메뉴 건너뛰기




Volumn 59, Issue 9, 2002, Pages 1513-1533

Redox-driven proton translocation in methanogenic archaea

Author keywords

Energy transduction; F420H2 dehydrogenase; Heterodisulfide reductase; Hydrogenase; Methanogens; NADH dehydrogenase; Proton translocation; Respiratory chain

Indexed keywords

BACTERIAL MEMBRANE; BIOCHEMISTRY; DISULFIDE BOND; ELECTROCHEMICAL ANALYSIS; ELECTRON TRANSPORT; ENERGY METABOLISM; ENERGY TRANSFER; ENZYME BINDING; EUKARYOSIS; MEMBRANE BINDING; METHANOBACTERIUM; METHANOSARCINA; METHYLATION; MITOCHONDRIAL RESPIRATION; NONHUMAN; OXIDATION REDUCTION REACTION; PROTON TRANSPORT; REVIEW; SPECIES DIFFERENTIATION;

EID: 0036709867     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-002-8526-3     Document Type: Review
Times cited : (70)

References (112)
  • 1
    • 0033867966 scopus 로고    scopus 로고
    • Taxonomy, phylogenetic and ecological diversity of methanogenic Archaea
    • Garcia J. L., Patel B. K. C. and Ollivier B. (2000) Taxonomy, phylogenetic and ecological diversity of methanogenic Archaea. Anaerobe 6: 205-226
    • (2000) Anaerobe , vol.6 , pp. 205-226
    • Garcia, J.L.1    Patel, B.K.C.2    Ollivier, B.3
  • 2
    • 0030871461 scopus 로고    scopus 로고
    • Energetics of syntrophic cooperation in methanogenic degradation
    • Schink B. (1997) Energetics of syntrophic cooperation in methanogenic degradation. Microbiol. Mol. Biol. Rev. 61: 262-280
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 262-280
    • Schink, B.1
  • 3
    • 0031716660 scopus 로고    scopus 로고
    • Molecular methods for the study of methanotroph ecology
    • Murrell J. C., McDonald I. R. and Bourne D. G. (1998) Molecular methods for the study of methanotroph ecology. FEMS Microbiol. Ecol. 27: 103-114
    • (1998) FEMS Microbiol. Ecol. , vol.27 , pp. 103-114
    • Murrell, J.C.1    McDonald, I.R.2    Bourne, D.G.3
  • 4
    • 0027934272 scopus 로고
    • Global emission of methane during the last several centuries
    • Khalil M. A. K. and Rasmussen R. A. (1994) Global emission of methane during the last several centuries. Chemosphere 29: 833-842
    • (1994) Chemosphere , vol.29 , pp. 833-842
    • Khalil, M.A.K.1    Rasmussen, R.A.2
  • 5
    • 0039864615 scopus 로고    scopus 로고
    • Ruminants and environment: Methanogenesis
    • Demeyer D. and Fievez V. (2000) Ruminants and environment: Methanogenesis. Ann. Zootechnie 49: 95-112
    • (2000) Ann. Zootechnie , vol.49 , pp. 95-112
    • Demeyer, D.1    Fievez, V.2
  • 6
    • 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
  • 7
    • 0032883772 scopus 로고    scopus 로고
    • Novel reactions involved in energy conservation by methanogenic archaea
    • Deppenmeier U., Lienard T. and Gottschalk G. (1999) Novel reactions involved in energy conservation by methanogenic archaea. FEBS Lett. 457: 291-297
    • (1999) FEBS Lett. , vol.457 , pp. 291-297
    • Deppenmeier, U.1    Lienard, T.2    Gottschalk, G.3
  • 8
    • 0022387752 scopus 로고
    • Unusual coenzymes of methanogenesis
    • Wolfe R. S. (1985) Unusual coenzymes of methanogenesis. TIBS 10: 396-399
    • (1985) TIBS , vol.10 , pp. 396-399
    • Wolfe, R.S.1
  • 9
    • 0002806157 scopus 로고
    • Diversity and taxonomy of methanogens
    • Ferry J. G. (ed.), Chapman and Hall, New York
    • Boone D. R., Whitman W. B. and Rouviere P. E. (1993) Diversity and taxonomy of methanogens. In: Methanogenesis, pp. 35-80, Ferry J. G. (ed.), Chapman and Hall, New York
    • (1993) Methanogenesis , pp. 35-80
    • Boone, D.R.1    Whitman, W.B.2    Rouviere, P.E.3
  • 11
    • 0026494662 scopus 로고
    • Energetics of methanogenesis in vesicular systems
