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Volumn 181, Issue 20, 1999, Pages 6516-6523

Sulfide-quinone reductase from Rhodobacter capsulatus: Requirement for growth, periplasmic localization, and extension of gene sequence analysis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HYBRID PROTEIN; OXIDOREDUCTASE; QUINONE DERIVATIVE; SULFIDE;

EID: 0344631752     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.20.6516-6523.1999     Document Type: Article
Times cited : (77)

References (42)
  • 1
    • 0000972384 scopus 로고
    • Structure and sequence of the photosynthesis gene cluster
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Kluwer, Dordrecht, The Netherlands
    • Alberti, M., D. H. Burke, and J. E. Hearst. 1995. Structure and sequence of the photosynthesis gene cluster, p. 1083-1106. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1083-1106
    • Alberti, M.1    Burke, D.H.2    Hearst, J.E.3
  • 2
    • 0028022988 scopus 로고
    • Purification and characterization of sulfide-quinone reductase (SQR), a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limnetica
    • Arieli, B., Y. Shahak, D. Taglicht, G. Hauska, and E. Padan. 1994. Purification and characterization of sulfide-quinone reductase (SQR), a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limnetica. J. Biol. Chem. 268:5705-5711.
    • (1994) J. Biol. Chem. , vol.268 , pp. 5705-5711
    • Arieli, B.1    Shahak, Y.2    Taglicht, D.3    Hauska, G.4    Padan, E.5
  • 3
    • 0343995028 scopus 로고
    • Partial resolution of the photophosphorylating system of Rhodopseudomonas capsulatus
    • Baccarini-Melandri, A., and B. A. Melandri. 1972. Partial resolution of the photophosphorylating system of Rhodopseudomonas capsulatus. Methods Enzymol. 23:556-561.
    • (1972) Methods Enzymol. , vol.23 , pp. 556-561
    • Baccarini-Melandri, A.1    Melandri, B.A.2
  • 4
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox factors
    • Berks, B. C. 1996. A common export pathway for proteins binding complex redox factors. Mol. Microbiol. 22:393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 5
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H. W., and D. Roulland-Dussoix. 1969. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 41:459-472.
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 6
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and ø80 phages transducing
    • Brickman, E., and J. Beckwith. 1975. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and ø80 phages transducing. J. Mol. Biol. 96:307-331.
    • (1975) J. Mol. Biol. , vol.96 , pp. 307-331
    • Brickman, E.1    Beckwith, J.2
  • 7
    • 0001864314 scopus 로고
    • Sulfur compounds as photosynthetic electron donors
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Kluwer, Dordrecht, The Netherlands
    • Brune, D. C. 1995. Sulfur compounds as photosynthetic electron donors, p. 847-870. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 847-870
    • Brune, D.C.1
  • 8
    • 0016754292 scopus 로고
    • Sulfide-dependent anoxygenic photosynthesis in the cyanobacterium Oscillatoria limnetica
    • Cohen, Y., B. B. Jorgensen, E. Padan, and M. Shilo. 1975. Sulfide-dependent anoxygenic photosynthesis in the cyanobacterium Oscillatoria limnetica. Nature 257:489-492.
    • (1975) Nature , vol.257 , pp. 489-492
    • Cohen, Y.1    Jorgensen, B.B.2    Padan, E.3    Shilo, M.4
  • 9
    • 0024240748 scopus 로고
    • Conjugal transfer of DNA to cyanobacteria
    • Elhai, J., and C. P. Wolk. 1988. Conjugal transfer of DNA to cyanobacteria. Methods Enzymol. 167:747-754.
    • (1988) Methods Enzymol. , vol.167 , pp. 747-754
    • Elhai, J.1    Wolk, C.P.2
  • 10
    • 0025091237 scopus 로고
    • Developmental regulation and spatial pattern of expression of the structural genes for nitrogenase in the cyanobacterium Anabaena
    • Elhai, J., and C. P. Wolk. 1990. Developmental regulation and spatial pattern of expression of the structural genes for nitrogenase in the cyanobacterium Anabaena. EMBO J. 9:3379-3388.
    • (1990) EMBO J. , vol.9 , pp. 3379-3388
    • Elhai, J.1    Wolk, C.P.2
  • 11
    • 0030693176 scopus 로고    scopus 로고
    • Characterization of a gene encoding dihydrolipoamide dehydrogenase of the cyanobacterium Synechocystis sp. strain PCC 6803
    • Engels, A., and E. K. Pistorius. 1997. Characterization of a gene encoding dihydrolipoamide dehydrogenase of the cyanobacterium Synechocystis sp. strain PCC 6803. Microbiology 143:3543-3553.
