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Volumn 182, Issue 11, 2000, Pages 3097-3103

A membrane-bound flavocytochrome c-sulfide dehydrogenase from the purple phototrophic sulfur bacterium Ectothiorhodospira vacuolata

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME; FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE; FLAVOPROTEIN; RNA; UNCLASSIFIED DRUG;

EID: 0034087223     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.11.3097-3103.2000     Document Type: Article
Times cited : (24)

References (54)
  • 1
    • 0015598626 scopus 로고
    • The amino acid sequences of cytochromes c-551 from three species of Pseudomonas
    • Ambler, R. P., and M. Wynn. 1973. The amino acid sequences of cytochromes c-551 from three species of Pseudomonas. Biochem. J. 131:485-498.
    • (1973) Biochem. J. , vol.131 , pp. 485-498
    • Ambler, R.P.1    Wynn, M.2
  • 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. 269:5705-5711.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5705-5711
    • Arieli, B.1    Shahak, Y.2    Taglicht, D.3    Hauska, G.4    Padan, E.5
  • 4
    • 0001023705 scopus 로고
    • Cytochromes
    • R. K. Clayton and W. R. Sistrom (ed.), Plenum Press, New York, N.Y.
    • Bartsch, R. G. 1978. Cytochromes, p. 249-279. In R. K. Clayton and W. R. Sistrom (ed.), The photosynthetic bacteria. Plenum Press, New York, N.Y.
    • (1978) The Photosynthetic Bacteria , pp. 249-279
    • Bartsch, R.G.1
  • 5
    • 0025854529 scopus 로고
    • The distribution of soluble metallo-redox proteins in purple phototrophic bacteria
    • Bartsch, R. G. 1991. The distribution of soluble metallo-redox proteins in purple phototrophic bacteria. Biochim. Biophys. Acta 1058:28-30.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 28-30
    • Bartsch, R.G.1
  • 6
    • 0010333120 scopus 로고
    • Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium
    • Bartsch, R. G., and M. D. Kamen. 1960. Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium. J. Biol. Chem. 235:825-831.
    • (1960) J. Biol. Chem. , vol.235 , pp. 825-831
    • Bartsch, R.G.1    Kamen, M.D.2
  • 7
    • 2042454654 scopus 로고
    • Complex c-type cytochromes with bound flavin
    • K. Okunuki, M. D. Kamen, and I. Sekuzu (ed.), University of Tokyo Press, Tokyo, Japan
    • Bartsch, R. G., T. E. Meyer, and A. B. Robinson. 1968. Complex c-type cytochromes with bound flavin, p. 443-451. In K. Okunuki, M. D. Kamen, and I. Sekuzu (ed.), Structure and function of cytochromes. University of Tokyo Press, Tokyo, Japan.
    • (1968) Structure and Function of Cytochromes , pp. 443-451
    • Bartsch, R.G.1    Meyer, T.E.2    Robinson, A.B.3
  • 8
    • 0029160337 scopus 로고
    • The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha
    • Berks, B. C., D. J. Richardson, A. Reilly, A. C. Willis, and S. J. Ferguson. 1995. The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha. Biochem. J. 309:983-992.
    • (1995) Biochem. J. , vol.309 , pp. 983-992
    • Berks, B.C.1    Richardson, D.J.2    Reilly, A.3    Willis, A.C.4    Ferguson, S.J.5
  • 9
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P. 1993. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins 17:363-374.
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 10
    • 0024968473 scopus 로고
    • Sulfur oxidation by phototrophic bacteria
    • Brune, D. C. 1989. Sulfur oxidation by phototrophic bacteria. Biochim. Biophys. Acta 973:189-221.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 189-221
    • Brune, D.C.1
  • 11
    • 0001864314 scopus 로고
    • Sulfur compounds as photosynthetic electron donors
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Kluwer Academic Publishers, New York, N.Y.
