Jr.

Arch. Biochem. Biophys.

394

76-86

390159

11912914

Superoxide reductase activities of neelaredoxin and desulfoferrodoxin metalloproteins

2002

Rusnak, F.; Ascenso, C.; Moura, I.; Moura, J.J.G.

Methods Enzymol.

349

243-258

392696

11863445

Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization

2002

Fang, J.; Beattie, D.S.

Biochemistry

41

3065-3072

394273

8382922

Polyene antibiotics inhibit superoxide-producing NADPH oxidase in a polymorphonuclear cell-free system

1993

Capuozzo, E.; Crifo, C.; Salerno, C.

Biochem. Pharmacol.

45

766-768

394274

8088410

Prostaglandin E1 and analogs of prostacyclin influencing superoxide production by the human neutrophil NADPH oxidase system

1994

Umeki, S.

Int. J. Biochem.

26

1003-1008

394275

8038232

Mechanisms for the activation/electron transfer of neutrophil NADPH-oxidase complex and molecular pathology of chronic granulomatous disease

1994

Umeki, S.

Ann. Hematol.

68

267-277

395458

2536368

The roles of superoxide anion and methylene blue in the reductive activation of indoleamine 2,3-dioxygenase by ascorbic acid or by xanthine oxidase-hypoxanthine

1989

Sono, M.

J. Biol. Chem.

264

1616-1622

395461

6203011

Overview: superoxygenase

1984

Yoshida, R.; Hayaishi, O.

Methods Enzymol.

105

61-70

395466

10719243

Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway

2000

Dang, Y.; Dale, W.E.; Brown, O.R.

Free Radic. Biol. Med.

28

615-624

396627

-

The selenoprotein glutathione peroxidase

1989

Flohe, L.

Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York

-

643-731

438089

4324341

Further characterization of bovine superoxide dismutase and its isolation from bovine heart

1971

Keele, B.B.; McCord, J.M.; Fridovich, I.

J. Biol. Chem.

246

2875-2880

438090

4559499

Superoxide dismutase from Streptococcus mutans. Isolation and characterization of two forms of the enzyme

1972

Vance, P.G.; Keele, B.B.; Rajagopalan, K.V.

J. Biol. Chem.

247

4782-4786

438091

4337330

Preparation and physicochemical properties of green pea superoxide dismutase

1972

Sawada, Y.; Ohyama, T.; Yamazaki, I.

Biochim. Biophys. Acta

268

305-312

438092

2226833

The primary structure of superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis

1990

Amano, A.; Shizukuishi, S.; Tsunemitsu, A.; Maekawa, K.; Tsunasawa, S.

FEBS Lett.

272

217-220

438093

2738919

Characterization of crystals of genetically engineered human manganese superoxide dismutase

1989

Wagner, U.G.; Werber, M.M.; Beck, Y.; Hartman, J.R.; Frolow, F.; Sussman, J.L.

J. Mol. Biol.

206

787-788

438094

2325128

Crystallographic characterization of a Cu,Zn superoxide dismutase from Photobacterium leiognathi

1990

Redford, S.M.; McRee, D.E.; Getzoff, E.D.; Steinman, H.M.; Tainer, J.A.

J. Mol. Biol.

212

449-451

438095

2655595

Crystallographic characterization and three-dimensional model of yeast Cu,Zn superoxide dismutase

1989

Frigerio, F.; Falconi, M.; Gatti, G.; Bolognesi, M.; Desideri, A.; Marmocchi, F.; Rotilio, G.

Biochem. Biophys. Res. Commun.

160

677-681

438096

1851570

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1978

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Iron-containing superoxide dismutase from Crithidia fasciculata. Purification, characterization, and similarity to Leishmanial and trypanosomal enzymes

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The purification and properties of superoxide dismutase from a blue-green alga

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Cobalt erythrocuprein: preparation and properties

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Purification and physicochemical properties of superoxide dismutase from two photosynthetic microorganisms

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Purification, crystallization and properties of iron-containing superoxide dismutase from Pseudomonas ovalis

1976

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Isolation and characterization of the iron-containing superoxide dismutase of Methanobacterium bryantii

1981

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Purification of the cytosolic CuZn-superoxide dismutase (CuZn-SOD) of Marchantia paleacea var. diptera and its resemblance to CuZn-SOD from chloroplasts

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Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells

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Mol. Cells

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cDNA cloning, high-level expression, purification, and characterization of an avian Cu,Zn superoxide dismutase from Peking duck

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Purification and characterization of canine manganese superoxide dismutase and its immunohistochemical localization in canine heart compared with that of copper-zinc superoxide dismutase

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Int. J. Biochem. Cell Biol.

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The Cu,Zn superoxide dismutases of Aspergillus flavus, Aspergillus niger, Aspergillus nidulans, and Aspergillus terreus: purification and biochemical comparison with the Aspergillus fumigatus Cu,Zn superoxide dismutase

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Infect. Immun.

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Structural studies of an eukaryotic cambialistic superoxide dismutase purified from the mature seeds of camphor tree

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Peroxisomal manganese superoxide dismutase: purification and properties of the isoenzyme from pea leaves

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A superoxide dismutase from the archaeon Sulfolobus solfataricus is an extracellular enzyme and prevents the deactivation by superoxide of cell-bound proteins

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Mutation of the metal-bridging proton-donor His63 residue in human copper, zinc superoxide dismutase. Biochemical and biophysical analysis of the His63-Cys mutant

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Purification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas

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Characterization of an atypical superoxide dismutase from Sinorhizobium meliloti

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Copper/zinc-superoxide dismutase from lemon cDNA and enzyme stability

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Characterization of recombinant Saccharomyces cerevisiae manganese-containing superoxide dismutase and its H30A and K170R mutants expressed in Escherichia coli

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Tobacco nectarin I. Purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues

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Selenium-containing xanthine dehydrogenase from Eubacterium barkeri

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Cloning and partial characterization of the xanthine dehydrogenase gene of Calliphora vicina, a distant relative of Drosophila melanogaster

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