메뉴 건너뛰기




Volumn 179, Issue 14, 1997, Pages 4607-4615

A rubrerythrin operon and nigerythrin gene in Desulfovibrio vulgaris (Hildenborough)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FERRIC ION; FERRIC SULFATE; FERROUS ION; IRON; RUBREDOXIN;

EID: 0030856583     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.14.4607-4615.1997     Document Type: Article
Times cited : (43)

References (55)
  • 4
    • 0026347331 scopus 로고
    • Determinant of protein hyperthermostability: Purification and amino acid sequence of rubredoxin from the hyperthermophilic archaeabacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR
    • Blake, P. R., J. B. Park, F. O. Bryant, S. Aono, J. K. Magnuson, E. Eccleston, J. B. Howard, M. F. Summers, and M. W. W. Adams. 1991. Determinant of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaeabacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR. Biochemistry 30:10885-10895.
    • (1991) Biochemistry , vol.30 , pp. 10885-10895
    • Blake, P.R.1    Park, J.B.2    Bryant, F.O.3    Aono, S.4    Magnuson, J.K.5    Eccleston, E.6    Howard, J.B.7    Summers, M.F.8    Adams, M.W.W.9
  • 5
    • 0002599331 scopus 로고    scopus 로고
    • Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin
    • Bonomi, F., D. M. Kurtz, Jr., and X. Cui. 1996. Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin. J. Inorg. Biochem. 1:67-72.
    • (1996) J. Inorg. Biochem. , vol.1 , pp. 67-72
    • Bonomi, F.1    Kurtz Jr., D.M.2    Cui, X.3
  • 6
    • 0024729942 scopus 로고
    • Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris (Hildenborough)
    • Brumlik, M. J., and G. Voordouw. 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
  • 8
    • 0002364807 scopus 로고
    • Survival of sulfate-reducing bacteria alter oxygen stress, and growth in sulfate-free oxygen-sulfide gradients
    • Cypionka, H., F. Widdel, and N. Pfennig. 1985. Survival of sulfate-reducing bacteria alter oxygen stress, and growth in sulfate-free oxygen-sulfide gradients. FEMS Microbiol. Ecol. 31:39-45.
    • (1985) FEMS Microbiol. Ecol. , vol.31 , pp. 39-45
    • Cypionka, H.1    Widdel, F.2    Pfennig, N.3
  • 11
    • 0029997030 scopus 로고    scopus 로고
    • Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins
    • Devrees, B., P. Tavares, J. Lampreia, N. Van Damme, J. Le Gall, J. J. G. Monra, J. Van Beeumen, and I. Moura. 1996. Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins. FEBS Lett. 385:138-142.
    • (1996) FEBS Lett. , vol.385 , pp. 138-142
    • Devrees, B.1    Tavares, P.2    Lampreia, J.3    Van Damme, N.4    Le Gall, J.5    Monra, J.J.G.6    Van Beeumen, J.7    Moura, I.8
  • 12
    • 0026577438 scopus 로고
    • Nucleotide sequence of dcrA, a Desulfovibrio vulgaris (Hildenborough) chemoreceptor gene, and its expression in Escherichia coli
    • Dolla, A., R. Fu, M. J. Brumlik, and G. Voordouw. 1992. Nucleotide sequence of dcrA, a Desulfovibrio vulgaris (Hildenborough) chemoreceptor gene, and its expression in Escherichia coli. J. Bacteriol. 174:1726-1733.
    • (1992) J. Bacteriol. , vol.174 , pp. 1726-1733
    • Dolla, A.1    Fu, R.2    Brumlik, M.J.3    Voordouw, G.4
  • 13
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with non-redox functions
    • Flint, D. H., and R. M. Allen. 1996. Iron-sulfur proteins with non-redox functions. Chem. Rev. 96:2315-2334.
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 14
    • 0028942712 scopus 로고
    • Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain
    • Gupta, N., F. Bonomi, D. M. Kurtz, Jr., N. Ravi, D. L. Wang, and B. H. Huynh. 1995. Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain. Biochemistry 34:3310-3318.
    • (1995) Biochemistry , vol.34 , pp. 3310-3318
    • Gupta, N.1    Bonomi, F.2    Kurtz Jr., D.M.3    Ravi, N.4    Wang, D.L.5    Huynh, B.H.6
  • 15
    • 0029818614 scopus 로고    scopus 로고
    • The role of fur in the acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition
    • Hall, H. K., and J. W. Foster. 1996. The role of Fur in the acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition. J. Bacteriol. 178:5683-5691.