    • 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 Academic Publishers, New York, N.Y.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 847-870
    • Brune, D.C.1
  • 13
    • 0029974220 scopus 로고    scopus 로고
    • Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate
    • Clementz, T., J. J. Bednarski, and C. R. Raetz. 1996. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271:12095-12102.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12095-12102
    • Clementz, T.1    Bednarski, J.J.2    Raetz, C.R.3
  • 15
    • 0027221966 scopus 로고
    • Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum
    • Dolata, M. M., J. J. Van Beeumen, R. P. Ambler, T. E. Meyer, and M. A. Cusanovich. 1993. Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. J. Biol. Chem. 268:14426-14431.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14426-14431
    • Dolata, M.M.1    Van Beeumen, J.J.2    Ambler, R.P.3    Meyer, T.E.4    Cusanovich, M.A.5
  • 16
    • 12944321851 scopus 로고
    • Characterization of two soluble basic cytochromes isolated from the anoxygenic phototrophic sulfur bacterium Chlorobium phaeobacteroides
    • Fischer, U. 1989. Characterization of two soluble basic cytochromes isolated from the anoxygenic phototrophic sulfur bacterium Chlorobium phaeobacteroides. Z. Naturforsch. Sect. C 44:71-76.
    • (1989) Z. Naturforsch. Sect. C , vol.44 , pp. 71-76
    • Fischer, U.1
  • 18
    • 0032466668 scopus 로고    scopus 로고
    • Physiology and genetics of sulfur-oxidizing bacteria
    • Friedrich, C. G. 1998. Physiology and genetics of sulfur-oxidizing bacteria. Adv. Microb. Physiol. 39:235-289.
    • (1998) Adv. Microb. Physiol. , vol.39 , pp. 235-289
    • Friedrich, C.G.1
  • 19
    • 0018486945 scopus 로고
    • Flavocytochrome c of Chromatium vinosum
    • Fukumori, Y., and T. Yamanaka. 1979. Flavocytochrome c of Chromatium vinosum. J. Biochem. 85:1405-1414.
    • (1979) J. Biochem. , vol.85 , pp. 1405-1414
    • Fukumori, Y.1    Yamanaka, T.2
  • 20
    • 0028173490 scopus 로고
    • Characterization of flavocytochrome c-552 from the thermophilic photosynthetic bacterium Chromatium tepidum
    • Garcia-Castillo, M. C., B. S. Lou, M. R. Ondrias, D. E. Robertson, and D. B. Knaff. 1994. Characterization of flavocytochrome c-552 from the thermophilic photosynthetic bacterium Chromatium tepidum. Arch. Biochem. Biophys. 315:262-266.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 262-266
    • Garcia-Castillo, M.C.1    Lou, B.S.2    Ondrias, M.R.3    Robertson, D.E.4    Knaff, D.B.5
  • 21
    • 0345563260 scopus 로고    scopus 로고
    • Phylogenetic relationships among the Chromateaceae, their taxonomic reclassification and description of the new genera Allochromatium, Halochromatium, Isochromatium, Marichromatium, Thiococcus. Thiohalocapsa, and Thermochromatium
    • Imhoff, J. F., J, Süling, and R. Petri. 1998. Phylogenetic relationships among the Chromateaceae, their taxonomic reclassification and description of the new genera Allochromatium, Halochromatium, Isochromatium, Marichromatium, Thiococcus. Thiohalocapsa, and Thermochromatium. Int. J. Syst. Bacteriol. 48:1129-1143.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 1129-1143
    • Imhoff, J.F.1    Süling, J.2    Petri, R.3
  • 22
    • 0027190918 scopus 로고
    • Identification of cysteine residues alkylated with 3-bromopropylamine by protein sequence analysis
    • Jue, R. A., and H. E. Hale. 1993. Identification of cysteine residues alkylated with 3-bromopropylamine by protein sequence analysis. Anal. Biochem. 210: 39-44.
    • (1993) Anal. Biochem. , vol.210 , pp. 39-44
    • Jue, R.A.1    Hale, H.E.2
  • 24
    • 0029977436 scopus 로고    scopus 로고
    • Isolation and characterization of soluble electron transfer proteins from Chromatium purpuratum
    • Kerfeld, C. A., C. Dhan, M. Hirasawa, S. Kleis-San Francisco, T. O. Yeates, and D. B. Knaff. 1996. Isolation and characterization of soluble electron transfer proteins from Chromatium purpuratum. Biochemistry 35:7812-7818.
