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Volumn 41, Issue 1, 2013, Pages 421-426

Evolution of Na+ and H+ bioenergetics in methanogenic archaea

Author keywords

ATP synthase; Ferredoxin: heterodisulfide oxidoreductase; Methyltransferase; Proton potential; Rnf; Sodium potential

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOCHROME; HYDROGEN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SODIUM ION;

EID: 84873138724     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120294     Document Type: Conference Paper
Times cited : (37)

References (49)
  • 1
    • 0026619677 scopus 로고
    • Biochemistry of methanogenesis
    • Wolfe, R. S. (1992) Biochemistry of methanogenesis. Biochem. Soc. Symp. 58, 41-49
    • (1992) Biochem. Soc. Symp. , vol.58 , pp. 41-49
    • Wolfe, R.S.1
  • 2
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer, R. K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144, 2377-2406
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 3
    • 44449149379 scopus 로고    scopus 로고
    • Life close to the thermodynamic limit: How methanogenic archaea conserve energy
    • Deppenmeier, U. and Müller, V. (2008) Life close to the thermodynamic limit: how methanogenic archaea conserve energy. Results Probl. Cell. Differ. 45, 123-152
    • (2008) Results Probl. Cell. Differ. , vol.45 , pp. 123-152
    • Deppenmeier, U.1    Müller, V.2
  • 4
    • 47549119041 scopus 로고    scopus 로고
    • Methanogenic archaea: Ecologically relevant differences in energy conservation
    • Thauer, R. K., Kaster, A. K., Seedorf, H., Buckel, W. and Hedderich, R. (2008) Methanogenic archaea: ecologically relevant differences in energy conservation. Nat. Rev. Microbiol. 6, 579-591
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 579-591
    • Thauer, R.K.1    Kaster, A.K.2    Seedorf, H.3    Buckel, W.4    Hedderich, R.5
  • 5
    • 0021763540 scopus 로고
    • Coupling of ATP synthesis and methane formation from methanol and molecular hydrogen in Methanosarcina barkeri
    • Blaut, M. and Gottschalk, G. (1984) Coupling of ATP synthesis and methane formation from methanol and molecular hydrogen in Methanosarcina barkeri. Eur. J. Biochem. 141, 217-222
    • (1984) Eur. J. Biochem. , vol.141 , pp. 217-222
    • Blaut, M.1    Gottschalk, G.2
  • 6
    • 0035342616 scopus 로고    scopus 로고
    • +-translocating methyltransferase complex from methanogenic archaea
    • DOI 10.1016/S0005-2728(00)00274-7, PII S0005272800002747
    • +-translocating methyltransferase complex from methanogenic archaea. Biochim. Biophys. Acta 1505, 28-36 (Pubitemid 32204456)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.1 , pp. 28-36
    • Gottschalk, G.1    Thauer, R.K.2
  • 8
    • 0024289450 scopus 로고
    • Electron-transport-driven sodium extrusion during the methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri
    • Müller, V., Winner, C. and Gottschalk, G. (1988) Electron-transport-driven sodium extrusion during the methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri. Eur. J. Biochem. 178, 519-525
    • (1988) Eur. J. Biochem. , vol.178 , pp. 519-525
    • Müller, V.1    Winner, C.2    Gottschalk, G.3
  • 9
    • 0029956986 scopus 로고    scopus 로고
    • 5-methyltetrahydromethanopterin: coenzyme M methyltransferase from methanosarcina mazei Go1 reconstituted in ether lipid liposomes
    • Lienard, T., Becher, B., Marschall, M., Bowien, S. and Gottschalk, G. (1996) Sodium ion translocation by N5-methyltetrahydromethanopterin: coenzyme M methyltransferase from Methanosarcina mazei Gö1 reconstituted in ether lipid liposomes. Eur. J. Biochem. 239, 857-864 (Pubitemid 26253064)
    • (1996) European Journal of Biochemistry , vol.239 , Issue.3 , pp. 857-864
    • Lienard, T.1    Becher, B.2    Marschall, M.3    Bowien, S.4    Gottschalk, G.5
  • 10
    • 0036709867 scopus 로고    scopus 로고
    • Redox-driven proton translocation in methanogenic archaea
    • Deppenmeier, U. (2002) Redox-driven proton translocation in methanogenic archaea. Cell. Mol. Life Sci. 59, 1-21
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1-21
    • Deppenmeier, U.1
  • 12
    • 79952588675 scopus 로고    scopus 로고
    • Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
