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Volumn 69, Issue 11, 2003, Pages 6345-6353

Energy Conservation in Acetogenic Bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ACETOGENIN; ADENOSINE TRIPHOSPHATE; HYDROGEN; SODIUM;

EID: 10744223111     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.11.6345-6353.2003     Document Type: Short Survey
Times cited : (264)

References (80)
  • 2
    • 0002889025 scopus 로고
    • Occurence of corrinoid-containing membrane proteins in anaerobic bacteria
    • Dangel, W., H. Schulz, G. Diekert, H. König, and G. Fuchs. 1987. Occurence of corrinoid-containing membrane proteins in anaerobic bacteria. Arch. Microbiol. 148:52-56.
    • (1987) Arch. Microbiol. , vol.148 , pp. 52-56
    • Dangel, W.1    Schulz, H.2    Diekert, G.3    König, H.4    Fuchs, G.5
  • 3
    • 0024441894 scopus 로고
    • Structure and function of a menaquinone involved in electron transport in membranes of Clostridium thermoautotrophicum and Clostridium thermoaceticum
    • Das, A., J. Hugenholtz, H. van Halbeek, and L. G. Ljungdahl. 1989. Structure and function of a menaquinone involved in electron transport in membranes of Clostridium thermoautotrophicum and Clostridium thermoaceticum. J. Bacteriol. 171:5823-5829.
    • (1989) J. Bacteriol. , vol.171 , pp. 5823-5829
    • Das, A.1    Hugenholtz, J.2    Van Halbeek, H.3    Ljungdahl, L.G.4
  • 4
    • 0031046043 scopus 로고    scopus 로고
    • 0 ATP synthase from the obligately anaerobic gram-positive bacterium Clostridium thermoautotrophicum
    • 0 ATP synthase from the obligately anaerobic gram-positive bacterium Clostridium thermoautotrophicum. J. Bacteriol. 179:1714-1720.
    • (1997) J. Bacteriol. , vol.179 , pp. 1714-1720
    • Das, A.1    Ivey, D.M.2    Ljungdahl, L.G.3
  • 5
    • 0030998932 scopus 로고    scopus 로고
    • 0 ATP synthase from the obligately anaerobic bacterium Clostridium thermoaceticum
    • 0 ATP synthase from the obligately anaerobic bacterium Clostridium thermoaceticum. J. Bacteriol. 179:3746-3755.
    • (1997) J. Bacteriol. , vol.179 , pp. 3746-3755
    • Das, A.1    Ljungdahl, L.G.2
  • 6
    • 0242503650 scopus 로고    scopus 로고
    • Electron-transport systems in acetogens
    • L. G. Ljungdahl, M. W. Adams, L. L. Barton, J. G. Ferry, and M. K. Johnson (ed.). Springer, New York, N.Y.
    • Das, A., and L. G. Ljungdahl. 2003. Electron-transport systems in acetogens, p. 191-204. In L. G. Ljungdahl, M. W. Adams, L. L. Barton, J. G. Ferry, and M. K. Johnson (ed.), Biochemistry and physiology of anaerobic bacteria. Springer, New York, N.Y.
    • (2003) Biochemistry and Physiology of Anaerobic Bacteria , pp. 191-204
    • Das, A.1    Ljungdahl, L.G.2
  • 7
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic archaea
    • Deppenmeier, U., V. Müller, and G. Gottschalk. 1996. Pathways of energy conservation in methanogenic archaea. Arch. Microbiol. 165:149-163.
    • (1996) Arch. Microbiol. , vol.165 , pp. 149-163
    • Deppenmeier, U.1    Müller, V.2    Gottschalk, G.3
  • 9
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • Dimroth, P. 1997. Primary sodium ion translocating enzymes. Biochim. Biophys. Acta 1318:11-51.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 10
    • 0034663502 scopus 로고    scopus 로고
    • Critical evaluation of the one-versus the two-channel model for the operation of the ATP synthase's motor
    • Dimroth, P., U. Matthey, and G. Kaim. 2000. Critical evaluation of the one-versus the two-channel model for the operation of the ATP synthase's motor. Biochim. Biophys. Acta 1459:506-513.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 506-513
    • Dimroth, P.1    Matthey, U.2    Kaim, G.3
  • 11
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/ acetyl CoA synthase
    • Doukov, T. I., T. M. Iverson, J. Seravalli, S. W. Ragsdale, and C. L. Drennan. 2002. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/ acetyl CoA synthase. Science 298:567-572.