    • Blaut M., Müller V. and Gottschalk G. (1992) Energetics of methanogenesis in vesicular systems. J. Bioenerg. Biomemb. 24: 529-546
    • (1992) J. Bioenerg. Biomemb. , vol.24 , pp. 529-546
    • Blaut, M.1    Müller, V.2    Gottschalk, G.3
  • 12
    • 0001780722 scopus 로고
    • Conversion of methanol and methylamines to methane amd carbon dioxide
    • Ferry J. G. (ed.), Chapman and Hall, New York
    • Keltjens J. T and Vogels G. D. (1993) Conversion of methanol and methylamines to methane amd carbon dioxide. In: Methanogenesis, pp. 209-252, Ferry J. G. (ed.), Chapman and Hall, New York
    • (1993) Methanogenesis , pp. 209-252
    • Keltjens, J.T.1    Vogels, G.D.2
  • 13
    • 0000537597 scopus 로고
    • Naturally occuring 5-deazaflavin coenzymes: Biological redox roles
    • Walsh C. (1986) Naturally occuring 5-deazaflavin coenzymes: Biological redox roles. Acc. Chem. Res. 19: 216-221
    • (1986) Acc. Chem. Res. , vol.19 , pp. 216-221
    • Walsh, C.1
  • 14
    • 0031921345 scopus 로고    scopus 로고
    • Isolation and characterization of methanophenazine and the function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1
    • Abken H.-J., Tietze M., Brodersen J., Bäumer S., Beifuss U. and Deppenmeier U. (1998) Isolation and characterization of methanophenazine and the function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1. J. Bacteriol. 180: 2027-2032
    • (1998) J. Bacteriol. , vol.180 , pp. 2027-2032
    • Abken, H.-J.1    Tietze, M.2    Brodersen, J.3    Bäumer, S.4    Beifuss, U.5    Deppenmeier, U.6
  • 16
    • 0005116849 scopus 로고    scopus 로고
    • Ech hydrogenase has important functions in the metabolism of Methanosarcina barkeri growing on different substrates
    • Meuer J., Kuettner H. G., Metcalf W. W and Hedderich H. (2001) Ech hydrogenase has important functions in the metabolism of Methanosarcina barkeri growing on different substrates. Biospektrum; special issue, 88
    • (2001) Biospektrum , Issue.SPEC. ISSUE , pp. 88
    • Meuer, J.1    Kuettner, H.G.2    Metcalf, W.W.3    Hedderich, H.4
  • 17
    • 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
  • 18
    • 0005194997 scopus 로고    scopus 로고
    • Structure and function of the nickel enzyme methyl-coenzyme M reductase
    • Thauer R. K. (1999) Structure and function of the nickel enzyme methyl-coenzyme M reductase. J. Inorg. Biochem. 74: 54-54
    • (1999) J. Inorg. Biochem. , vol.74 , pp. 54
    • Thauer, R.K.1
  • 19
    • 0001203042 scopus 로고
    • Bioenergetics of methanogenesis
    • Ferry J. G. (ed.), Chapman and Hall, New York
    • Müller V., Blaut M. and Gottschalk G. (1993) Bioenergetics of methanogenesis. In: Methanogenesis, pp. 360-406, Ferry J. G. (ed.), Chapman and Hall, New York
    • (1993) Methanogenesis , pp. 360-406
    • Müller, V.1    Blaut, M.2    Gottschalk, G.3
  • 21
    • 0030838597 scopus 로고    scopus 로고
    • Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila
    • Ferry J. G. (1997) Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila. Biofactors 6: 25-35
    • (1997) Biofactors , vol.6 , pp. 25-35
    • Ferry, J.G.1
  • 22
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic Archaea
    • Deppenmeier U., Müller V. and Gottschalk G. (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
  • 24
  • 25
    • 0026788551 scopus 로고
    • Energy transduction in the methanogen Methanococcus voltae is based on a sodium ion current
    • Dybas M. and Konisky J. (1992) Energy transduction in the methanogen Methanococcus voltae is based on a sodium ion current. J. Bacteriol. 174: 5575-5583
    • (1992) J. Bacteriol. , vol.174 , pp. 5575-5583
    • Dybas, M.1    Konisky, J.2
  • 27
    • 0025189332 scopus 로고
