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Volumn 169, Issue 5, 1998, Pages 424-433

A periplasmic flavoprotein in Wolinella succinogenes that resembles the fumarate reductase of Shewanella putrefaciens

Author keywords

Key words Fumarate reduction; Shewanella putrefaciens; Sulfide oxidation; Wolinella succinogenes

Indexed keywords

FLAVOPROTEIN; FORMIC ACID; FUMARATE REDUCTASE; FUMARIC ACID; SULFIDE;

EID: 0031947454     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050593     Document Type: Article
Times cited : (26)

References (56)
  • 5
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks BC (1996) A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22:393-404
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 6
    • 0029160337 scopus 로고
    • The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha
    • Berks BC, Richardson DJ, Reilly A, Willis AC, Ferguson SJ (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
  • 7
    • 84931997607 scopus 로고
    • Zur Eliminierung von Trübungsfehlern bei der Eiweißbestimmung mit der Biuretmethode
    • Bode C, Goebbel H, Stähler E (1968) Zur Eliminierung von Trübungsfehlern bei der Eiweißbestimmung mit der Biuretmethode. Z Klin Chem Klin Biochem 6:418-422
    • (1968) Z Klin Chem Klin Biochem , vol.6 , pp. 418-422
    • Bode, C.1    Goebbel, H.2    Stähler, E.3
  • 8
    • 0020509776 scopus 로고
    • Energy metabolism and biosynthesis of Vibrio succinogenes growing with nitrate or nitrite as terminal electron acceptor
    • Bokranz M et al. (1983) Energy metabolism and biosynthesis of Vibrio succinogenes growing with nitrate or nitrite as terminal electron acceptor. Arch Microbiol 135:36-41
    • (1983) Arch Microbiol , vol.135 , pp. 36-41
    • Bokranz, M.1
  • 9
    • 0025912548 scopus 로고
    • Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes
    • Bokranz M, Gutmann M, Körtner C, Kojro E, Fahrenholz F, Lauterbach F, Kroger A (1991) Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes. Arch Microbiol 156:119-128
    • (1991) Arch Microbiol , vol.156 , pp. 119-128
    • Bokranz, M.1    Gutmann, M.2    Körtner, C.3    Kojro, E.4    Fahrenholz, F.5    Lauterbach, F.6    Kroger, A.7
  • 10
    • 0020322828 scopus 로고
    • Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source
    • Bronder M, Mell H, Stupperich E, Kröger A (1982) Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source. Arch Microbiol 131:216-223
    • (1982) Arch Microbiol , vol.131 , pp. 216-223
    • Bronder, M.1    Mell, H.2    Stupperich, E.3    Kröger, A.4
  • 11
    • 0024968473 scopus 로고
    • Sulfur oxidation by phototrophic bacteria
    • Brune DC (1989) Sulfur oxidation by phototrophic bacteria. Biochim Biophys Acta 975:189-221
    • (1989) Biochim Biophys Acta , vol.975 , pp. 189-221
    • Brune, D.C.1
  • 12
    • 0028519153 scopus 로고
    • The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium
    • Chen Z et al. (1994) The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium. Science 266:430-432
    • (1994) Science , vol.266 , pp. 430-432
    • Chen, Z.1
  • 13
    • 0027221966 scopus 로고
    • Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium. Chromatium vinosum. a 2.6-kilobase pair DNa fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin
    • Dolata MM, Van Beeumen JJ, Ambler RP, Meyer TE, Cusanovich MA (1993) Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium. Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin. 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
  • 14
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower WJ, Miller JF, Ragsdale CW (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res 16:6127-6145
    • (1988) Nucleic Acids Res , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 15
    • 0021085263 scopus 로고
    • Lambda replacement vectors carrying polylinker sequences
    • Frischauf A, Lehrbach H, Poustka A, Murray N (1983) Lambda replacement vectors carrying polylinker sequences. J Mol Biol 170:827-842
    • (1983) J Mol Biol , vol.170 , pp. 827-842