    • (2002) Science , vol.298 , pp. 567-572
    • Doukov, T.I.1    Iverson, T.M.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 12
    • 0030838596 scopus 로고    scopus 로고
    • Acetogenic bacteria: What are the in situ consequences of their diverse metabolic diversities?
    • Drake, H. L., S. Daniel, K. Küsel, C. Matthies, C. Kuhner, and S. Braus-Strohmeyer. 1997. Acetogenic bacteria: what are the in situ consequences of their diverse metabolic diversities? Biofactors 1:13-24.
    • (1997) Biofactors , vol.1 , pp. 13-24
    • Drake, H.L.1    Daniel, S.2    Küsel, K.3    Matthies, C.4    Kuhner, C.5    Braus-Strohmeyer, S.6
  • 13
    • 0010402471 scopus 로고
    • Acetogenesis: Reality in the laboratory, uncertainty elsewhere
    • H. L. Drake (ed.). Chapman & Hall, New York, N.Y.
    • Drake, H. L., S. L. Daniel, C. Matthies, and K. Küsel. 1994. Acetogenesis: reality in the laboratory, uncertainty elsewhere, p. 273-302. In H. L. Drake (ed.), Acetogenesis. Chapman & Hall, New York, N.Y.
    • (1994) Acetogenesis , pp. 273-302
    • Drake, H.L.1    Daniel, S.L.2    Matthies, C.3    Küsel, K.4
  • 14
    • 0242690158 scopus 로고    scopus 로고
    • How the diverse physiologic potentials of acetogens determine their in situ realities
    • L. G. Ljungdahl, M. W. Adams, L. L. Barton, J. G. Ferry, and M. K. Johnson (ed.). Springer, New York, N.Y.
    • Drake, H. L., and K. Küsel. 2003. How the diverse physiologic potentials of acetogens determine their in situ realities, p. 171-190. In L. G. Ljungdahl, M. W. Adams, L. L. Barton, J. G. Ferry, and M. K. Johnson (ed.), Biochemistry and physiology of anaerobic bacteria. Springer, New York, N.Y.
    • (2003) Biochemistry and Physiology of Anaerobic Bacteria , pp. 171-190
    • Drake, H.L.1    Küsel, K.2
  • 15
    • 33746916074 scopus 로고    scopus 로고
    • Acetogenic prokaryotes
    • M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, and E. Stackebrandt (ed.), in press. Springer-Verlag, New York, N.Y.
    • Drake, H. L., K. Küsel, and C. Matthies. Acetogenic prokaryotes. In M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, and E. Stackebrandt (ed.), The prokaryotes, 3rd ed., in press. Springer-Verlag, New York, N.Y.
    • The Prokaryotes, 3rd Ed.
    • Drake, H.L.1    Küsel, K.2    Matthies, C.3
  • 16
    • 0033960457 scopus 로고    scopus 로고
    • + transport to rotary catalysis in F-type ATP synthases: Structure and organization of the transmembrane rotary motor
    • + transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor. J. Exp. Biol. 203:9-17.
    • (2000) J. Exp. Biol. , vol.203 , pp. 9-17
    • Fillingame, R.H.1    Jiang, W.2    Dmitriev, O.Y.3
  • 17
    • 0029065372 scopus 로고
    • 0-type enzyme as deduced from the primary structure of its β, γ, and ε subunits
    • 0-type enzyme as deduced from the primary structure of its β, γ, and ε subunits. Biochim. Biophys. Acta 1229:393-397.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 393-397
    • Forster, A.1    Daniel, R.2    Müller, V.3
  • 18
    • 0029764693 scopus 로고    scopus 로고
    • Effect of nitrate on the autotrophic metabolism of the acetogens Clostridium thermoautotrophicum and Clostridium thermoaceticum
    • Fröstl, J. M., C. Seifritz, and H. L. Drake. 1996. Effect of nitrate on the autotrophic metabolism of the acetogens Clostridium thermoautotrophicum and Clostridium thermoaceticum. J. Bacteriol. 178:4597-4603.
