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Volumn 257, Issue 1, 1998, Pages 210-215

Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential

Author keywords

Bacillus subtilis; Proton potential; Reversed electron transport; Succinate dehydrogenase; Succinate quinone oxidoreductase

Indexed keywords

1,4 BENZOQUINONE; CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; HEME; MENAQUINONE; OXIDOREDUCTASE; PROTON; SUCCINATE DEHYDROGENASE; SUCCINIC ACID; VALINOMYCIN;

EID: 0032189445     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570210.x     Document Type: Article
Times cited : (109)

References (38)
  • 1
    • 0343052744 scopus 로고    scopus 로고
    • Succinate: Quinone oxidoreductases. Variations on a conserved theme
    • Hägerhäll, C. (1997) Succinate: quinone oxidoreductases. Variations on a conserved theme, Biochim. Biophys. Acta 1320, 107-141.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 107-141
    • Hägerhäll, C.1
  • 2
    • 77956839772 scopus 로고
    • Progress in succinate: Quinone oxidoreductase research
    • (Ernster, L., ed.) Elsevier, New York
    • Hederstedt, L. & Ohnishi, T. (1992) Progress in succinate: quinone oxidoreductase research, in Molecular mechanisms in bioenergetics (Ernster, L., ed.) pp. 163-198, Elsevier, New York.
    • (1992) Molecular Mechanisms in Bioenergetics , pp. 163-198
    • Hederstedt, L.1    Ohnishi, T.2
  • 3
    • 0030600143 scopus 로고    scopus 로고
    • A structural model for the membrane-integral domain of succinate: Quinone oxidoreductases
    • Hägerhäll, C. & Hederstedt, L. (1996) A structural model for the membrane-integral domain of succinate: quinone oxidoreductases, FEBS Lett. 389, 25-31.
    • (1996) FEBS Lett. , vol.389 , pp. 25-31
    • Hägerhäll, C.1    Hederstedt, L.2
  • 4
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • (Neidhardt, F. C., ed.) Am. Soc. Microbiol., Washington, DC
    • Gennis, R. G. & Stewart, V. (1996) Respiration, in: Escherichia coli and Salmonella typhimurium (Neidhardt, F. C., ed.) pp. 219-226. Am. Soc. Microbiol., Washington, DC.
    • (1996) Escherichia Coli and Salmonella Typhimurium , pp. 219-226
    • Gennis, R.G.1    Stewart, V.2
  • 5
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • Unden, G. & Bongaerts, J. (1997) Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors, Biochim. Biophys. Acta 1320, 217-234.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 6
    • 0017394859 scopus 로고
    • Role of quinones in electron transport to oxygen and nitrate in Escherichia coli
    • Wallace, B. J. & Young, I. G. (1977) Role of quinones in electron transport to oxygen and nitrate in Escherichia coli, Biochim. Biophys. Acta 461, 84-100.
    • (1977) Biochim. Biophys. Acta , vol.461 , pp. 84-100
    • Wallace, B.J.1    Young, I.G.2
  • 7
    • 0025328799 scopus 로고
    • The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli
    • Wissenbach, U., Kröger, A. & Unden, G. (1990) The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli, Arch. Microbiol. 154, 60-66.
    • (1990) Arch. Microbiol. , vol.154 , pp. 60-66
    • Wissenbach, U.1    Kröger, A.2    Unden, G.3
  • 8
    • 0025647235 scopus 로고
    • Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis
    • Lemma, E., Unden, G. & Kröger, A. (1990) Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis, Arch. Microbiol. 155, 62-67.
    • (1990) Arch. Microbiol. , vol.155 , pp. 62-67
    • Lemma, E.1    Unden, G.2    Kröger, A.3
  • 10
    • 0026698031 scopus 로고
    • Two hemes in Bacillus subtilis succinate:menaquinone oxidoreductase (complex II)
    • Hägerhäll, C., Aasa, R., von Wachenfeldt, C. & Hederstedt, L. (1992) Two hemes in Bacillus subtilis succinate:menaquinone oxidoreductase (complex II), Biochemistry 31, 7411-7421.