    • (1996) Biochemistry , vol.35 , pp. 7812-7818
    • Kerfeld, C.A.1    Dhan, C.2    Hirasawa, M.3    Kleis-San Francisco, S.4    Yeates, T.O.5    Knaff, D.B.6
  • 25
    • 0015862850 scopus 로고
    • Cytochrome c (553, Chlorobium thiosulfatophilum) is a sulfide-cytochrome c reductase
    • Kusai, A., and T. Yamanaka. 1973. Cytochrome c (553, Chlorobium thiosulfatophilum) is a sulfide-cytochrome c reductase. FEBS Lett. 34:235-237.
    • (1973) FEBS Lett. , vol.34 , pp. 235-237
    • Kusai, A.1    Yamanaka, T.2
  • 26
    • 0021322969 scopus 로고
    • Iron sulfur proteins of the purple sulfur bacterium Ectothiorkodospira shaposhnikovii
    • Küsche, W. H., and H. G. Trüper. 1984. Iron sulfur proteins of the purple sulfur bacterium Ectothiorkodospira shaposhnikovii. Arch. Microbiol. 137: 266-271.
    • (1984) Arch. Microbiol. , vol.137 , pp. 266-271
    • Küsche, W.H.1    Trüper, H.G.2
  • 27
    • 84961494830 scopus 로고
    • Cytochromes of the purple sulfur bacterium Ectothiorhodospira shaposhnikovii
    • Küsche, W. H., and H. G. Trüper. 1984. Cytochromes of the purple sulfur bacterium Ectothiorhodospira shaposhnikovii. Z. Naturforsch. Sect. C 39: 894-901.
    • (1984) Z. Naturforsch. Sect. C , vol.39 , pp. 894-901
    • Küsche, W.H.1    Trüper, H.G.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemlli, 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
    • Laemlli, U.K.1
  • 29
    • 0028785330 scopus 로고
    • Mutation of the htrB locus of Haemophilus influenzae non-typeable strain 2019 is associated with modifications of lipid A and phosphorylation of the lipo-oligosaccharide
    • Lee, N.-G., M. G. Sunshine, J. J. Engstram, B. W. Gibson, and M. A. Apicella. 1995. Mutation of the htrB locus of Haemophilus influenzae non-typeable strain 2019 is associated with modifications of lipid A and phosphorylation of the lipo-oligosaccharide. J. Biol. Chem. 270:27151-27159.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27151-27159
    • Lee, N.-G.1    Sunshine, M.G.2    Engstram, J.J.3    Gibson, B.W.4    Apicella, M.A.5
  • 31
    • 0021945136 scopus 로고
    • Chromatium flavocytochrome c - Kinetics of reduction of the heme subunit and the flavocytochrome mitochondrial cytochrome c complex
    • Meyer, T. E., W. P. Vorkink, G. Tollin, and M. A. Cusanovich. 1985. Chromatium flavocytochrome c - kinetics of reduction of the heme subunit and the flavocytochrome mitochondrial cytochrome c complex. Arch. Biochem. Biophys. 236:52-58.
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 52-58
    • Meyer, T.E.1    Vorkink, W.P.2    Tollin, G.3    Cusanovich, M.A.4
  • 32
    • 0026740398 scopus 로고
    • Localization of cytochromes to the outer membrane of anaerobically grown Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1992. Localization of cytochromes to the outer membrane of anaerobically grown Shewanella putrefaciens MR-1. J. Bacteriol. 147:3429-3438.
    • (1992) J. Bacteriol. , vol.147 , pp. 3429-3438
    • Myers, C.R.1    Myers, J.M.2
  • 33
    • 0032516752 scopus 로고    scopus 로고
    • Isolation and sequence of omcA, a gene encoding a decaheme outer membrane cytochrome c of Shewanella putrefaciens MR-1, and detection of omcA homologs in other strains of S. putrefaciens
    • Myers, J. M., and C. R. Myers. 1998. Isolation and sequence of omcA, a gene encoding a decaheme outer membrane cytochrome c of Shewanella putrefaciens MR-1, and detection of omcA homologs in other strains of S. putrefaciens. Biochim. Biophys. Acta 1373:237-251.
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 237-251
    • Myers, J.M.1    Myers, C.R.2
  • 34
    • 0031946732 scopus 로고    scopus 로고
    • Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum
    • Pattaragulwanit, K., D. C. Brune, G. Truper, and C. Wahl. 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, D.C.2    Truper, G.3    Wahl, C.4
  • 35
    • 0031864741 scopus 로고    scopus 로고
    • Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum
    • Reinartz, M., J. Tschape, T. Bruser, H. G. Truper, 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    Tschape, J.2    Bruser, T.3    Truper, H.G.4    Dahl, C.5
  • 37
    • 12944307967 scopus 로고
    • Enzymes with active-site redox-active disulfide bonds
    • Schulz, G. E., and P. A. Karplus. 1987. Enzymes with active-site redox-active disulfide bonds. Biochem. Soc. Trans. 16:81-84.