    • (1996) J. Bacteriol. , vol.178 , pp. 4597-4603
    • Fröstl, J.M.1    Seifritz, C.2    Drake, H.L.3
  • 19
    • 0000491579 scopus 로고
    • 2 fixation in acetogenic bacteria: Variations on a theme
    • 2 fixation in acetogenic bacteria: variations on a theme. FEMS Microbiol. Rev. 39:181-213.
    • (1986) FEMS Microbiol. Rev. , vol.39 , pp. 181-213
    • Fuchs, G.1
  • 21
    • 0035342616 scopus 로고    scopus 로고
    • +-translocating methyltransferase complex from methanogenic archaea
    • +-translocating methyltransferase complex from methanogenic archaea. Biochim. Biophys. Acta 1505: 28-36.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 28-36
    • Gottschalk, G.1    Thauer, R.K.2
  • 22
    • 0016612344 scopus 로고
    • Presence of cytochrome and menaquinone in Clostridium formicoaceticum and Clostridium thermoaceticum
    • Gottwald, M., J. R. Andreesen, J. LeGall, and L. G. Ljungdahl. 1975. Presence of cytochrome and menaquinone in Clostridium formicoaceticum and Clostridium thermoaceticum. J. Bacteriol. 122:325-328.
    • (1975) J. Bacteriol. , vol.122 , pp. 325-328
    • Gottwald, M.1    Andreesen, J.R.2    LeGall, J.3    Ljungdahl, L.G.4
  • 24
    • 0027172356 scopus 로고
    • Acetogenesis and ATP synthesis in Acetobacterium woodii are coupled via a transmembrane primary sodium ion gradient
    • Heise, R., V. Müller, and G. Gottschalk. 1993. Acetogenesis and ATP synthesis in Acetobacterium woodii are coupled via a transmembrane primary sodium ion gradient. FEMS Microbiol. Lett. 112:261-268.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 261-268
    • Heise, R.1    Müller, V.2    Gottschalk, G.3
  • 25
    • 0026553733 scopus 로고
    • Presence of a sodium-translocating ATPase in membrane vesicles of the homoacetogenic bacterium Acetobacterium woodii
    • Heise, R., V. Müller, and G. Gottschalk. 1992. Presence of a sodium-translocating ATPase in membrane vesicles of the homoacetogenic bacterium Acetobacterium woodii. Eur. J. Biochem. 206:553-557.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 553-557
    • Heise, R.1    Müller, V.2    Gottschalk, G.3
  • 26
    • 0024430852 scopus 로고
    • Sodium dependence of acetate formation by the acetogenic bacterium Acetobacterium woodii
    • Heise, R., V. Müller, and G. Gottschalk. 1989. Sodium dependence of acetate formation by the acetogenic bacterium Acetobacterium woodii. J. Bacteriol. 171:5473-5478.
    • (1989) J. Bacteriol. , vol.171 , pp. 5473-5478
    • Heise, R.1    Müller, V.2    Gottschalk, G.3
  • 27
    • 0026355811 scopus 로고
    • A sodium-stimulated ATP synthase in the acetogenic bacterium Acetobacterium woodii
    • Heise, R., J. Reidlinger, V. Müller, and G. Gottschalk. 1991. A sodium-stimulated ATP synthase in the acetogenic bacterium Acetobacterium woodii. FEBS Lett. 295:119-122.