    • (1992) Biochemistry , vol.31 , pp. 7411-7421
    • Hägerhäll, C.1    Aasa, R.2    Von Wachenfeldt, C.3    Hederstedt, L.4
  • 11
    • 0029103120 scopus 로고
    • Transmembrane topology and axial ligands to hemes in the cytochrome b subunit of Bacillus subtilis succinate: Menaquinone reductase
    • Hägerhäll, C., Friden, H., Aasa, R. & Hederstedt, L. (1995) Transmembrane topology and axial ligands to hemes in the cytochrome b subunit of Bacillus subtilis succinate: menaquinone reductase, Biochemistry 34, 11 080-11 089.
    • (1995) Biochemistry , vol.34 , pp. 11080-11089
    • Hägerhäll, C.1    Friden, H.2    Aasa, R.3    Hederstedt, L.4
  • 12
    • 0031661681 scopus 로고    scopus 로고
    • Expression of the succinate dehydrogenase genes (sdhCAB) from the facultative anaerobic Paenibacillus macerans during aerobic growth
    • in the press
    • Schirawski, J., Hankeln, T. & Unden, G. (1998) Expression of the succinate dehydrogenase genes (sdhCAB) from the facultative anaerobic Paenibacillus macerans during aerobic growth, Arch. Microbiol., in the press.
    • (1998) Arch. Microbiol.
    • Schirawski, J.1    Hankeln, T.2    Unden, G.3
  • 13
    • 0027860384 scopus 로고
    • Molecular identification of tRNA group 3 bacilli (Ash, Farrow, Wallbanks and Collins) using a PCR probe test
    • Ash, C., Priest, F. G. & Collins, M. D. (1993) Molecular identification of tRNA group 3 bacilli (Ash, Farrow, Wallbanks and Collins) using a PCR probe test, Antonie van Leeuwenhoek 64, 263-260.
    • (1993) Antonie Van Leeuwenhoek , vol.64 , pp. 263-1260
    • Ash, C.1    Priest, F.G.2    Collins, M.D.3
  • 14
    • 0015377507 scopus 로고
    • The nutrition of Bacillus megaterium and Bacillus cereus
    • White, P. J. (1972) The nutrition of Bacillus megaterium and Bacillus cereus, J. Gen. Microbiol. 71, 505-514.
    • (1972) J. Gen. Microbiol. , vol.71 , pp. 505-514
    • White, P.J.1
  • 15
    • 0028913541 scopus 로고
    • Anaerobic respiration of Bacillus macerans with fumarate, TMAO, nitrite and nitrate and regulation of the pathways by oxygen and nitrate
    • Schirawski, J. & Unden, G. (1995) Anaerobic respiration of Bacillus macerans with fumarate, TMAO, nitrite and nitrate and regulation of the pathways by oxygen and nitrate, Arch. Microbiol. 163, 148-154.
    • (1995) Arch. Microbiol. , vol.163 , pp. 148-154
    • Schirawski, J.1    Unden, G.2
  • 17
    • 0028176507 scopus 로고
    • Transport of C4-dicarboxylates by anaerobically grown Escherichia coli: Energetics and mechanism of exchange, uptake and efflux
    • Engel, P., Krämer, R. & Unden, G. (1994) Transport of C4-dicarboxylates by anaerobically grown Escherichia coli: energetics and mechanism of exchange, uptake and efflux, Eur. J. Biochem. 222, 605-614.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 605-614
    • Engel, P.1    Krämer, R.2    Unden, G.3
  • 18
    • 84931997607 scopus 로고
    • Zur Eliminierung von Trübungsfehlern bei der Eiweißbestimmung mit der Biuretmethode
    • Bode, C. H., Goebell, H. & Stähler, E. (1968) Zur Eliminierung von Trübungsfehlern bei der Eiweißbestimmung mit der Biuretmethode, Z. Klein. Chem. Biochem. 6, 418-422.
    • (1968) Z. Klein. Chem. Biochem. , vol.6 , pp. 418-422
    • Bode, C.H.1    Goebell, H.2    Stähler, E.3
  • 19
    • 0026802544 scopus 로고
    • Anaerobic fumarate transport in Escherichia coli by an fnr-dependent dicarboxylate uptake system which is different from aerobic dicarboxylate uptake
    • Engel, P., Krämer, R. & Unden, G. (1992) Anaerobic fumarate transport in Escherichia coli by an fnr-dependent dicarboxylate uptake system which is different from aerobic dicarboxylate uptake, J. Bacteriol. 174, 5533-5539.