    • 2-dependent heterodisulfide reductase in methanogenic bacterium strain Gö1 and Methanolobus tindarius
    • 2-dependent heterodisulfide reductase in methanogenic bacterium strain Gö1 and Methanolobus tindarius. FEBS Lett. 261: 199-203
    • (1990) FEBS Lett. , vol.261 , pp. 199-203
    • Deppenmeier, U.1    Blaut, M.2    Mahlmann, A.3    Gottschalk, G.4
  • 28
    • 0023932844 scopus 로고
    • Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetategrown Methanosarcina thermophila
    • Terlesky K. C. and Ferry J. G. (1988) Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetategrown Methanosarcina thermophila. J. Biol. Chem. 263: 4075-4079
    • (1988) J. Biol. Chem. , vol.263 , pp. 4075-4079
    • Terlesky, K.C.1    Ferry, J.G.2
  • 29
    • 0023276124 scopus 로고
    • Immunoelectron microscopic demonstration of ATPase on the cytoplasmic membrane of the methanogenic bacterium strain Gö1
    • Mayer F., Jussofie A., Salzmann M., Lübben M., Rohde M. and Gottschalk G. (1987) Immunoelectron microscopic demonstration of ATPase on the cytoplasmic membrane of the methanogenic bacterium strain Gö1. J. Bacteriol. 169: 2307-2309
    • (1987) J. Bacteriol. , vol.169 , pp. 2307-2309
    • Mayer, F.1    Jussofie, A.2    Salzmann, M.3    Lübben, M.4    Rohde, M.5    Gottschalk, G.6
  • 30
    • 0024204347 scopus 로고
    • A methyl-CoM methylreductase system from methanogenic bacterium strain Gö1 not requiring ATP for activity
    • Deppenmeier U., Blaut M., Jussofie A. and Gottschalk G. (1988) A methyl-CoM methylreductase system from methanogenic bacterium strain Gö1 not requiring ATP for activity. FEBS Lett. 241: 60-64
    • (1988) FEBS Lett. , vol.241 , pp. 60-64
    • Deppenmeier, U.1    Blaut, M.2    Jussofie, A.3    Gottschalk, G.4
  • 31
    • 0032586729 scopus 로고    scopus 로고
    • Structure and function of the A1Ao-ATPases from methanogenic archaea
    • Müller V., Ruppert C. and Lemker T. (1999) Structure and function of the A1Ao-ATPases from methanogenic archaea. J. Bioenerg. Biomembr. 31: 15-27
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 15-27
    • Müller, V.1    Ruppert, C.2    Lemker, T.3
  • 32
    • 0025979785 scopus 로고
    • 2: Heterodisulfide oxidoreductase, a second energy-conserving system in the methanogenic strain Gö 1
    • 2: Heterodisulfide oxidoreductase, a second energy-conserving system in the methanogenic strain Gö 1. Arch. Microbiol. 155: 272-277
    • (1991) Arch. Microbiol. , vol.155 , pp. 272-277
    • Deppenmeier, U.1    Blaut, M.2    Gottschalk, G.3
  • 33
    • 0034679503 scopus 로고    scopus 로고
    • Methanophenazine: Structure, total synthesis and function of a new cofactor from methanogenic archaea
    • Beifuss U., Tietze M., Bäumer S. and Deppenmeier U. (2000) Methanophenazine: Structure, total synthesis and function of a new cofactor from methanogenic archaea. Angew. Chem. Int. Ed. 39: 2470-2473
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 2470-2473
    • Beifuss, U.1    Tietze, M.2    Bäumer, S.3    Deppenmeier, U.4
  • 35
    • 0032586857 scopus 로고    scopus 로고
    • 2: Heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: Identification of two proton-translocating segments
    • 2: Heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: Identification of two proton-translocating segments. J. Bacteriol. 181: 4076-4080
    • (1999) J. Bacteriol. , vol.181 , pp. 4076-4080
    • Ide, T.1    Bäumer, S.2    Deppenmeier, U.3
  • 36
    • 0023194208 scopus 로고
    • Proton translocation coupled to methanogenesis from methanol + hydrogen in Methanosarcina barkeri
    • Blaut M., Müller V. and Gottschalk G. (1987) Proton translocation coupled to methanogenesis from methanol + hydrogen in Methanosarcina barkeri. FEBS Lett. 215: 53-57