    • Kaster, A. K., Moll, J., Parey, K. and Thauer, R. K. (2011) Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc. Natl. Acad. Sci. U. S. A. 108, 2981-2986
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2981-2986
    • Kaster, A.K.1    Moll, J.2    Parey, K.3    Thauer, R.K.4
  • 13
    • 0031921345 scopus 로고    scopus 로고
    • Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1
    • Abken, H. J., Tietze, M., Brodersen, J., Baumer, S., Beifuss, U. and Deppenmeier, U. (1998) Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1. J. Bacteriol. 180, 2027-2032 (Pubitemid 28212686)
    • (1998) Journal of Bacteriology , vol.180 , Issue.8 , pp. 2027-2032
    • Abken, H.-J.1    Tietze, M.2    Brodersen, J.3    Baumer, S.4    Beifuss, U.5    Deppenmeier, U.6
  • 15
    • 11144347500 scopus 로고    scopus 로고
    • The membrane-bound electron transport system of methanosarcina species
    • DOI 10.1023/B:JOBB.0000019598.64642.97
    • Deppenmeier, U. (2004) The membrane-bound electron transport system of Methanosarcina species. J. Bioenerg. Biomembr. 36, 55-64 (Pubitemid 38500760)
    • (2004) Journal of Bioenergetics and Biomembranes , vol.36 , Issue.1 , pp. 55-64
    • Deppenmeier, U.1
  • 16
    • 0032586857 scopus 로고    scopus 로고
    • 2:heterodisulfide oxidoreductase from Methanosarcina mazei Go1: Identification of two proton-translocating segments
    • 2:heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: identification of two proton-translocating segments. J. Bacteriol. 181, 4076-4080 (Pubitemid 29295927)
    • (1999) Journal of Bacteriology , vol.181 , Issue.13 , pp. 4076-4080
    • Ide, T.1    Baumer, S.2    Deppenmeier, U.3
  • 17
    • 41349089084 scopus 로고    scopus 로고
    • Methanogenesis in marine sediments
    • DOI 10.1196/annals.1419.007, Incredible Anaerobes From Physiology to Genomics to Fuels
    • Ferry, J. G. and Lessner, D. J. (2008) Methanogenesis in marine sediments. Ann. N. Y. Acad. Sci. 1125, 147-157 (Pubitemid 351451153)
    • (2008) Annals of the New York Academy of Sciences , vol.1125 , pp. 147-157
    • Ferry, J.G.1    Lessner, D.J.2
  • 19
    • 2142697116 scopus 로고    scopus 로고
    • Energy-Converting [NiFe] Hydrogenases from Archaea and Extremophiles: Ancestors of Complex I
    • DOI 10.1023/B:JOBB.0000019599.43969.33
    • Hedderich, R. (2004) Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. J. Bioenerg. Biomembr. 36, 65-75 (Pubitemid 38500761)
    • (2004) Journal of Bioenergetics and Biomembranes , vol.36 , Issue.1 , pp. 65-75
    • Hedderich, R.1
  • 20
    • 77955246393 scopus 로고    scopus 로고
    • Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei
    • Welte, C., Krätzer, C. and Deppenmeier, U. (2010) Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei. FEBS J. 277, 3396-3403
    • (2010) FEBS J. , vol.277 , pp. 3396-3403
    • Welte, C.1    Krätzer, C.2    Deppenmeier, U.3
  • 21
    • 79951579402 scopus 로고    scopus 로고
    • Biochemistry, evolution and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes
    • Biegel, E., Schmidt, S., González, J. M. and Müller, V. (2011) Biochemistry, evolution and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes. Cell. Mol. Life Sci. 68, 613-634
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 613-634
    • Biegel, E.1    Schmidt, S.2    González, J.M.3    Müller, V.4
  • 23
    • 84870499112 scopus 로고    scopus 로고
    • Electron transport during aceticlastic methanogenesis by Methanosarcina acetivorans involves a sodium-translocating Rnf complex
    • Schlegel, K., Welte, C., Deppenmeier, U. and Müller, V. (2012) Electron transport during aceticlastic methanogenesis by Methanosarcina acetivorans involves a sodium-translocating Rnf complex. FEBS J. 279, 4444-4452
    • (2012) FEBS J. , vol.279 , pp. 4444-4452
    • Schlegel, K.1    Welte, C.2    Deppenmeier, U.3    Müller, V.4
  • 24
    • 4944246136 scopus 로고    scopus 로고
    • +/ATP coupling ratio
    • DOI 10.1016/j.febslet.2004.08.065, PII S0014579304010841
    • +/ATP stoichiometry. FEBS Lett. 576, 1-4 (Pubitemid 39330446)
    • (2004) FEBS Letters , vol.576 , Issue.1-2 , pp. 1-4
    • Cross, R.L.1    Muller, V.2
  • 26
    • 0037955289 scopus 로고    scopus 로고
    • ATP synthases: Structure, function and evolution of unique energy converters