    • (1987) Biochem. Soc. Trans. , vol.16 , pp. 81-84
    • Schulz, G.E.1    Karplus, P.A.2
  • 38
    • 0344631752 scopus 로고    scopus 로고
    • Sulfide-quinone reductase from Rhodobacter capsulants: Requirement for growth, periplasmic localization, and extension of gene sequence analysis
    • Schutz, M., I. Maldener, C. Griesbeck, and G. Hauska. 1999. Sulfide-quinone reductase from Rhodobacter capsulants: requirement for growth, periplasmic localization, and extension of gene sequence analysis. J. Bacteriol. 181:6516-6523.
    • (1999) J. Bacteriol. , vol.181 , pp. 6516-6523
    • Schutz, M.1    Maldener, I.2    Griesbeck, C.3    Hauska, G.4
  • 39
    • 1842375039 scopus 로고    scopus 로고
    • Sulfide-quinone reductase from Rhodobacter capsulatus
    • Schutz, M., Y. Shahak, E. Padan, and G. Hauska. 1997. Sulfide-quinone reductase from Rhodobacter capsulatus. J. Biol. Chem. 272:9890-9894.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9890-9894
    • Schutz, M.1    Shahak, Y.2    Padan, E.3    Hauska, G.4
  • 40
    • 0026521170 scopus 로고
    • Sulfide quinone reductase (SQR) activity in Chlorobium
    • Shahak, Y., B. Arieli, E. Padan, and G. Hauska. 1992. Sulfide quinone reductase (SQR) activity in Chlorobium. FEBS Lett. 299:127-130.
    • (1992) FEBS Lett. , vol.299 , pp. 127-130
    • Shahak, Y.1    Arieli, B.2    Padan, E.3    Hauska, G.4
  • 41
    • 0013649061 scopus 로고    scopus 로고
    • Sulfide-dependent anoxygenic photosynthesis in prokaryotes
    • G. A. Peschek, W. Loffelhardt, and G. Schmetterer (ed.), Kluwer Academic Publishers, New York, N.Y.
    • Shahak, Y., M. Schutz, M. Bronstein, C. Griesbeck, G. Hauska, and E. Padan. 1999. Sulfide-dependent anoxygenic photosynthesis in prokaryotes, p. 217-228. In G. A. Peschek, W. Loffelhardt, and G. Schmetterer (ed.), The phototrophic prokaryotes. Kluwer Academic Publishers, New York, N.Y.
    • (1999) The Phototrophic Prokaryotes , pp. 217-228
    • Shahak, Y.1    Schutz, M.2    Bronstein, M.3    Griesbeck, C.4    Hauska, G.5    Padan, E.6
  • 43
    • 0013570688 scopus 로고
    • Cytochromes of the non-thiosulfate-utilizing green sulfur bacterium Chlorobium limicola
    • Steinmetz, M. A., and U. Fischer. 1981. Cytochromes of the non-thiosulfate-utilizing green sulfur bacterium Chlorobium limicola. Arch. Microbiol. 130: 31-37.
    • (1981) Arch. Microbiol. , vol.130 , pp. 31-37
    • Steinmetz, M.A.1    Fischer, U.2
  • 45
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P. E., D. Ryan, and W. Ledwin. 1976. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem 75:168-176.
    • (1976) Anal. Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Ledwin, W.3
  • 46
    • 4244217559 scopus 로고
    • 5 from Azotobacter vinelandii
    • 5 from Azotobacter vinelandii. Biochem. J. 64:582-589.