    • (1992) J. Bacteriol. , vol.174 , pp. 5533-5539
    • Engel, P.1    Krämer, R.2    Unden, G.3
  • 20
    • 0018386943 scopus 로고
    • Site of interaction between phenazine methosulfate and the respiratory chain of Bacillus subtilis
    • Bisshop, A., Bergsma, J. & Konings, W. N. (1979) Site of interaction between phenazine methosulfate and the respiratory chain of Bacillus subtilis, Eur. J. Biochem. 93, 369-374.
    • (1979) Eur. J. Biochem. , vol.93 , pp. 369-374
    • Bisshop, A.1    Bergsma, J.2    Konings, W.N.3
  • 21
    • 0015501704 scopus 로고
    • Transport of dicarboxylic acids in Bacillus subtilis
    • Fournier, R. E., McKillen, M. N. & Pardee, A. B. (1972) Transport of dicarboxylic acids in Bacillus subtilis, J. Biol. Chem. 247, 5587-5595.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5587-5595
    • Fournier, R.E.1    McKillen, M.N.2    Pardee, A.B.3
  • 22
    • 0020597550 scopus 로고
    • Orientation of succinate dehydrogenase and cytochrome b558 in the Bacillus subtilis cytoplasmic membrane
    • Hederstedt, L. & Rutberg, L. (1983) Orientation of succinate dehydrogenase and cytochrome b558 in the Bacillus subtilis cytoplasmic membrane, J. Bacteriol. 153, 57-65.
    • (1983) J. Bacteriol. , vol.153 , pp. 57-65
    • Hederstedt, L.1    Rutberg, L.2
  • 23
    • 0026089233 scopus 로고
    • The structure of the dihaem cytochrome b of fumarate reduetase in Wolinella succinogenes: Circular dichroism and sequence analysis studies
    • Degli Esposti, M., Crimi, M., Körtner, C., Kröger, A. & Link, T. (1991) The structure of the dihaem cytochrome b of fumarate reduetase in Wolinella succinogenes: circular dichroism and sequence analysis studies. Biochim. Biophys. Acta 1056, 243-249.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 243-249
    • Degli Esposti, M.1    Crimi, M.2    Körtner, C.3    Kröger, A.4    Link, T.5
  • 24
    • 0028831032 scopus 로고
    • HOQNO interaction with cytochrome b in succinate: Menaquinone oxidoreductase from Bacillus subtilis
    • Smirnova, I. A., Hägerhäll, C., Konstantinov, A. A. & Hederstedt, L. (1995) HOQNO interaction with cytochrome b in succinate: menaquinone oxidoreductase from Bacillus subtilis, FEBS Lett. 359, 23-26.
    • (1995) FEBS Lett. , vol.359 , pp. 23-26
    • Smirnova, I.A.1    Hägerhäll, C.2    Konstantinov, A.A.3    Hederstedt, L.4
  • 25
    • 0026770801 scopus 로고
    • An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: Effects on fumarate, DMSO, TMAO and nitrate respiration
    • Wissenbach, U., Ternes, D. & Unden, G. (1992) An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, DMSO, TMAO and nitrate respiration, Arch. Microbiol. 158, 68-73.
    • (1992) Arch. Microbiol. , vol.158 , pp. 68-73
    • Wissenbach, U.1    Ternes, D.2    Unden, G.3
  • 26
    • 29244434147 scopus 로고
    • (Dubourguier, H. C., Albagnac, G., Montreuil, J., Romond, C., Sautière, P. & Guillaume, J., eds) Elsevier, Amsterdam
    • Kröger, A., Schröder, I. & Paulsen, J. (1986) in Biology of anaerobic bacteria (Dubourguier, H. C., Albagnac, G., Montreuil, J., Romond, C., Sautière, P. & Guillaume, J., eds) pp. 93-104, Elsevier, Amsterdam.
    • (1986) Biology of Anaerobic Bacteria , pp. 93-104
    • Kröger, A.1    Schröder, I.2    Paulsen, J.3
  • 27
    • 0023726308 scopus 로고
    • Citric-acid cycle, 50 years on. Modifications and an alternative pathway in anaerobic bacteria
    • Thauer, R. K. (1988) Citric-acid cycle, 50 years on. Modifications and an alternative pathway in anaerobic bacteria, Eur. J. Biochem. 176, 497-508.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 497-508
    • Thauer, R.K.1
  • 30
    • 0028823997 scopus 로고