    • (1991) FEBS Lett. , vol.295 , pp. 119-122
    • Heise, R.1    Reidlinger, J.2    Müller, V.3    Gottschalk, G.4
  • 28
    • 0023481430 scopus 로고
    • Carbon monoxide-driven electron transport in Clostridium thermoautotrophicum membranes
    • Hugenholtz, J., D. M. Ivey, and L. G. Ljungdahl. 1987. Carbon monoxide-driven electron transport in Clostridium thermoautotrophicum membranes. J. Bacteriol. 169:5845-5847.
    • (1987) J. Bacteriol. , vol.169 , pp. 5845-5847
    • Hugenholtz, J.1    Ivey, D.M.2    Ljungdahl, L.G.3
  • 29
    • 0025428205 scopus 로고
    • Amino acid transport in membrane vesicles of Clostridium thermoautotrophicum
    • Hugenholtz, J., and L. G. Ljungdahl. 1990. Amino acid transport in membrane vesicles of Clostridium thermoautotrophicum. FEMS Microbiol. Lett. 69:117-122.
    • (1990) FEMS Microbiol. Lett. , vol.69 , pp. 117-122
    • Hugenholtz, J.1    Ljungdahl, L.G.2
  • 30
    • 0024671412 scopus 로고
    • Electron transport and electrochemical proton gradient in membrane vesicles of Clostridium thermoaceticum
    • Hugenholtz, J., and L. G. Ljungdahl. 1989. Electron transport and electrochemical proton gradient in membrane vesicles of Clostridium thermoaceticum. J. Bacteriol. 171:2873-2875.
    • (1989) J. Bacteriol. , vol.171 , pp. 2873-2875
    • Hugenholtz, J.1    Ljungdahl, L.G.2
  • 31
    • 0036205493 scopus 로고    scopus 로고
    • - as the coupling ion during hydrogen-dependent caffeate reduction by Acetobacterium woodii
    • - as the coupling ion during hydrogen-dependent caffeate reduction by Acetobacterium woodii. J. Bacteriol. 184:1947-1951.
    • (2002) J. Bacteriol. , vol.184 , pp. 1947-1951
    • Imkamp, F.1    Müller, V.2
  • 33
    • 0032491417 scopus 로고    scopus 로고
    • +-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis
    • +-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis. J. Biol. Chem. 273:29701-29705.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29701-29705
    • Jones, P.C.1    Fillingame, R.H.2
  • 34
    • 0027144899 scopus 로고
    • 0 ATPase in Escherichia coli by homologous recombination
    • 0 ATPase in Escherichia coli by homologous recombination. Eur. J. Biochem. 218:937-944.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 937-944
    • Kaim, G.1    Dimroth, P.2
  • 35
    • 0030809240 scopus 로고    scopus 로고
    • + in the c subunit of the ATP synthase from Propionigenium modestum
    • + in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 36:9185-9194.
    • (1997) Biochemistry , vol.36 , pp. 9185-9194
    • Kaim, G.1    Wehrle, F.2    Gerike, U.3    Dimroth, P.4
  • 37
    • 0029956986 scopus 로고    scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanosarcina mazei Göl reconstituted in ether lipid liposomes
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanosarcina mazei Göl reconstituted in ether lipid liposomes. Eur. J. Biochem. 239:857-864.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 857-864
    • Lienard, T.1    Becher, B.2    Marschall, M.3    Bowien, S.4    Gottschalk, G.5
  • 38
    • 0002328698 scopus 로고
    • The acetyl-CoA pathway and the chemiosmotic generation of ATP during acetogenesis
    • H. L. Drake (ed.). Chapman & Hall, New York, N.Y.
    • Ljungdahl, L. G. 1994. The acetyl-CoA pathway and the chemiosmotic generation of ATP during acetogenesis, p. 63-87. In H. L. Drake (ed.), Acetogenesis. Chapman & Hall, New York, N.Y.
    • (1994) Acetogenesis , pp. 63-87
    • Ljungdahl, L.G.1
  • 39
    • 0022526191 scopus 로고
    • The autotrophic pathway of acetate synthesis in acetogenic bacteria
    • Ljungdahl, L. G. 1986. The autotrophic pathway of acetate synthesis in acetogenic bacteria. Annu. Rev. Microbiol. 40:415-450.