    • (1987) FEBS Lett. , vol.215 , pp. 53-57
    • Blaut, M.1    Müller, V.2    Gottschalk, G.3
  • 37
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer J., Bartoschek S., Koch J., Künkel A. and Hedderich R. (1999) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 265: 325-335
    • (1999) Eur. J. Biochem. , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Künkel, A.4    Hedderich, R.5
  • 38
    • 0028130513 scopus 로고
    • Characterization of a CO: Heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila
    • Peer C. W., Painter M. H., Rasche M. E. and Ferry J. G. (1994) Characterization of a CO: Heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila. J. Bacteriol. 176: 6974-6979
    • (1994) J. Bacteriol. , vol.176 , pp. 6974-6979
    • Peer, C.W.1    Painter, M.H.2    Rasche, M.E.3    Ferry, J.G.4
  • 39
    • 0032521598 scopus 로고    scopus 로고
    • An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea
    • Künkel A., Vorholt J. A., Thauer R. K. and Hedderich R. (1998) An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea. Eur. J. Biochem. 252: 467-476
    • (1998) Eur. J. Biochem. , vol.252 , pp. 467-476
    • Künkel, A.1    Vorholt, J.A.2    Thauer, R.K.3    Hedderich, R.4
  • 41
    • 0028810413 scopus 로고
    • Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri
    • Michel R., Massanz C., Kostka S., Richter M. and Fiebig K. (1995) Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 233: 727-735
    • (1995) Eur. J. Biochem. , vol.233 , pp. 727-735
    • Michel, R.1    Massanz, C.2    Kostka, S.3    Richter, M.4    Fiebig, K.5
  • 42
    • 0025604784 scopus 로고
    • Conservation of primary structure in prokaryotic hydrogenases
    • Reeve J. N. and Beckler G. S. (1990) Conservation of primary structure in prokaryotic hydrogenases. FEMS Microbiol. Rev. 87: 419-424
    • (1990) FEMS Microbiol. Rev. , vol.87 , pp. 419-424
    • Reeve, J.N.1    Beckler, G.S.2
  • 44
    • 0028009865 scopus 로고
    • Purification and characterization of membrane-bound hydrogenase from Methanosarcina barkeri MS
    • Kemner J. M. and Zeikus J. G. (1994) Purification and characterization of membrane-bound hydrogenase from Methanosarcina barkeri MS. Arch. Microbiol. 161: 47-54
    • (1994) Arch. Microbiol. , vol.161 , pp. 47-54
    • Kemner, J.M.1    Zeikus, J.G.2
  • 45
    • 0028790975 scopus 로고
    • Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Gö 1
    • Deppenmeier U. (1995) Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Gö 1. Arch. Microbiol. 164: 370-376
    • (1995) Arch. Microbiol. , vol.164 , pp. 370-376
    • Deppenmeier, U.1
  • 46
    • 0028890441 scopus 로고
    • Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Gö 1, both encoding a membrane-bound hydrogenase and a cytochrome b
    • Deppenmeier U., Blaut M., Lentes S., Herzberg C. and Gottschalk G. (1995) Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Gö 1, both encoding a membrane-bound hydrogenase and a cytochrome b. Eur. J. Biochem. 227: 261-269
    • (1995) Eur. J. Biochem. , vol.227 , pp. 261-269
    • Deppenmeier, U.1    Blaut, M.2    Lentes, S.3    Herzberg, C.4    Gottschalk, G.5
  • 48
    • 0034099642 scopus 로고    scopus 로고
    • Membrane targeting and translocation of bacterial hydrogenases
    • Wu L. E, Chanal A. and Rodrigue A. (2000) Membrane targeting and translocation of bacterial hydrogenases. Arch. Microbiol. 173: 319-324
    • (2000) Arch. Microbiol. , vol.173 , pp. 319-324
    • Wu, L.E.1    Chanal, A.2    Rodrigue, A.3
  • 49
    • 0028785074 scopus 로고
    • Antigenic determinants of the membrane-bound hydrogenase in Alcaligenes eutrophus are exposed toward the periplasm