    • (1997) Microbiology , vol.143 , pp. 3543-3553
    • Engels, A.1    Pistorius, E.K.2
  • 12
    • 0030992284 scopus 로고    scopus 로고
    • Isolation, partial characterization and localization of a dihydrolipoamide dehydrogenase from the cyanobacterium Synechocystis sp. strain PCC 6803
    • Engels, A., U. Kahmann, H. G. Ruppel, and E. K. Pistorius. 1997. Isolation, partial characterization and localization of a dihydrolipoamide dehydrogenase from the cyanobacterium Synechocystis sp. strain PCC 6803. Biochim. Biophys. Acta 1340:33-44.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 33-44
    • Engels, A.1    Kahmann, U.2    Ruppel, H.G.3    Pistorius, E.K.4
  • 13
    • 0013676429 scopus 로고    scopus 로고
    • Physiology and genetics of bacterial sulfur oxidation
    • Friedrich, C. G. 1998. Physiology and genetics of bacterial sulfur oxidation. Adv. Microb. Physiol. 00:236-289.
    • (1998) Adv. Microb. Physiol. , pp. 236-289
    • Friedrich, C.G.1
  • 14
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant, S., J. Jersee, F. Bloom, and D. Hanahan. 1990. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc. Natl. Acad. Sci. USA 87:4645-4649.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4645-4649
    • Grant, S.1    Jersee, J.2    Bloom, F.3    Hanahan, D.4
  • 15
    • 0015440284 scopus 로고
    • Sulfide utilization by purple nonsulfur bacteria
    • Hansen, T. A., and H. van Gemerden. 1972. Sulfide utilization by purple nonsulfur bacteria. Arch. Microbiol. 86:49-56.
    • (1972) Arch. Microbiol. , vol.86 , pp. 49-56
    • Hansen, T.A.1    Van Gemerden, H.2
  • 16
    • 0002558837 scopus 로고
    • Taxonomy and physiology of phototrophic purple bacteria and green sulfur bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Kluwer, Dordrecht, The Netherlands
    • Imhoff, J. F. 1995. Taxonomy and physiology of phototrophic purple bacteria and green sulfur bacteria, p. 1-15. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1-15
    • Imhoff, J.F.1
  • 17
    • 0020529417 scopus 로고
    • Thioacetamide as a source of hydrogen sulfide for colony growth of purple sulfur bacteria
    • Irgens, R. L. 1983. Thioacetamide as a source of hydrogen sulfide for colony growth of purple sulfur bacteria. Curr. Microbiol. 8:183-186.
    • (1983) Curr. Microbiol. , vol.8 , pp. 183-186
    • Irgens, R.L.1
  • 18
    • 77957010716 scopus 로고
    • Bacterial membranes
    • Kabak, H. R. 1971. Bacterial membranes. Methods Enzymol. 22:99-120.
    • (1971) Methods Enzymol. , vol.22 , pp. 99-120
    • Kabak, H.R.1
  • 19
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T., et al. 1996. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1
  • 20
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H. P., et al. 1997. The complete genome sequence of the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus. Nature 390:364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1
  • 21
    • 0021528535 scopus 로고
    • Construction of a gene bank of Rhodopseudomonas capsulata using a broad host range DNA cloning system
    • Klug, G., and G. Drews. 1984. Construction of a gene bank of Rhodopseudomonas capsulata using a broad host range DNA cloning system. Arch. Microbiol. 139:319-332.
    • (1984) Arch. Microbiol. , vol.139 , pp. 319-332
    • Klug, G.1    Drews, G.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 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
  • 25
    • 0025095225 scopus 로고
    • Alkaline phosphatase fusions: Sensors of subcellular location
    • Manoil, C., J. J. Mekalanos, and J. Beckwith. 1990. Alkaline phosphatase fusions: sensors of subcellular location. J. Bacteriol. 172:515-518.
    • (1990) J. Bacteriol. , vol.172 , pp. 515-518
    • Manoil, C.1    Mekalanos, J.J.2    Beckwith, J.3
  • 26
    • 84916338716 scopus 로고
    • Subcommittee on Medical and Biologic Effects on Environmental Pollutants
    • Division of Medical Science, Assembly of Life Science, University Park Press, Baltimore, Md.
    • National Research Council. 1979. Subcommittee on Medical and Biologic Effects on Environmental Pollutants, Division of Medical Science, Assembly of Life Science, Hydrogen sulfide. University Park Press, Baltimore, Md.
    • (1979) Hydrogen Sulfide
  • 27
    • 0031946732 scopus 로고    scopus 로고
    • Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum
    • Pattaragulwanit, K., C. D. Brune, H. G. Trüper, and C. Dahl. 1998. Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum. Arch. Microbiol. 169:434-444.