    • (1996) J. Bacteriol. , vol.178 , pp. 5683-5691
    • Hall, H.K.1    Foster, J.W.2
  • 16
    • 0028576948 scopus 로고
    • Metabolism of sulfate-reducing prokaryotes
    • Hansen, T. A. 1994. Metabolism of sulfate-reducing prokaryotes. Antonie Leeuwenhoek 66:165-185.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 165-185
    • Hansen, T.A.1
  • 17
    • 0029898120 scopus 로고    scopus 로고
    • Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities
    • Hasset, D. J., P. A. Sokol, M. L. Howell, J.-F. Ma, H. T. Schweizer, U. Ochsner, and M. L. Vasil. 1996. Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities. J. Bacteriol. 178:3996-4003.
    • (1996) J. Bacteriol. , vol.178 , pp. 3996-4003
    • Hasset, D.J.1    Sokol, P.A.2    Howell, M.L.3    Ma, J.-F.4    Schweizer, H.T.5    Ochsner, U.6    Vasil, M.L.7
  • 18
    • 0002125420 scopus 로고
    • Significance of superoxide dismutase and catalase activities in the strict anaerobes, sulfate-reducing bacteria
    • A. M. Michael, J. M. McCord, and I. Fridovich (ed.), Academic Press. New York. N.Y.
    • Hatchikan, C. E., J. LeGall, and G. R. Bell. 1977. Significance of superoxide dismutase and catalase activities in the strict anaerobes, sulfate-reducing bacteria, p. 159-172. In A. M. Michael, J. M. McCord, and I. Fridovich (ed.), Superoxide and superoxide dismutase. Academic Press. New York. N.Y.
    • (1977) Superoxide and Superoxide Dismutase , pp. 159-172
    • Hatchikan, C.E.1    LeGall, J.2    Bell, G.R.3
  • 19
    • 0028583118 scopus 로고
    • Recomhinant proteins can be isolated from Escherichia coli cells by repeated cycles of freezing and thawing
    • Johnson, B. H., and M. H. Hecht. 1994. Recomhinant proteins can be isolated from Escherichia coli cells by repeated cycles of freezing and thawing. Bio/Technology 12:1357-1360.
    • (1994) Bio/Technology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 20
    • 12644273812 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in diiron-oxo proteins
    • Kurtz, D. M., Jr. 1997. Structural similarity and functional diversity in diiron-oxo proteins. J. Inorg. Biochem. 2:159-167.
    • (1997) J. Inorg. Biochem. , vol.2 , pp. 159-167
    • Kurtz Jr., D.M.1
  • 21
    • 0026318136 scopus 로고
    • Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris. Identification of potential ligands to the diiron site. Biochem
    • Kurtz, D. M., Jr., and B. C. Prickril. 1991. Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris. Identification of potential ligands to the diiron site. Biochem. Biophys. Res. Commun. 181:337-341.
    • (1991) Biophys. Res. Commun. , vol.181 , pp. 337-341
    • Kurtz Jr., D.M.1    Prickril, B.C.2
  • 22
    • 0029869132 scopus 로고    scopus 로고
    • Anaerobes response to oxygen: The sulfate-reducing bacteria
    • LeGall, J., and A. V. Xavier. 1996. Anaerobes response to oxygen: the sulfate-reducing bacteria. Anaerobe 2:1-9.
    • (1996) Anaerobe , vol.2 , pp. 1-9
    • LeGall, J.1    Xavier, A.V.2
  • 23
    • 0030474295 scopus 로고    scopus 로고
    • Ruhrerythrin from Clostridium perfringens: Cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function
    • Lehmann, Y., L. Meile, and M. Teuber. 1996. Ruhrerythrin from Clostridium perfringens: cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function. J. Bacteriol. 178:7152-7158.
    • (1996) J. Bacteriol. , vol.178 , pp. 7152-7158
    • Lehmann, Y.1    Meile, L.2    Teuber, M.3
  • 24
    • 0024996440 scopus 로고
    • Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: Rubrerythrin and a new, highly active enzyme
    • Liu, M.-Y., and J. LeGall. 1990. Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: rubrerythrin and a new, highly active enzyme. Biochem. Biophys. Res. Commun. 171:316-318.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 316-318
    • Liu, M.-Y.1    LeGall, J.2
  • 25
    • 0015477653 scopus 로고
    • Clostridial rubredoxin
    • Lovenberg, W. 1972. Clostridial rubredoxin. Methods Enzymol. 53:477-480.
    • (1972) Methods Enzymol. , vol.53 , pp. 477-480
    • Lovenberg, W.1
  • 26
    • 0027404899 scopus 로고
    • Influence of oxygen on sulfate reduction and growth of sulfate-reducing bacteria
    • Marschall, C., P. Frenzel, and H. Cypionka. 1993. Influence of oxygen on sulfate reduction and growth of sulfate-reducing bacteria. Arch. Microbiol. 159:168-173.