    • (1986) Annu. Rev. Microbiol. , vol.40 , pp. 415-450
    • Ljungdahl, L.G.1
  • 41
    • 0025955510 scopus 로고
    • Differential gene expression from the Escherichia coli atp operon mediated by segmental differences in mRNA stability
    • McCarthy, J. E., B. Gerstel, B. Surin, U. Wiedemann, and P. Ziemke. 1991. Differential gene expression from the Escherichia coli atp operon mediated by segmental differences in mRNA stability. Mol. Microbiol. 10:2447-2458.
    • (1991) Mol. Microbiol. , vol.10 , pp. 2447-2458
    • McCarthy, J.E.1    Gerstel, B.2    Surin, B.3    Wiedemann, U.4    Ziemke, P.5
  • 42
    • 0022021846 scopus 로고
    • Translational initiation frequency of atp genes from Escherichia coli: Identification of an intercistronic sequence that enhances translation
    • McCarthy, J. E., H. U. Schairer, and W. Sebald. 1985. Translational initiation frequency of atp genes from Escherichia coli: identification of an intercistronic sequence that enhances translation. EMBO J. 4:519-526.
    • (1985) EMBO J. , vol.4 , pp. 519-526
    • McCarthy, J.E.1    Schairer, H.U.2    Sebald, W.3
  • 43
    • 84992540924 scopus 로고    scopus 로고
    • Bacterial fermentation
    • Macmillan, London, United Kingdom
    • Müller, V. 2001. Bacterial fermentation. In Encyclopedia of life sciences. [Online.] Macmillan, London, United Kingdom. http://www.els.net.
    • (2001) Encyclopedia of Life Sciences. [Online]
    • Müller, V.1
  • 45
    • 0001203042 scopus 로고
    • Bioenergetics of methanogenesis
    • J. G. Ferry (ed.). Chapman & Hall, New York, N.Y.
    • Müller, V., M. Blaut, and G. Gottschalk. 1993. Bioenergetics of methanogenesis, p. 360-406. In J. G. Ferry (ed.), Methanogenesis. Chapman & Hall, New York, N.Y.
    • (1993) Methanogenesis , pp. 360-406
    • Müller, V.1    Blaut, M.2    Gottschalk, G.3
  • 46
    • 0000317411 scopus 로고
    • The sodium ion cycle in acetogenic and methanogenic bacteria: Generation and utilization of a primary electrochemical sodium ion gradient
    • H. L. Drake (ed.). Chapman & Hall, New York, N.Y.
    • Müller, V., and G. Gottschalk. 1994. The sodium ion cycle in acetogenic and methanogenic bacteria: generation and utilization of a primary electrochemical sodium ion gradient, p. 127-156. In H. L. Drake (ed.), Acetogenesis. Chapman & Hall, New York, N.Y.
    • (1994) Acetogenesis , pp. 127-156
    • Müller, V.1    Gottschalk, G.2
  • 47
    • 0037955289 scopus 로고    scopus 로고
    • ATP synthases: Structure, function and evolution of unique energy converters
    • Müller, V., and G. Grüber. 2003. ATP synthases: structure, function and evolution of unique energy converters. Cell. Mol. Life Sci. 60:474-494.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 474-494
    • Müller, V.1    Grüber, G.2
  • 50
    • 0026787745 scopus 로고
    • Structural conservation and functional diversity of V-ATPases
    • Nelson, N. 1992. Structural conservation and functional diversity of V-ATPases. J. Bioenerg. Biomembr. 24:407-414.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 407-414
    • Nelson, N.1
  • 51
    • 0344279652 scopus 로고
    • Generation of an electrochemical proton gradient in Streptococcus cremoris by lactate efflux
    • Otto, R., A. S. M. Sonnenberg, H. Veldkamp, and W. N. Konings. 1980. Generation of an electrochemical proton gradient in Streptococcus cremoris by lactate efflux. Proc. Natl. Acad. Sci. USA 77:5502-5506.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5502-5506
    • Otto, R.1    Sonnenberg, A.S.M.2    Veldkamp, H.3    Konings, W.N.4
  • 52
    • 0000971863 scopus 로고
    • The anaerobic way of life
    • A. Balows, H. G. Trüper, M. Dworkin, W. Harder, and K. H. Schleifer (ed.). Springer Verlag, Berlin, Germany
    • Peinemann, S., and G. Gottschalk. 1992. The anaerobic way of life, p. 300-311. In A. Balows, H. G. Trüper, M. Dworkin, W. Harder, and K. H. Schleifer (ed.), The prokaryotes. Springer Verlag, Berlin, Germany.