    • (1956) Biochem. J. , vol.64 , pp. 582-589
    • Tissieres, A.1
  • 47
    • 0025785321 scopus 로고
    • Covalent structure of the diheme cytochrome subunit and amino terminal sequence of the flavoprotein subunit of flavocytochrome c from Chromatium vinosum
    • Van Beeumen, J. J., H. Demol, B. Samyn, R. G. Bartsch, T. E. Meyer, M. M. Dolata, and M. A. Cusanovich. 1991. Covalent structure of the diheme cytochrome subunit and amino terminal sequence of the flavoprotein subunit of flavocytochrome c from Chromatium vinosum. J. Biol. Chem. 266:12921-12931.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12921-12931
    • Van Beeumen, J.J.1    Demol, H.2    Samyn, B.3    Bartsch, R.G.4    Meyer, T.E.5    Dolata, M.M.6    Cusanovich, M.A.7
  • 48
    • 0025280235 scopus 로고
    • Complete amino acid sequence of the cytochrome subunit and amino-terminal .sequence of the flavin subunit of flavocytochrome c (sulfide dehydrogenase) from Chlorobium thiosulfalophilum
    • Van Beeumen, J. J., S. Van Bun, T. E. Meyer, R. G. Bartsch, and M. A. Cusanovich. 1990. Complete amino acid sequence of the cytochrome subunit and amino-terminal .sequence of the flavin subunit of flavocytochrome c (sulfide dehydrogenase) from Chlorobium thiosulfalophilum. J. Biol. Chem. 265:9793-9799.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9793-9799
    • Van Beeumen, J.J.1    Van Bun, S.2    Meyer, T.E.3    Bartsch, R.G.4    Cusanovich, M.A.5
  • 49
    • 0029810580 scopus 로고    scopus 로고
    • Covalent structure of the flavoprotein subunit of the flavocytochrome c: Sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum
    • Van Driessche, G., M. Koh, Z. W. Chen, F. S. Mathews, T. E. Meyer, R. G. Bartsch, M. A. Cusanovich, and J. J. Van Beeumen. 1996. Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum. Protein Sci. 5:1753-1764.
    • (1996) Protein Sci. , vol.5 , pp. 1753-1764
    • Van Driessche, G.1    Koh, M.2    Chen, Z.W.3    Mathews, F.S.4    Meyer, T.E.5    Bartsch, R.G.6    Cusanovich, M.A.7    Van Beeumen, J.J.8
  • 50
    • 0031003025 scopus 로고    scopus 로고
    • A novel membrane-hound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobaccilus sp. W5
    • Visser, M., G. A. H. de Jong, L. A. Robertson, and J. G. Kuenen. 1997. A novel membrane-hound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobaccilus sp. W5. Arch. Microbiol. 167:295-301.
    • (1997) Arch. Microbiol. , vol.167 , pp. 295-301
    • Visser, M.1    De Jong, G.A.H.2    Robertson, L.A.3    Kuenen, J.G.4
  • 51
    • 0026716643 scopus 로고
    • Membrane protein structure prediction, hydrophobicity analysis and the positive-inside rule
    • Von Heijne, G. 1992. Membrane protein structure prediction, hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-195.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-1195
    • Von Heijne, G.1
  • 52
    • 0030843666 scopus 로고    scopus 로고
    • Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: Essential role of sulfite dehydrogenase in lithotrophic sulfur oxidation
    • Wodara, C., F. Bardischewsky, and C. G. Friedrich. 1997. Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: essential role of sulfite dehydrogenase in lithotrophic sulfur oxidation. J. Bacteriol. 179:5014-5023.
    • (1997) J. Bacteriol. , vol.179 , pp. 5014-5023
    • Wodara, C.1    Bardischewsky, F.2    Friedrich, C.G.3
  • 53
    • 0018813230 scopus 로고
    • Acetate metabolism in Ectothiorhodospira shaposhnikovii growing in dark
    • Zakharchuk, L. M., and R. N. Ivanovskii. 1980. Acetate metabolism in Ectothiorhodospira shaposhnikovii growing in dark. Mikrobiologiia 49:14-19.
    • (1980) Mikrobiologiia , vol.49 , pp. 14-19
    • Zakharchuk, L.M.1    Ivanovskii, R.N.2
  • 54
    • 0019052069 scopus 로고
    • Purification and properties of cytochrome c-552 from purple sulfur bacterium Thiocapsa roseopersina
    • English translation
    • Zorin, N. A., and I. N. Gogotov. 1980. Purification and properties of cytochrome c-552 from purple sulfur bacterium Thiocapsa roseopersina. Biokhimia 45:1134-1138. (English translation.)
    • (1980) Biokhimia , vol.45 , pp. 1134-1138
    • Zorin, N.A.1    Gogotov, I.N.2


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