    • (1993) Arch. Microbiol. , vol.159 , pp. 168-173
    • Marschall, C.1    Frenzel, P.2    Cypionka, H.3
  • 27
    • 0011448278 scopus 로고
    • Filamentous coliphage M13 as a cloning vehicle: Insertion of a HindII fragment of the lac regulatory region in M13 replicative form in vitro
    • Messing, J., B. Gronenborn, B. Müller-Hill, and P. H. Hofschneider. 1977. Filamentous coliphage M13 as a cloning vehicle: insertion of a HindII fragment of the lac regulatory region in M13 replicative form in vitro. Proc. Natl. Acad. Sci. USA 74:3642-3646.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3642-3646
    • Messing, J.1    Gronenborn, B.2    Müller-Hill, B.3    Hofschneider, P.H.4
  • 28
    • 0028673449 scopus 로고
    • Characterization of 3 proteins containing multiple iron sites - Rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster
    • Moura, L, P. Tavares, and N. Ravi. 1994. Characterization of 3 proteins containing multiple iron sites - rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster. Methods Enzymol. 243:216-240.
    • (1994) Methods Enzymol. , vol.243 , pp. 216-240
    • Moura, L.1    Tavares, P.2    Ravi, N.3
  • 29
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands, J. B. 1995. Siderophores: structure and function of microbial iron transport compounds. J. Biol. Chem. 270:26723-26726.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 31
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • O'Halloran, T. 1993. Transition metals in control of gene expression. Science 261:715-725.
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.1
  • 32
    • 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
    • Pianzzola, M. J., M. Soubes, and D. Touati. 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
  • 33
    • 0027511224 scopus 로고
    • Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters
    • Pierik, A. J., R. B. G. Wolbert, G. L. Portier, M. F. J. M. Verhagen, and W. R. Hagen. 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.G.2    Portier, G.L.3    Verhagen, M.F.J.M.4    Hagen, W.R.5
  • 34
    • 0026347046 scopus 로고
    • Cloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenhorough)
    • Prickril, B. C., D. M. Kurtz, Jr., J. LeGall, and G. Voordouw. 1991. Cloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenhorough). Biochemistry 30:11118-11123.
    • (1991) Biochemistry , vol.30 , pp. 11118-11123
    • Prickril, B.C.1    Kurtz Jr., D.M.2    LeGall, J.3    Voordouw, G.4
  • 35
    • 0027251630 scopus 로고
    • Coordinate regulation of siderophore and exotoxin A production: Molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene
    • Prince, R. W., C. D. Cox, and M. L. Vasil. 1993. Coordinate regulation of siderophore and exotoxin A production: molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene. J. Bacteriol. 175:2589-2598.
    • (1993) J. Bacteriol. , vol.175 , pp. 2589-2598
    • Prince, R.W.1    Cox, C.D.2    Vasil, M.L.3
  • 36
    • 0026972793 scopus 로고
    • Polymerase chain-reaction (PCR) techniques for site-directed mutagenesis
    • Reikofski, J., and B. Y. Tao. 1992. Polymerase chain-reaction (PCR) techniques for site-directed mutagenesis. Biotechnol. Adv. 10:535-547.
    • (1992) Biotechnol. Adv. , vol.10 , pp. 535-547
    • Reikofski, J.1    Tao, B.Y.2
  • 38
    • 0012120182 scopus 로고
    • Media for thermophiles
    • F. T. Robb, A. R. Place, K. R. Sowers, H. J. Schreier, S. SasSarma, and E. M. Fleischmann (ed.), Cold Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Robb, F. T., and A. R. Place. 1995. Media for thermophiles, p. 167. In F. T. Robb, A. R. Place, K. R. Sowers, H. J. Schreier, S. SasSarma, and E. M. Fleischmann (ed.), Archaea: a laboratory manual for thermophiles. Cold Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1995) Archaea: A Laboratory Manual for Thermophiles , pp. 167
    • Robb, F.T.1    Place, A.R.2
  • 42
    • 0023472472 scopus 로고
    • Coomassie blue-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for direct visualization of polypeptides during electrophoresis
    • Schagger, H., and G. von Jagow. 1987. Coomassie blue-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for direct visualization of polypeptides during electrophoresis. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 43
    • 85036487646 scopus 로고    scopus 로고
    • Shenvi, N. V., and D. M. Kurtz, Jr. Unpublished data
    • Shenvi, N. V., and D. M. Kurtz, Jr. Unpublished data.