    • (1992) The Prokaryotes , pp. 300-311
    • Peinemann, S.1    Gottschalk, G.2
  • 53
    • 0019806869 scopus 로고
    • Sodium dependence of growth and methane formation in Methanobacterium thermoautotrophicum
    • Perski, H. J., J. Moll, and R. K. Thauer. 1981. Sodium dependence of growth and methane formation in Methanobacterium thermoautotrophicum. Arch. Microbiol. 130:319-321.
    • (1981) Arch. Microbiol. , vol.130 , pp. 319-321
    • Perski, H.J.1    Moll, J.2    Thauer, R.K.3
  • 54
    • 0001580628 scopus 로고
    • Sodium dependence of methane formation in methanogenic bacteria
    • Perski, H. J., P. Schönheit, and R. K. Thauer. 1982. Sodium dependence of methane formation in methanogenic bacteria. FEBS Lett. 143:323-326.
    • (1982) FEBS Lett. , vol.143 , pp. 323-326
    • Perski, H.J.1    Schönheit, P.2    Thauer, R.K.3
  • 56
    • 0001689934 scopus 로고    scopus 로고
    • Ni containing carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Ragsdale, S. W., and M. Kumar. 1996. Ni containing carbon monoxide dehydrogenase/acetyl-CoA synthase. Chem. Rev. 96:2515-2539.
    • (1996) Chem. Rev. , vol.96 , pp. 2515-2539
    • Ragsdale, S.W.1    Kumar, M.2
  • 57
    • 0021527029 scopus 로고
    • Hydrogenase from Acetobacterium woodii
    • Ragsdale, S. W., and L. G. Ljungdahl. 1984. Hydrogenase from Acetobacterium woodii. Arch. Microbiol. 139:361-365.
    • (1984) Arch. Microbiol. , vol.139 , pp. 361-365
    • Ragsdale, S.W.1    Ljungdahl, L.G.2
  • 58
    • 0033607683 scopus 로고    scopus 로고
    • 0-ATPase operon from Acetobacterium woodii. Operon structure and presence of multiple copies of atpE which encode proteolipids of 8- and 18-kDa
    • 0-ATPase operon from Acetobacterium woodii. Operon structure and presence of multiple copies of atpE which encode proteolipids of 8- and 18-kDa. J. Biol. Chem. 274:33999-34004.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33999-34004
    • Rahlfs, S.1    Aufurth, S.2    Müller, V.3
  • 60
    • 0342617520 scopus 로고    scopus 로고
    • - specificity as revealed by sequence comparisons
    • - specificity as revealed by sequence comparisons. FEBS Lett. 404:269-271.
    • (1997) FEBS Lett. , vol.404 , pp. 269-271
    • Rahlfs, S.1    Müller, V.2
  • 64
    • 0035808978 scopus 로고    scopus 로고
    • 0 ATPase from the cytoplasmic membrane of methanogenic archaea by chloroform/methanol and characterization of subunit c of Methanothermobacter thermoautotrophicus as a 16-kDa proteolipid
    • 0 ATPase from the cytoplasmic membrane of methanogenic archaea by chloroform/methanol and characterization of subunit c of Methanothermobacter thermoautotrophicus as a 16-kDa proteolipid. FEMS Microbiol. Lett. 195:47-51.