    • Syntrophobacter pfennigii sp. nov., new syntrophically propionate-oxidizing anaerobe growing in pure culture with propionate and sulfate
    • Wallrabenstein, C., Hauschild, E. & Schink, B. (1995) Syntrophobacter pfennigii sp. nov., new syntrophically propionate-oxidizing anaerobe growing in pure culture with propionate and sulfate, Arch. Microbiol. 164, 346-352.
    • (1995) Arch. Microbiol. , vol.164 , pp. 346-352
    • Wallrabenstein, C.1    Hauschild, E.2    Schink, B.3
  • 31
    • 0022628946 scopus 로고
    • ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans
    • Paulsen, J., Kröger, A. & Thauer, R. K. (1986) ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans, Arch. Microbiol. 144, 78-83.
    • (1986) Arch. Microbiol. , vol.144 , pp. 78-83
    • Paulsen, J.1    Kröger, A.2    Thauer, R.K.3
  • 32
    • 0032518289 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon
    • Simon, J., Gross, R., Ringel, M., Schmidt, K. & Kröger, A. (1998) Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon, Eur. J. Biochem. 151, 418-426.
    • (1998) Eur. J. Biochem. , vol.151 , pp. 418-426
    • Simon, J.1    Gross, R.2    Ringel, M.3    Schmidt, K.4    Kröger, A.5
  • 33
    • 0032518432 scopus 로고    scopus 로고
    • Changes in proton potential and the cellular energetics of Escherichia coli during growth by aerobic or anaerobic respiration or by fermentation
    • Tran, Q. H. & Unden, G. (1998) Changes in proton potential and the cellular energetics of Escherichia coli during growth by aerobic or anaerobic respiration or by fermentation, Eur. J. Biochem. 251, 538-543.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 538-543
    • Tran, Q.H.1    Unden, G.2
  • 34
    • 0028138965 scopus 로고
    • Identification of the axial ligands of cytochrome b556 in succinate: Ubiquinone oxidoreductase from Escherichia coli
    • Peterson, J., Vibat, C. & Gennis, R. B. (1994) Identification of the axial ligands of cytochrome b556 in succinate: ubiquinone oxidoreductase from Escherichia coli, FEBS Lett. 355, 155-156.
    • (1994) FEBS Lett. , vol.355 , pp. 155-156
    • Peterson, J.1    Vibat, C.2    Gennis, R.B.3
  • 35
    • 0024286155 scopus 로고
    • Purification and properties of succinate-ubiquinone oxidoreductase complex from Paracoccus denitrificans
    • Pennoyer, J. D., Ohnishi, T. & Trumpower, B. L. (1988) Purification and properties of succinate-ubiquinone oxidoreductase complex from Paracoccus denitrificans, Biochim. Biophys. Acta 935, 195-207.
    • (1988) Biochim. Biophys. Acta , vol.935 , pp. 195-207
    • Pennoyer, J.D.1    Ohnishi, T.2    Trumpower, B.L.3
  • 36
    • 0026615072 scopus 로고
    • Cytochrome b560 (QPs1) of mitochondrial succinate-ubiquinone reductase. Immunochemistry, cloning, and nucleotide sequencing
    • Yu, L., Wei, Y. Y., Usui, S. & Yu, C. A. (1992) Cytochrome b560 (QPs1) of mitochondrial succinate-ubiquinone reductase. Immunochemistry, cloning, and nucleotide sequencing, J. Biol. Chem. 267, 24 508-24 515.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24508-24515
    • Yu, L.1    Wei, Y.Y.2    Usui, S.3    Yu, C.A.4
  • 37
    • 0027209342 scopus 로고
    • Nucleotide sequence of a putative succinate dehydrogenase operon in Thermoplasma acidophilum
    • Bach, M., Reiländer, H., Gärtner, P., Lottspeich, F. & Michel, H. (1993) Nucleotide sequence of a putative succinate dehydrogenase operon in Thermoplasma acidophilum, Biochim. Biophys. Acta 1174, 103-107.
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 103-107
    • Bach, M.1    Reiländer, H.2    Gärtner, P.3    Lottspeich, F.4    Michel, H.5
  • 38
    • 7344263027 scopus 로고    scopus 로고
    • EMBL database, accession no. Y07709
    • EMBL database, accession no. Y07709.


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