    • Eismann K., Mlejnek K., Zipprich D., Hoppert M., Gerberding H. and Mayer F. (1995) Antigenic determinants of the membrane-bound hydrogenase in Alcaligenes eutrophus are exposed toward the periplasm. J. Bacteriol. 177: 6309-6312
    • (1995) J. Bacteriol. , vol.177 , pp. 6309-6312
    • Eismann, K.1    Mlejnek, K.2    Zipprich, D.3    Hoppert, M.4    Gerberding, H.5    Mayer, F.6
  • 50
    • 0029764690 scopus 로고    scopus 로고
    • The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling
    • Bernhard M., Schwartz E., Rietdorf J. and Friedrich, B. (1996) The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling. J. Bacteriol. 178: 4522-4529
    • (1996) J. Bacteriol. , vol.178 , pp. 4522-4529
    • Bernhard, M.1    Schwartz, E.2    Rietdorf, J.3    Friedrich, B.4
  • 51
    • 0033555715 scopus 로고    scopus 로고
    • Inhibition of membrane-bound electron transport of the methanogenic archaeon Methanosarcina mazei Gö1 by diphenyleneiodonium
    • Brodersen J., Bäumer S., Abken H.-J., Gottschalk G. and Deppenmeier U. (1999) Inhibition of membrane-bound electron transport of the methanogenic archaeon Methanosarcina mazei Gö1 by diphenyleneiodonium. Eur. J. Biochem. 259: 218-224
    • (1999) Eur. J. Biochem. , vol.259 , pp. 218-224
    • Brodersen, J.1    Bäumer, S.2    Abken, H.-J.3    Gottschalk, G.4    Deppenmeier, U.5
  • 52
    • 0025187801 scopus 로고
    • Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum
    • Hedderich R., Berkessel A. and Thauer R. K. (1990) Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 193: 255-261
    • (1990) Eur. J. Biochem. , vol.193 , pp. 255-261
    • Hedderich, R.1    Berkessel, A.2    Thauer, R.K.3
  • 53
    • 0031055712 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoprotein
    • Künkel A., Vaupel M., Heim S., Thauer R. K. and Hedderich R. (1997) Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoprotein. Eur. J. Biochem. 244: 226-234
    • (1997) Eur. J. Biochem. , vol.244 , pp. 226-234
    • Künkel, A.1    Vaupel, M.2    Heim, S.3    Thauer, R.K.4    Hedderich, R.5
  • 54
    • 0032516483 scopus 로고    scopus 로고
    • Purification and properties of the heme and iron-sulfur containing heterodisulfide reductase from Methanosarcina thermophila
    • Simianu M., Murakami E., Brewer J. M. and Ragsdale S. W. (1998) Purification and properties of the heme and iron-sulfur containing heterodisulfide reductase from Methanosarcina thermophila. Biochemistry 37: 10027-10039
    • (1998) Biochemistry , vol.37 , pp. 10027-10039
    • Simianu, M.1    Murakami, E.2    Brewer, J.M.3    Ragsdale, S.W.4
  • 55
    • 0034858150 scopus 로고    scopus 로고
    • A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea
    • Madadi-Kahkesh S., Duin E. C., Heim S., Albracht S. P. J., Johnson M. K. and Hedderich R. (2001) A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. Eur. J. Biochem. 268: 2566-2577
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2566-2577
    • Madadi-Kahkesh, S.1    Duin, E.C.2    Heim, S.3    Albracht, S.P.J.4    Johnson, M.K.5    Hedderich, R.6
  • 56
    • 0035951806 scopus 로고    scopus 로고
    • Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophila
    • Murakami E., Deppenmeier U. and Ragsdale S. W. (2001) Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophila. J. Biol. Chem. 276: 2432-2439
    • (2001) J. Biol. Chem. , vol.276 , pp. 2432-2439
    • Murakami, E.1    Deppenmeier, U.2    Ragsdale, S.W.3
  • 59
    • 0030833398 scopus 로고    scopus 로고
    • 2 dehydrogenase from Methanosarcina mazei Gö1
    • 2 dehydrogenase from Methanosarcina mazei Gö1. FEMS Lett. 154: 231-237
    • (1997) FEMS Lett. , vol.154 , pp. 231-237