  • 45
    • 0027289080 scopus 로고
    • Protein molecular weight determinants by MALDI mass spectrometry: A superior alternative to gel filtration
    • Smith, E. T., D. S. Cornett, I. J. Amster, and M. W. W. Adams. 1993. Protein molecular weight determinants by MALDI mass spectrometry: a superior alternative to gel filtration. Anal. Biochem. 209:379-380.
    • (1993) Anal. Biochem. , vol.209 , pp. 379-380
    • Smith, E.T.1    Cornett, D.S.2    Amster, I.J.3    Adams, M.W.W.4
  • 47
    • 0028960213 scopus 로고
    • Functional domains of the Escherichia coli ferric uptake regulatory protein (Fur)
    • Stojiljkovic, I., and K. Hantke. 1995. Functional domains of the Escherichia coli ferric uptake regulatory protein (Fur). Mol. Gen. Genet. 247:199-205.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 199-205
    • Stojiljkovic, I.1    Hantke, K.2
  • 48
    • 0026713811 scopus 로고
    • The primary structure of a protein containing a putative [6Fc-6S] prismane cluster form Desulfovibrio vulgaris (Hildenborough)
    • Stokkermans, J. P. W. G., A. J. Pierik, R. B. G. Wolbert, W. R. Hagen, W. M. A. M. Van Dongen, and C. Veeger. 1992. The primary structure of a protein containing a putative [6Fc-6S] prismane cluster form Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 208:435-442.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 435-442
    • Stokkermans, J.P.W.G.1    Pierik, A.J.2    Wolbert, R.B.G.3    Hagen, W.R.4    Van Dongen, W.M.A.M.5    Veeger, C.6
  • 50
    • 0002878518 scopus 로고
    • Expression using the T7 RNA polymerase/promoter system
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Greene Publishing and Wiley-Interscience, New York, N.Y.
    • Tabor, S. 1990. Expression using the T7 RNA polymerase/promoter system, p. 16.2.1-16.2.11. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. Greene Publishing and Wiley-Interscience, New York, N.Y.
    • (1990) Current Protocols in Molecular Biology , pp. 1621-16211
    • Tabor, S.1
  • 51
    • 0027435546 scopus 로고
    • Sequence and activity of an endogenous promoter of the assimilatory sulfite reductase gene from Desulfovibrio vulgaris (Hildenborough)
    • Tan, J., and J. A. Cowan. 1993. Sequence and activity of an endogenous promoter of the assimilatory sulfite reductase gene from Desulfovibrio vulgaris (Hildenborough). Biotechnol. Lett. 15:901-906.
    • (1993) Biotechnol. Lett. , vol.15 , pp. 901-906
    • Tan, J.1    Cowan, J.A.2
  • 52
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis arc generated by iron in Δfur mutants of Escherichia coli: A protective role of superoxide dismutase
    • Touati, D., M. Jacques, B. Tardat, L. Bouchard, and S. Despied. 1995. Lethal oxidative damage and mutagenesis arc generated by iron in Δfur mutants of Escherichia coli: a protective role of superoxide dismutase. J. Bacteriol. 177:2305-2314.
    • (1995) J. Bacteriol. , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 53
    • 0029081824 scopus 로고
    • The genus Desulfovibrio: The centennial
    • Voordouw, G. 1995. The genus Desulfovibrio: the centennial. Appl. Environ. Microbiol. 61:2813-2819.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2813-2819
    • Voordouw, G.1
  • 54
    • 0004080071 scopus 로고
    • Molecular biology of sulfate-reducing bacteria
    • J. M. Odom and R. J. Singleton (ed.), Springer-Verlag, New York, N.Y.
    • Voordouw, G. 1994. Molecular biology of sulfate-reducing bacteria, p. 88-130. In J. M. Odom and R. J. Singleton (ed.), The sulfate-reducing bacteria: contemporary perspectives. Springer-Verlag, New York, N.Y.
    • (1994) The Sulfate-reducing Bacteria: Contemporary Perspectives , pp. 88-130
    • Voordouw, G.1
  • 55
    • 0001614970 scopus 로고
    • Gram-negative mesophilic sulfate-reducing bacteria
    • A. Balows, H. G. Truper, M. Dworkin, W. Harder, and K. H. Schleifer (ed.), Springer-Verlag, New York, N.Y.
    • Widdel, F., and F. Bak. 1992. Gram-negative mesophilic sulfate-reducing bacteria, p. 3352-3378. In A. Balows, H. G. Truper, M. Dworkin, W. Harder, and K. H. Schleifer (ed.), The prokaryotes: a handbook on the biology of bacteria. Ecophysiology, isolation, identification, application. Springer-Verlag, New York, N.Y.
    • (1992) The Prokaryotes: a Handbook on the Biology of Bacteria. Ecophysiology, Isolation, Identification, Application , pp. 3352-3378
    • Widdel, F.1    Bak, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.