    • Frischauf, A.1    Lehrbach, H.2    Poustka, A.3    Murray, N.4
  • 16
    • 0020074305 scopus 로고
    • A dot-immunobinding assay for monoclonal and other antibodies
    • Hawkes R, Niday E, Gordon J (1982) A dot-immunobinding assay for monoclonal and other antibodies. Anal Biochem 119:142-147
    • (1982) Anal Biochem , vol.119 , pp. 142-147
    • Hawkes, R.1    Niday, E.2    Gordon, J.3
  • 17
    • 0000207681 scopus 로고
    • TMbase - a database of membrane-spanning protein segments
    • Hofmann K, Stoffel W (1993) TMbase - a database of membrane-spanning protein segments. Biol Chem Hoppe Seyler 374:166
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 18
    • 0029094712 scopus 로고
    • The electron transfer from hydrogenase and formate dehydrogenase to polysulfide reductase in the membrane of Wolinella succinogenes
    • Jankielewicz A, Klimmek O, Kroger A (1995) The electron transfer from hydrogenase and formate dehydrogenase to polysulfide reductase in the membrane of Wolinella succinogenes. Biochim Biophys Acta 1231:157-162
    • (1995) Biochim Biophys Acta , vol.1231 , pp. 157-162
    • Jankielewicz, A.1    Klimmek, O.2    Kroger, A.3
  • 19
    • 0026011830 scopus 로고
    • 1-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins
    • 1-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins. FEBS Lett 279:205-209
    • (1991) FEBS Lett , vol.279 , pp. 205-209
    • Jüngst, A.1    Wakabayashi, S.2    Matsubara, H.3    Zumft, W.G.4
  • 20
    • 0018721473 scopus 로고
    • Physical characterisation of the "Rac prophage" in E. coli K-12
    • Kaiser K, Murray NE (1979) Physical characterisation of the "Rac prophage" in E. coli K-12. Mol Gen Genet 175:159-174
    • (1979) Mol Gen Genet , vol.175 , pp. 159-174
    • Kaiser, K.1    Murray, N.E.2
  • 22
    • 0026018923 scopus 로고
    • Growth of Wolinella succinogenes with polysulphide as terminal acceptor of phosphorylative electron transport
    • Klimmek O, Kröger A, Steudel R, Holdl G (1991) Growth of Wolinella succinogenes with polysulphide as terminal acceptor of phosphorylative electron transport. Arch Microbiol 155: 177-182
    • (1991) Arch Microbiol , vol.155 , pp. 177-182
    • Klimmek, O.1    Kröger, A.2    Steudel, R.3    Holdl, G.4
  • 25
    • 0026550359 scopus 로고
    • Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase
    • Krafft T et al. (1992) Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase. Eur J Biochem 206:503-510
    • (1992) Eur J Biochem , vol.206 , pp. 503-510
    • Krafft, T.1
  • 26
    • 0029016693 scopus 로고
    • The function of Wolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor
    • Krafft T, Gross R, Kröger A (1995) The function of Wolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor. Eur J Biochem 230:601-606
    • (1995) Eur J Biochem , vol.230 , pp. 601-606
    • Krafft, T.1    Gross, R.2    Kröger, A.3
  • 27
    • 0028798864 scopus 로고
    • Periplasmic sulphide dehydrogenase (Sud) from Wolinella succinogenes: Isolation, nucleotide sequence of the sud gne and its expression in Escherichia coli
    • Kreis-Kleinschmidt V, Fahrenholz F, Kojro E, Kröger A (1995) Periplasmic sulphide dehydrogenase (Sud) from Wolinella succinogenes: isolation, nucleotide sequence of the sud gne and its expression in Escherichia coli. Eur J Biochem 227:137-142
    • (1995) Eur J Biochem , vol.227 , pp. 137-142
    • Kreis-Kleinschmidt, V.1    Fahrenholz, F.2    Kojro, E.3    Kröger, A.4
  • 28
    • 0018183608 scopus 로고
    • Fumarate as terminal acceptor of phosphorylative electron transport
    • Kröger A (1978) Fumarate as terminal acceptor of phosphorylative electron transport. Biochim Biophys Acta 505:129-145
    • (1978) Biochim Biophys Acta , vol.505 , pp. 129-145
    • Kröger, A.1
  • 30
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods 10:203-209
    • (1984) J Biochem Biophys Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 32
    • 0023655557 scopus 로고
    • Cloning and expression of the genes of two fumarate reductase subunits from Wolinella succinogenes