    • (1998) Arch. Microbiol. , vol.169 , pp. 434-444
    • Pattaragulwanit, K.1    Brune, C.D.2    Trüper, H.G.3    Dahl, C.4
  • 28
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. M. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 30
    • 0031864741 scopus 로고    scopus 로고
    • Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum
    • Reinartz, M., J. Tschäpe, T. Brüser, H. G. Trüper, and C. Dahl. 1998. Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum. Arch. Microbiol. 170:59-68.
    • (1998) Arch. Microbiol. , vol.170 , pp. 59-68
    • Reinartz, M.1    Tschäpe, J.2    Brüser, T.3    Trüper, H.G.4    Dahl, C.5
  • 31
    • 0031670477 scopus 로고    scopus 로고
    • Sulfide-quinone reductase activity in membranes of the chemotrophic bacterium Paracoccus denitrificans GB17
    • Schütz, M., C. Klughammer, C. Griesbeck, A. Quentmeier, C. G. Friedrich, and G. Hauska. 1998. Sulfide-quinone reductase activity in membranes of the chemotrophic bacterium Paracoccus denitrificans GB17. Arch. Microbiol. 170:353-360.
    • (1998) Arch. Microbiol. , vol.170 , pp. 353-360
    • Schütz, M.1    Klughammer, C.2    Griesbeck, C.3    Quentmeier, A.4    Friedrich, C.G.5    Hauska, G.6
  • 32
    • 1842375039 scopus 로고    scopus 로고
    • Sulfide-quinone reductase from Rhodobacter capsulatus: Purification, cloning and expression
    • Schütz, M., Y. Shahak, E. Padan, and G. Hauska. 1997. Sulfide-quinone reductase from Rhodobacter capsulatus: purification, cloning and expression. J. Biol. Chem. 272:9890-9894.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9890-9894
    • Schütz, M.1    Shahak, Y.2    Padan, E.3    Hauska, G.4
  • 34
    • 0013649061 scopus 로고    scopus 로고
    • Sulfide-dependent anoxygenic photosynthesis in prokaryotes: Sulfide-quinone reductase (SQR), the initial step
    • G. A. Peschek, W. Löffelhardt, and G. Schmetterer (ed.), Plenum Press, New York, N.Y.
    • Shahak, Y., M. Schütz, M. Bronstein, C. Griesbeck, G. Hauska, and E. Padan. 1997. Sulfide-dependent anoxygenic photosynthesis in prokaryotes: sulfide-quinone reductase (SQR), the initial step, p. 217-228. In G. A. Peschek, W. Löffelhardt, and G. Schmetterer (ed.), Proceedings of the 9th International Symposium on Phototrophic Procaryotes (Vienna 1997). Plenum Press, New York, N.Y.
    • (1997) Proceedings of the 9th International Symposium on Phototrophic Procaryotes (Vienna 1997) , pp. 217-228
    • Shahak, Y.1    Schütz, M.2    Bronstein, M.3    Griesbeck, C.4    Hauska, G.5    Padan, E.6
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 34250582917 scopus 로고
    • Sulphur metabolism in Thiorhodaceae. 1. Quantitative measurements on growing cells of Chromatium okenii
    • Trüper, H. G., and H. G. Schlegel. 1964. Sulphur metabolism in Thiorhodaceae. 1. Quantitative measurements on growing cells of Chromatium okenii. Antonie Leeuwenhoek 30:225-281.
    • (1964) Antonie Leeuwenhoek , vol.30 , pp. 225-281
    • Trüper, H.G.1    Schlegel, H.G.2
  • 39
    • 0000657541 scopus 로고
    • The sulfide affinity of phototrophic bacteria in relation to the location of elemental sulfur
    • Van Gemerden, H. 1984. The sulfide affinity of phototrophic bacteria in relation to the location of elemental sulfur. Arch. Microbiol. 139:289-294.
    • (1984) Arch. Microbiol. , vol.139 , pp. 289-294
    • Van Gemerden, H.1
  • 40
    • 0031003025 scopus 로고    scopus 로고
    • A novel membrane-bound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobacillus sp. W5
    • Van Visser, J., G. A. H. de Jong, L. A. Robertson, and J. G. Kuenen. 1997. A novel membrane-bound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobacillus sp. W5. Arch. Microbiol. 167: 295-301.
    • (1997) Arch. Microbiol. , vol.167 , pp. 295-301
    • Van Visser, J.1    De Jong, G.A.H.2    Robertson, L.A.3    Kuenen, J.G.4
  • 42
    • 0016720598 scopus 로고
    • Characterization of Rhodopseudomonas capsulata
    • Weaver, P. F., J. D. Wall, and H. Gest. 1975. Characterization of Rhodopseudomonas capsulata. Arch. Microbiol. 105:207-221.
    • (1975) Arch. Microbiol. , vol.105 , pp. 207-221
    • Weaver, P.F.1    Wall, J.D.2    Gest, H.3


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