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Volumn 261, Issue 2, 1999, Pages 438-443

The superoxide dismutase activity of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774

Author keywords

Desulfoferrodoxin; Desulfovibrio; Rubredoxin; Superoxide dismutase; Thioredoxin

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; CYANIDE; SUPEROXIDE DISMUTASE; XANTHINE OXIDASE;

EID: 0001473620     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00278.x     Document Type: Article
Times cited : (56)

References (40)
  • 1
    • 0014021901 scopus 로고
    • Dependence of sulphate-reduction on a crystallized ferredoxin from Desulfovibrio gigas
    • 1. Le Gall, J. & Dragoni, N. ( 1966) Dependence of sulphate-reduction on a crystallized ferredoxin from Desulfovibrio gigas. Biochem. Biophys. Res. Commum. 23, 145-149.
    • (1966) Biochem. Biophys. Res. Commum. , vol.23 , pp. 145-149
    • Le Gall, J.1    Dragoni, N.2
  • 2
    • 0015508213 scopus 로고
    • Purification et propriétés d'une rubrédoxine isolée à partir de Desulfovibrio vulgaris (Souche NCIB 8303)
    • 2. Bruschi, M. & Le Gall, J. (1972) Purification et propriétés d'une rubrédoxine isolée à partir de Desulfovibrio vulgaris (Souche NCIB 8303). Biochem. Biophys. Acta 263, 279-282.
    • (1972) Biochem. Biophys. Acta , vol.263 , pp. 279-282
    • Bruschi, M.1    Le Gall, J.2
  • 4
    • 0032537511 scopus 로고    scopus 로고
    • Characterisation of a new rubredoxin isolated from Desulfovibrio desulfuricans 27774: Definition of a new family of rubredoxins
    • 4. Le Gall, J., Liu, M.Y., Gomes, C.M., Braga, V., Pacheco, I., Regalla, M., Xavier, A.V. & Teixeira, M. (1998) Characterisation of a new rubredoxin isolated from Desulfovibrio desulfuricans 27774: definition of a new family of rubredoxins. FEBS Lett. 429, 295-298.
    • (1998) FEBS Lett. , vol.429 , pp. 295-298
    • Le Gall, J.1    Liu, M.Y.2    Gomes, C.M.3    Braga, V.4    Pacheco, I.5    Regalla, M.6    Xavier, A.V.7    Teixeira, M.8
  • 5
    • 0017389657 scopus 로고
    • Isolation and characterization of desulforedoxin a new type of non-heme iron protein from Desulfovibrio gigas
    • 5. Moura, I., Bruschi, M., Le Gall, J., Moura, J.J.G. & Xavier, A.V. (1977) Isolation and characterization of desulforedoxin a new type of non-heme iron protein from Desulfovibrio gigas. Biochem. Biophys. Res. Comm. 75, 1037-1044.
    • (1977) Biochem. Biophys. Res. Comm. , vol.75 , pp. 1037-1044
    • Moura, I.1    Bruschi, M.2    Le Gall, J.3    Moura, J.J.G.4    Xavier, A.V.5
  • 6
    • 0024281294 scopus 로고
    • Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear center
    • 6. Le Gall, J., Prickril, B.C., Moura, I., Xavier, A.V., Moura, J.J.G. & Huynh, B.H. (1988) Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear center. Biochemistry 27, 1636-1642.
    • (1988) Biochemistry , vol.27 , pp. 1636-1642
    • Le Gall, J.1    Prickril, B.C.2    Moura, I.3    Xavier, A.V.4    Moura, J.J.G.5    Huynh, B.H.6
  • 7
    • 0027511224 scopus 로고
    • Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters
    • 7. Pierik, A.J., Wolbert, R.B., Portier, G.L., Verhagen, M.F. & Hagen, W.R. (1993) Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters. Eur. J. Biochem. 212, 237-245.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 237-245
    • Pierik, A.J.1    Wolbert, R.B.2    Portier, G.L.3    Verhagen, M.F.4    Hagen, W.R.5
  • 9
    • 0025678997 scopus 로고
    • Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans ATCC 27774 and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center
    • 9. Moura, I., Tavares, P., Moura, J.J.G., Ravi, N., Huynh, B.H., Liu, M.Y. & Le Gall, J. (1990) Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans ATCC 27774 and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center. J. Biol. Chem. 265, 21596-21602.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21596-21602
    • Moura, I.1    Tavares, P.2    Moura, J.J.G.3    Ravi, N.4    Huynh, B.H.5    Liu, M.Y.6    Le Gall, J.7
  • 11
    • 0029997030 scopus 로고    scopus 로고
    • Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins
    • 11. Devreese, B., Tavares, P., Lampreia, J., Van Damme, N., Le Gall, J., Moura, J.J.G., Van Beeumen, J. & Moura, I. (1996) Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins. FEBS Lett. 385, 138-149.
    • (1996) FEBS Lett. , vol.385 , pp. 138-149
    • Devreese, B.1    Tavares, P.2    Lampreia, J.3    Van Damme, N.4    Le Gall, J.5    Moura, J.J.G.6    Van Beeumen, J.7    Moura, I.8
  • 13
    • 0030015101 scopus 로고    scopus 로고
    • Preliminary crystallographic analysis of the oxidized form of a two mono-nuclear iron centers protein from Desulfovibrio desulfuricans ATCC 27774
    • 13. Coelho, A.V., Matias, P.M., Carrondo, M.A., Tavares, P., Moura, J.J.G., Moura, I., Fülöp, V., Hajdu, J. & Le Gall, J. (1996) Preliminary crystallographic analysis of the oxidized form of a two mono-nuclear iron centers protein from Desulfovibrio desulfuricans ATCC 27774. Protein Sci. 5, 1189-1191.
    • (1996) Protein Sci. , vol.5 , pp. 1189-1191
    • Coelho, A.V.1    Matias, P.M.2    Carrondo, M.A.3    Tavares, P.4    Moura, J.J.G.5    Moura, I.6    Fülöp, V.7    Hajdu, J.8    Le Gall, J.9
  • 15
    • 0029123025 scopus 로고
    • Crystal structure of Desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: A novel non-heme iron protein structure
    • 15. Archer, M., Huber, R., Tavares, P., Moura, I., Moura, J.J.G., Carrondo, M.A., Sieker, L.C., Le Gall, J. & Romão, M.J. (1995) Crystal structure of Desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: a novel non-heme iron protein structure. J. Mol. Biol. 251, 690-702.
    • (1995) J. Mol. Biol. , vol.251 , pp. 690-702
    • Archer, M.1    Huber, R.2    Tavares, P.3    Moura, I.4    Moura, J.J.G.5    Carrondo, M.A.6    Sieker, L.C.7    Le Gall, J.8    Romão, M.J.9
  • 17
    • 0024729942 scopus 로고
    • Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough
    • 17. Brumlik, M.J. & Voordouw, G. (1989) Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 171, 4996-5004.
    • (1989) J. Bacteriol. , vol.171 , pp. 4996-5004
    • Brumlik, M.J.1    Voordouw, G.2
  • 18
    • 0025695335 scopus 로고
    • The nucleotide sequence of the Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event
    • 18. Brumlik, M.J., Leroy, G., Bruschi, M. & Voordouw, G. (1990) The nucleotide sequence of the Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event. J. Bacteriol. 172, 7289-7292.
    • (1990) J. Bacteriol. , vol.172 , pp. 7289-7292
    • Brumlik, M.J.1    Leroy, G.2    Bruschi, M.3    Voordouw, G.4
  • 19
    • 0027263895 scopus 로고
    • Rubredoxin oxidase, a new flavo-heme-protein, is the site of oxygen reduction to water by the 'strict anaerobe' Desulfovibrio gigas
    • 19. Chen, L., Liu, M.Y., Le Gall, J., Faraleira, P., Santos, H. & Xavier, A.V. (1993) Rubredoxin oxidase, a new flavo-heme-protein, is the site of oxygen reduction to water by the 'strict anaerobe' Desulfovibrio gigas. Biochem. Biophys. Res. Comm. 193, 100-105.
    • (1993) Biochem. Biophys. Res. Comm. , vol.193 , pp. 100-105
    • Chen, L.1    Liu, M.Y.2    Le Gall, J.3    Faraleira, P.4    Santos, H.5    Xavier, A.V.6
  • 20
    • 0030954667 scopus 로고    scopus 로고
    • Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin
    • 20. Gomes, C.M., Silva, G., Oliveira, S., LeGall, J., Liu, M.Y., Xavier, A.V., Rodrigues-Pousada, C. & Teixeira, M. (1997) Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin. J. Biol. Chem. 272, 22502-22508.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22502-22508
    • Gomes, C.M.1    Silva, G.2    Oliveira, S.3    LeGall, J.4    Liu, M.Y.5    Xavier, A.V.6    Rodrigues-Pousada, C.7    Teixeira, M.8
  • 21
    • 0028144995 scopus 로고
    • Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris and its coupling to adenylyl phosphosulfate reductase
    • 21. Chen, L., Le Gall, J. & Xavier, A.V. (1994) Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris and its coupling to adenylyl phosphosulfate reductase. Biochem. Biophys. Res. Comm. 203, 839-844.
    • (1994) Biochem. Biophys. Res. Comm. , vol.203 , pp. 839-844
    • Chen, L.1    Le Gall, J.2    Xavier, A.V.3
  • 25
    • 0029826704 scopus 로고    scopus 로고
    • Overproduction of the rbo gene product from Desulfovibrio species suppresses all deleterious effects of lack of superoxide dismutase in Escherichia coli