    • (2001) FEMS Microbiol. Lett. , vol.195 , pp. 47-51
    • Ruppert, C.1    Schmid, R.2    Hedderich, R.3    Müller, V.4
  • 65
    • 0031595840 scopus 로고    scopus 로고
    • 0 ATPase from Methanosarcina mazei: Cloning of the 5′ endof the aha operon encoding the membrane domain and expression of the proteolipid in a membrane-bound form in Escherichia coli
    • 0 ATPase from Methanosarcina mazei: cloning of the 5′ endof the aha operon encoding the membrane domain and expression of the proteolipid in a membrane-bound form in Escherichia coli. J. Bacteriol. 180:3448-3452.
    • (1998) J. Bacteriol. , vol.180 , pp. 3448-3452
    • Ruppert, C.1    Wimmers, S.2    Lemker, T.3    Müller, V.4
  • 68
    • 0027143972 scopus 로고
    • Nitrate as a preferred electron sink for the acetogen Clostridium thermoaceticum
    • Seifritz, C., S. L. Daniel, A. Gossner, and H. L. Drake. 1993. Nitrate as a preferred electron sink for the acetogen Clostridium thermoaceticum. J. Bacteriol. 175:8008-8013.
    • (1993) J. Bacteriol. , vol.175 , pp. 8008-8013
    • Seifritz, C.1    Daniel, S.L.2    Gossner, A.3    Drake, H.L.4
  • 69
    • 0033522371 scopus 로고    scopus 로고
    • Mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein catalyzed by the methyltransferase from Clostridium thermoaceticum: A key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis
    • Seravalli, J., S. Zhao, and S. W. Ragsdale. 1999. Mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein catalyzed by the methyltransferase from Clostridium thermoaceticum: a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis. Biochemistry 38:5728-5735.
    • (1999) Biochemistry , vol.38 , pp. 5728-5735
    • Seravalli, J.1    Zhao, S.2    Ragsdale, S.W.3
  • 72
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., A. G. Leslie, and J. E. Walker. 1999. Molecular architecture of the rotary motor in ATP synthase. Science 286:1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 73
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., K. Jungermann, and K. Decker. 1977. Energy conservation in chemotrophic anaerobic bacteria. Bacteriol. Rev. 41:100-180.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 74
    • 0021350907 scopus 로고
    • Growth yield increase linked to caffeate reduction in Acetobacterium woodii
    • Tschech, A., and N. Pfennig. 1984. Growth yield increase linked to caffeate reduction in Acetobacterium woodii. Arch. Microbiol. 137:163-167.
    • (1984) Arch. Microbiol. , vol.137 , pp. 163-167
    • Tschech, A.1    Pfennig, N.2
  • 76
    • 0026101873 scopus 로고
    • Thermodynamics of methylenetetrahydrofolate reduction to methyltetrahydrofolate and its implications for the energy metabolism of homoacetogenic bacteria
    • Wohlfarth, G., and G. Diekert. 1991. Thermodynamics of methylenetetrahydrofolate reduction to methyltetrahydrofolate and its implications for the energy metabolism of homoacetogenic bacteria. Arch. Microbiol. 155:378-381.
    • (1991) Arch. Microbiol. , vol.155 , pp. 378-381
    • Wohlfarth, G.1    Diekert, G.2
  • 78
    • 0025017689 scopus 로고
    • Differential effects of sodium on hydrogen- and glucose-dependent growth of the acetogenic bacterium Acetogenium kivui
    • Yang, H., and H. L. Drake. 1990. Differential effects of sodium on hydrogen- and glucose-dependent growth of the acetogenic bacterium Acetogenium kivui. Appl. Environ. Microbiol. 56:81-86.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 81-86
    • Yang, H.1    Drake, H.L.2
  • 80
    • 0028800799 scopus 로고
    • +-transporting ATP synthase by directed mutagenesis of subunit c
    • +-transporting ATP synthase by directed mutagenesis of subunit c. J. Biol. Chem. 270:87-93.
    • (1995) J. Biol. Chem. , vol.270 , pp. 87-93
    • Zhang, Y.1    Fillingame, R.H.2


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