    • DOI 10.1007/s000180300040
    • Müller, V. and Grüber, G. (2003) ATP synthases: structure, function and evolution of unique energy converters. Cell. Mol. Life Sci. 60, 474-494 (Pubitemid 36459527)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.3 , pp. 474-494
    • Muller, V.1    Gruber, G.2
  • 27
    • 65649105054 scopus 로고    scopus 로고
    • o ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy
    • o ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy. J. Biol. Chem. 284, 10110-10119
    • (2009) J. Biol. Chem. , vol.284 , pp. 10110-10119
    • Vonck, J.1    Pisa, K.Y.2    Morgner, N.3    Brutschy, B.4    Müller, V.5
  • 32
  • 33
    • 2542487925 scopus 로고    scopus 로고
    • 0 ATPases: From Multimeric to Monomeric Rotors Comprising 6-13 Ion Binding Sites
    • DOI 10.1023/B:JOBB.0000019603.68282.04
    • o ATPases: from multimeric to monomeric rotors comprising 6-13 ion binding sites. J. Bioenerg. Biomembr. 36, 115-125 (Pubitemid 38500765)
    • (2004) Journal of Bioenergetics and Biomembranes , vol.36 , Issue.1 , pp. 115-125
    • Mulller, V.1
  • 35
    • 70349828967 scopus 로고    scopus 로고
    • High-resolution structure of the rotor ring of a proton-dependent ATP synthase
    • Pogoryelov, D., Yildiz, O., Faraldo-Gómez, J. D. and Meier, T. (2009) High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat. Struct. Mol. Biol. 16, 1068-1073
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1068-1073
    • Pogoryelov, D.1    Yildiz, O.2    Faraldo-Gómez, J.D.3    Meier, T.4
  • 38
    • 0018239622 scopus 로고
    • Evidence for ATP synthesis driven by a proton gradient in Methanosarcina barkeri
    • Mountfort, D. O. (1978) Evidence for ATP synthesis driven by a proton gradient in Methanosarcina barkeri. Biochem. Biophys. Res. Commun. 85, 1346-1350
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 1346-1350
    • Mountfort, D.O.1
  • 39
    • 0001580628 scopus 로고
    • Sodium dependence of methane formation in methanogenic bacteria
    • Perski, H. J., Schönheit, P. and Thauer, R. K. (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
  • 41
    • 0024264942 scopus 로고
    • +-driven ATP synthesis in Methanobacterium thermoautotrophicum can be modulated with sodium ion concentrations in the growth medium
    • DOI 10.1016/0014-5793(88)80990-6
    • +-driven ATP synthesis in Methanobacterium thermoautotrophicum can be modulated with sodium ion concentrations in the growth medium. FEBS Lett. 242, 85-88 (Pubitemid 19012253)
    • (1988) FEBS Letters , vol.242 , Issue.1 , pp. 85-88
    • Smigan, P.1    Horovska, L.2    Greksak, M.3
  • 45
    • 55749086840 scopus 로고    scopus 로고
    • Mutations alter the sodium versus proton use of a Bacillus clausii flagellar motor and confer dual ion use on Bacillus subtilis motors
    • Terahara, N., Krulwich, T. A. and Ito, M. (2008) Mutations alter the sodium versus proton use of a Bacillus clausii flagellar motor and confer dual ion use on Bacillus subtilis motors. Proc. Natl. Acad. Sci. U. S. A. 105, 14359-14364
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14359-14364
    • Terahara, N.1    Krulwich, T.A.2    Ito, M.3
  • 47
    • 0028803285 scopus 로고
    • Cation-selectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: Dependence on the environment in which the proteins are expressed
    • Tolner, B., Ubbink-Kok, T., Poolman, B. and Konings, W. N. (1995) Cation-selectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: dependence on the environment in which the proteins are expressed. Mol. Microbiol. 18, 123-133
    • (1995) Mol. Microbiol. , vol.18 , pp. 123-133
    • Tolner, B.1    Ubbink-Kok, T.2    Poolman, B.3    Konings, W.N.4
  • 48
    • 84866550896 scopus 로고    scopus 로고
    • Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic methanogenesis
    • Lie, T. J., Costa, K. C., Lupa, B., Korpole, S., Whitman, W. B. and Leigh, J. A. (2012) Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic methanogenesis. Proc. Natl. Acad. Sci. U. S. A. 109, 15473-15478
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 15473-15478
    • Lie, T.J.1    Costa, K.C.2    Lupa, B.3    Korpole, S.4    Whitman, W.B.5    Leigh, J.A.6
  • 49


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