    • Lauterbach F, Könner C, Tripier D, Unden G (1987) Cloning and expression of the genes of two fumarate reductase subunits from Wolinella succinogenes. Eur J Biochem 166:447-152
    • (1987) Eur J Biochem , vol.166 , pp. 447-1152
    • Lauterbach, F.1    Könner, C.2    Tripier, D.3    Unden, G.4
  • 33
    • 0027327093 scopus 로고
    • Characterization of a chromosomal gene and the antigen it expresses from the Lyme disease agent, Borrelia burgdorferi
    • LeFebvre RB, Probert WS, Perng GC (1993) Characterization of a chromosomal gene and the antigen it expresses from the Lyme disease agent, Borrelia burgdorferi. J Clin Microbiol 31:2146-2151
    • (1993) J Clin Microbiol , vol.31 , pp. 2146-2151
    • LeFebvre, R.B.1    Probert, W.S.2    Perng, G.C.3
  • 34
    • 0030967062 scopus 로고    scopus 로고
    • Structure and function of a second gene cluster encoding the formate dehydrogenase of Wolinella succinogenes
    • Lenger R, Herrmann D, Gross R, Simon J, Kroger A (1997) Structure and function of a second gene cluster encoding the formate dehydrogenase of Wolinella succinogenes. Eur J Biochem 246:646-651
    • (1997) Eur J Biochem , vol.246 , pp. 646-651
    • Lenger, R.1    Herrmann, D.2    Gross, R.3    Simon, J.4    Kroger, A.5
  • 35
    • 0027411256 scopus 로고
    • Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors
    • Lorenzen JP, Kroger A, Unden G (1993) Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors. Arch Microbiol 159:477-183
    • (1993) Arch Microbiol , vol.159 , pp. 477-1183
    • Lorenzen, J.P.1    Kroger, A.2    Unden, G.3
  • 36
    • 0028073773 scopus 로고
    • DMSO respiration by the anaerobic rumen bacterium Wolinella succinogenes
    • Lorenzen JP, Steinwachs S, Unden G (1994) DMSO respiration by the anaerobic rumen bacterium Wolinella succinogenes. Arch Microbiol 162:277-281
    • (1994) Arch Microbiol , vol.162 , pp. 277-281
    • Lorenzen, J.P.1    Steinwachs, S.2    Unden, G.3
  • 37
    • 0028033432 scopus 로고
    • Purification and properties of a novel cytochrome: Flavocytochrome c from Shewanella putrefaciens
    • Morris CJ et al. (1994) Purification and properties of a novel cytochrome: flavocytochrome c from Shewanella putrefaciens. Biochem J 302:587-593
    • (1994) Biochem J , vol.302 , pp. 587-593
    • Morris, C.J.1
  • 38
    • 0021907290 scopus 로고
    • Characterization of fumarate reductase from Baker's yeast: Essential sulfhydryl group for binding of FAD
    • Muratsubaki H, Katsume T (1985) Characterization of fumarate reductase from Baker's yeast: essential sulfhydryl group for binding of FAD. J Biochem 97:1201-1209
    • (1985) J Biochem , vol.97 , pp. 1201-1209
    • Muratsubaki, H.1    Katsume, T.2
  • 39
    • 0031054309 scopus 로고    scopus 로고
    • Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction od iron (III), fumarate, and nitrate by Shewanella putrefaciens MR-1
    • Myers CR, Myers JM (1997) Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction od iron (III), fumarate, and nitrate by Shewanella putrefaciens MR-1. J Bacteriol 179:1143-1152
    • (1997) J Bacteriol , vol.179 , pp. 1143-1152
    • Myers, C.R.1    Myers, J.M.2
  • 40
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, Von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 41
    • 0025344277 scopus 로고
    • Isolation of prokaryotic RNA and detection of specific mRNA with biotinylated probes
    • Oelmüller U, Krüger N, Steinbüchel A, Friedrich CG (1990) Isolation of prokaryotic RNA and detection of specific mRNA with biotinylated probes. J Microbiol Methods 11:73-84
    • (1990) J Microbiol Methods , vol.11 , pp. 73-84
    • Oelmüller, U.1    Krüger, N.2    Steinbüchel, A.3    Friedrich, C.G.4
  • 42
    • 0019469231 scopus 로고
    • Nucleotide sequence of the kanamycin resistance transposon Tn903
    • Oka A, Sugisaki H, Tukanami M (1981) Nucleotide sequence of the kanamycin resistance transposon Tn903. J Mol Biol 147: 217-226
    • (1981) J Mol Biol , vol.147 , pp. 217-226
    • Oka, A.1    Sugisaki, H.2    Tukanami, M.3
  • 43
    • 0026752211 scopus 로고
    • Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: A tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-hound enzymes from other bacteria
    • Pealing SL, Black AC, Manson FDC, Ward FB, Chapman SK, Reid GA (1992) Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-hound enzymes from other bacteria. Biochemistry 31: 12132-12140
    • (1992) Biochemistry , vol.31 , pp. 12132-12140
    • Pealing, S.L.1    Black, A.C.2    Manson, F.D.C.3    Ward, F.B.4    Chapman, S.K.5    Reid, G.A.6
  • 44
    • 0029881191 scopus 로고    scopus 로고
    • Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: Structural and functional differences among prokaryotic nitrate reductases
    • Reyes F, Roldan MD, Klipp W, Castillo F, Moreno-Vivian C (1996) Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases. Mol Microbiol 19:1307-1318
    • (1996) Mol Microbiol , vol.19 , pp. 1307-1318
    • Reyes, F.1    Roldan, M.D.2    Klipp, W.3    Castillo, F.4    Moreno-Vivian, C.5
  • 45
    • 0018588890 scopus 로고
    • Regulatory sequences involved in the promotion and termination of RNA transcription
    • Rosenberg M, Court D (1979) Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet 13:319-353
    • (1979) Annu Rev Genet , vol.13 , pp. 319-353
    • Rosenberg, M.1    Court, D.2
  • 48
    • 0027175993 scopus 로고
    • Bacterial sulphur respiration
    • Schauder R, Kroger A (1993) Bacterial sulphur respiration. Arch Microbiol 159:491-497
    • (1993) Arch Microbiol , vol.159 , pp. 491-497
    • Schauder, R.1    Kroger, A.2
  • 49
    • 0021922837 scopus 로고
    • The membranous nitrite reductase involved in the electron transport of Wolinella succinogenes
    • Schröder I, Roherton AM, Bokranz M, Unden G, Böcher R, Kroger A (1985) The membranous nitrite reductase involved in the electron transport of Wolinella succinogenes. Arch Microbiol 140:380-386
    • (1985) Arch Microbiol , vol.140 , pp. 380-386
    • Schröder, I.1    Roherton, A.M.2    Bokranz, M.3    Unden, G.4    Böcher, R.5    Kroger, A.6
  • 50
    • 0032518289 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon
    • Simon J, Gross R, Ringel M, Schmidt E, Kröger A (1998) Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon. Eur J Biochem 251:418-126
    • (1998) Eur J Biochem , vol.251 , pp. 418-1126
    • Simon, J.1    Gross, R.2    Ringel, M.3    Schmidt, E.4    Kröger, A.5
  • 51
    • 0002878518 scopus 로고
    • Expression using the T7 RNA polymerase/promoter system
    • Ausubel FA, Brent R, Kingston RE, Moore DD (eds) Greene and Wiley-Interscience, New York
    • Tabor S (1990) Expression using the T7 RNA polymerase/promoter system. In: Ausubel FA, Brent R, Kingston RE, Moore DD (eds) Current protocols in molecular biology. Greene and Wiley-Interscience, New York, pp 16.2.1-16.2.11
    • (1990) Current Protocols in Molecular Biology , pp. 1621-16211
    • Tabor, S.1
  • 52
    • 0024961689 scopus 로고
    • Purification and some characteristics of a cytochrome c-containing nitrous oxide reductase from Wolinella succinogenes
    • Teraguchi S, Hollocher TC (1989) Purification and some characteristics of a cytochrome c-containing nitrous oxide reductase from Wolinella succinogenes. J Biol Chem 264:1972-1979
    • (1989) J Biol Chem , vol.264 , pp. 1972-1979
    • Teraguchi, S.1    Hollocher, T.C.2
  • 53
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 54
    • 0022821997 scopus 로고
    • Reconstitution of a functional electron transport chain from purified formate dehydrogenase and fumarate reductase complex
    • Linden G, Kroger A (1986) Reconstitution of a functional electron transport chain from purified formate dehydrogenase and fumarate reductase complex. Methods Enzymol 126:387-399
    • (1986) Methods Enzymol , vol.126 , pp. 387-399
    • Linden, G.1    Kroger, A.2
  • 55
    • 0020442864 scopus 로고
    • The pUC plasmidsm an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira J, Messing J (1982) The pUC plasmidsm an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 56


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