    • 25. Pianzzola, M.J., Soubes, M. & Touati, D. (1996) Overproduction of the rbo gene product from Desulfovibrio species suppresses all deleterious effects of lack of superoxide dismutase in Escherichia coli. J. Bacteriol. 178, 6736-6742.
    • (1996) J. Bacteriol. , vol.178 , pp. 6736-6742
    • Pianzzola, M.J.1    Soubes, M.2    Touati, D.3
  • 26
    • 0030867832 scopus 로고    scopus 로고
    • A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (Desulfoferrodoxin) from Desulfoarculus baarsii
    • 26. Liochev, S.I. & Fridovich, I. (1997) A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (Desulfoferrodoxin) from Desulfoarculus baarsii. J. Biol. Chem. 272, 25573-25575.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25573-25575
    • Liochev, S.I.1    Fridovich, I.2
  • 27
    • 0002125420 scopus 로고
    • Significance of superoxide dismutase and catalase activities in the strict anaerobes, sulfate reducing bacteria
    • (Michelson, A.M., McCord, J.M. & Fridovich, I., eds.), Academic Press, London, UK
    • 27. Hatchikian, C.E., Le Gall & J. & Bell, G.R. (1977) Significance of superoxide dismutase and catalase activities in the strict anaerobes, sulfate reducing bacteria. In Superoxide and Superoxide Dismutases (Michelson, A.M., McCord, J.M. & Fridovich, I., eds.), pp. 159-172. Academic Press, London, UK.
    • (1977) Superoxide and Superoxide Dismutases , pp. 159-172
    • Hatchikian, C.E.1    Le Gall, J.2    Bell, G.R.3
  • 28
    • 0019799521 scopus 로고
    • The isolation of a hexaheme cytochrome from Desulfovibrio desulfuricans and its identification as a new type of nitrite reductase
    • 28. Liu, M.C. & Peck, H.D. Jr (1981) The isolation of a hexaheme cytochrome from Desulfovibrio desulfuricans and its identification as a new type of nitrite reductase. J. Biol. Chem. 256, 13159-13164.
    • (1981) J. Biol. Chem. , vol.256 , pp. 13159-13164
    • Liu, M.C.1    Peck H.D., Jr.2
  • 29
    • 0018110759 scopus 로고
    • Purification of electron transfer components from sulphate-reducing bacteria
    • Biomembranes (Fleischer, S. & Packer, L., eds.), Academic Press, NY, USA
    • 29. LeGall, J. & Forget, N. (1978) Purification of electron transfer components from sulphate-reducing bacteria. In Methods in Enzymology. Vol. LIII, Biomembranes (Fleischer, S. & Packer, L., eds.), pp. 613-634. Academic Press, NY, USA.
    • (1978) Methods in Enzymology , vol.53 , pp. 613-634
    • LeGall, J.1    Forget, N.2
  • 30
    • 0014691242 scopus 로고
    • Superoxide dismutase, an enzymic function for erythrocuprein (hemocuprein)
    • 30. McCord, J.M. & Fridovich, I. (1969) Superoxide Dismutase, an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 31
    • 0001232852 scopus 로고
    • One-dimensional polyacrylamide gel electrophoresis
    • (Hames, B.D. & Rickwood, D., eds.), IRL Press, Oxford, UK
    • 31. Hames, B.D. (1990) One-dimensional polyacrylamide gel electrophoresis. In Gel Electrophoresis of Proteins, a Practical Approach (Hames, B.D. & Rickwood, D., eds.), pp. 30-50. IRL Press, Oxford, UK.
    • (1990) Gel Electrophoresis of Proteins, A Practical Approach , pp. 30-50
    • Hames, B.D.1
  • 32
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • 32. Beauchamp, C. & Fridovich, I. (1971) Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44, 276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 33. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 34. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0025040442 scopus 로고
    • Protein blotting followed by microsequencing
    • 35. Choli, T. & Withmann-Liebold (1990) Protein blotting followed by microsequencing. Electrophoresis 11, 562-568.
    • (1990) Electrophoresis , vol.11 , pp. 562-568
    • Choli, T.1    Whithmann-Liebold2
  • 36
    • 0015514831 scopus 로고
    • Circular dichroism studies of myoglobin and cytochrome c derivatives
    • 36. Bolard, J. & Garnier, A. (1972) Circular dichroism studies of myoglobin and cytochrome c derivatives. Biochim. Biophys. Acta 263, 535-540.
    • (1972) Biochim. Biophys. Acta , vol.263 , pp. 535-540
    • Bolard, J.1    Garnier, A.2


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