    • Abken, H.-J.1    Deppenmeier, U.2
  • 62
    • 0023245011 scopus 로고
    • A possible biochemical missing link among archaebacteria
    • Achenbach-Richter L., Stetter K. O. and Woese C. R. (1987) A possible biochemical missing link among archaebacteria. Nature 327: 348-349
    • (1987) Nature , vol.327 , pp. 348-349
    • Achenbach-Richter, L.1    Stetter, K.O.2    Woese, C.R.3
  • 65
    • 0031582715 scopus 로고    scopus 로고
    • Modular evolution of the respiratory NADH: Ubiquinone oxidoreductase and the origin of its modules
    • Friedrich T. and Weiss H. (1997) Modular evolution of the respiratory NADH: Ubiquinone oxidoreductase and the origin of its modules. J. Theor. Biol. 187: 529-540
    • (1997) J. Theor. Biol. , vol.187 , pp. 529-540
    • Friedrich, T.1    Weiss, H.2
  • 66
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH: Ubiquinone oxidoreductase in Escherichia coli: Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    • Weidner U., Geier S., Ptock A., Friedrich T, Leif H. and Weiss, H. (1993) The gene locus of the proton-translocating NADH: Ubiquinone oxidoreductase in Escherichia coli: Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J. Mol. Biol. 233: 109-122
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 68
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk H. P., Clayton R. A., Tomb J. F., White O., Nelson K. A., Ketchum K. A. et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.A.5    Ketchum, K.A.6
  • 69
    • 0031041453 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8
    • Yano T., Chu S. S., Sled V. D., Ohnishi T. and Yagi T. (1997) The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. J. Biol. Chem. 272: 4201-4211
    • (1997) J. Biol. Chem. , vol.272 , pp. 4201-4211
    • Yano, T.1    Chu, S.S.2    Sled, V.D.3    Ohnishi, T.4    Yagi, T.5
  • 70
    • 0033215393 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans
    • +-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. J. Biol. Chem. 274: 28606-28611
    • (1999) J. Biol. Chem. , vol.274 , pp. 28606-28611
    • Yano, T.1    Yagi, T.2
  • 71
    • 0028881842 scopus 로고
    • Structural analysis of NADH: Ubiquinone oxidoreductase from bovine heart mitochondria
    • Walker J. E., Skehel J. M. and Buchanan S. K. (1995) Structural analysis of NADH: Ubiquinone oxidoreductase from bovine heart mitochondria. Methods Enzymol. 260: 14-34
    • (1995) Methods Enzymol. , vol.260 , pp. 14-34
    • Walker, J.E.1    Skehel, J.M.2    Buchanan, S.K.3
  • 72
    • 0032490117 scopus 로고    scopus 로고
    • The NADH: Ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Friedrich T (1998) The NADH: Ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim. Biophys. Acta 1364: 134-146
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 134-146
    • Friedrich, T.1
  • 73
    • 0032726773 scopus 로고    scopus 로고
    • One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography
    • Bungert S., Krafft B., Schlesinger R. and Friedrich T. (1999) One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography. FEBS Lett. 460: 207-211
    • (1999) FEBS Lett. , vol.460 , pp. 207-211
    • Bungert, S.1    Krafft, B.2    Schlesinger, R.3    Friedrich, T.4
  • 74
    • 0027328631 scopus 로고
    • Intimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH: Ubiquinone oxidoreductase
    • Albracht S. P. (1993) Intimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH: Ubiquinone oxidoreductase. Biochim. Biophys. Acta 1144: 221-224
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 221-224
    • Albracht, S.P.1
  • 75
    • 0031886480 scopus 로고    scopus 로고
    • Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus
    • Massanz C., Schmidt S. and Friedrich B. (1998) Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus. J. Bacteriol. 180:1023-1029
    • (1998) J. Bacteriol. , vol.180 , pp. 1023-1029
    • Massanz, C.1    Schmidt, S.2    Friedrich, B.3
  • 76
    • 0025291627 scopus 로고
    • Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16
    • Tran-Betcke A., Warnecke U., Bocker C., Zaborosch C. and Friedrich B. (1990) Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol 172: 2920-2909
    • (1990) J. Bacteriol. , vol.172 , pp. 2920-2909
    • Tran-Betcke, A.1    Warnecke, U.2    Bocker, C.3    Zaborosch, C.4    Friedrich, B.5
  • 77
    • 0026032458 scopus 로고
    • Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • Pilkington S. J., Skehel J. M., Gennis R. B. and Walker J. E. (1991) Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 30:166-175
    • (1991) Biochemistry , vol.30 , pp. 166-175
    • Pilkington, S.J.1    Skehel, J.M.2    Gennis, R.B.3    Walker, J.E.4
  • 78
    • 0024350374 scopus 로고
    • Mitochondrial NADH: Ubiquinone reductase: Complementary DNA sequence of the import precursor of the bovine 75-kDa subunit
    • Runswick M. J., Gennis R. B., Fearnley I. M. and Walker J. E. (1989) Mitochondrial NADH: Ubiquinone reductase: Complementary DNA sequence of the import precursor of the bovine 75-kDa subunit. Biochemistry 28: 9452-9459
    • (1989) Biochemistry , vol.28 , pp. 9452-9459
    • Runswick, M.J.1    Gennis, R.B.2    Fearnley, I.M.3    Walker, J.E.4
  • 79
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Braun M., Bungert S. and Friedrich T (1998) Characterization of the overproduced NADH dehydrogenase fragment of the NADH: Ubiquinone oxidoreductase from Escherichia coli. Biochemistry 37: 1861-1867
    • (1998) Biochemistry , vol.37 , pp. 1861-1867
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 80
    • 0034773042 scopus 로고    scopus 로고
    • The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: Comparison of phylogenetically related enzymes
    • Yano T. and Ohnishi T. (2001) The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: Comparison of phylogenetically related enzymes. J. Bioenerg. Biomembr. 33: 213-222
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 213-222
    • Yano, T.1    Ohnishi, T.2
  • 81
    • 0034609560 scopus 로고    scopus 로고
    • FT-IR spectroscopic characterization of NADH: Ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain
    • Hellwig P., Scheide D., Bungert S., Mäntele W. and Friedrich T. (2000) FT-IR spectroscopic characterization of NADH: Ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain. Biochemistry 39: 10884-10891
    • (2000) Biochemistry , vol.39 , pp. 10884-10891
    • Hellwig, P.1    Scheide, D.2    Bungert, S.3    Mäntele, W.4    Friedrich, T.5
  • 82
    • 0034663582 scopus 로고    scopus 로고
    • Characterization of complex I-associated ubiquinone species: Towards the understanding of their functional roles in the electron/proton transfer reaction
    • Yano T., Magnitsky S. and Ohnishi T. (2000) Characterization of complex I-associated ubiquinone species: Towards the understanding of their functional roles in the electron/proton transfer reaction. Biochim. Biophys. Acta 1459: 299-304
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 299-304
    • Yano, T.1    Magnitsky, S.2    Ohnishi, T.3
  • 83
    • 0032311426 scopus 로고    scopus 로고
    • Structure-function studies of ironsulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain
    • Ohnishi T., Sled V. D., Yano T., Yagi T., Burbaev D. S. and Vinogradov A. D. (1998) Structure-function studies of ironsulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain. Biochim. Biophys. Acta 1365: 301-308
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 301-308
    • Ohnishi, T.1    Sled, V.D.2    Yano, T.3    Yagi, T.4    Burbaev, D.S.5    Vinogradov, A.D.6
  • 84
    • 0034663629 scopus 로고    scopus 로고
    • Characterization of two novel redox groups in the respiratory NADH: Ubiquinone oxidoreductase (complex I) Biochim
    • Friedrich T., Brors B., Hellwig P., Kintscher L., Rasmussen T., Scheide D. et al. (2000) Characterization of two novel redox groups in the respiratory NADH: Ubiquinone oxidoreductase (complex I) Biochim. Biophys. Acta 1459: 305-309
    • (2000) Biophys. Acta , vol.1459 , pp. 305-309
    • Friedrich, T.1    Brors, B.2    Hellwig, P.3    Kintscher, L.4    Rasmussen, T.5    Scheide, D.6
  • 85
    • 0034778053 scopus 로고    scopus 로고
    • Towards a characterization of the connecting module of complex I
    • Dupuis A., Prieur I. and Lunardi J. (2001) Towards a characterization of the connecting module of complex I. J. Bioenerg. Biomembr. 33: 159-168
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 159-168
    • Dupuis, A.1    Prieur, I.2    Lunardi, J.3
  • 86
    • 0034598939 scopus 로고    scopus 로고
    • A motif for quinone binding sites in respiratory and photosynthetic systems
    • Fisher N. and Rich P. R. (2000) A motif for quinone binding sites in respiratory and photosynthetic systems. J. Mol. Biol. 296: 1153-1162
    • (2000) J. Mol. Biol. , vol.296 , pp. 1153-1162
    • Fisher, N.1    Rich, P.R.2
  • 87
    • 0035795163 scopus 로고    scopus 로고
    • Evidence for quinone binding site close to the interface between NuoD and NuoB subunits of complex I
    • Prieur I., Lunardi J. and Dupuis A. (2001) Evidence for quinone binding site close to the interface between NuoD and NuoB subunits of complex I. Biochim. Biophys. Acta 1504: 173-178
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 173-178
    • Prieur, I.1    Lunardi, J.2    Dupuis, A.3
  • 88
    • 0032477715 scopus 로고    scopus 로고
    • The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes
    • Sazanov L. A., Burrows P. A. and Nixon P. J. (1998) The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes. Proc. Natl. Acad. Sci. USA 95: 1319-1324
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1319-1324
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 89
    • 0033983147 scopus 로고    scopus 로고
    • Progress in understanding structurefunction relationships in respiratory chain complex II
    • Ackrell B. A. (2000) Progress in understanding structurefunction relationships in respiratory chain complex II. FEBS Lett. 466:1-5
    • (2000) FEBS Lett. , vol.466 , pp. 1-5
    • Ackrell, B.A.1
  • 90
    • 0032504107 scopus 로고    scopus 로고
    • The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors
    • Darrouzet E., Issartel J.-P., Lunardi J. and Dupuis A. (1998) The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors. FEBS Lett. 431: 34-38
    • (1998) FEBS Lett. , vol.431 , pp. 34-38
    • Darrouzet, E.1    Issartel, J.-P.2    Lunardi, J.3    Dupuis, A.4
  • 91
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I
    • Kashani-Poor N., Zwicker K., Kerscher S. and Brandt U. (2001) A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I. J. Biol. Chem. 276: 24082-24087
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 92
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: An overview
    • Esposti M. D. (1998) Inhibitors of NADH-ubiquinone reductase: An overview. Biochim Biophys. Acta 1364: 222-235
    • (1998) Biochim Biophys. Acta , vol.1364 , pp. 222-235
    • Esposti, M.D.1
  • 94
    • 0035796952 scopus 로고    scopus 로고
    • Functional coupling of PSST and ND1 subunits in NADH: Ubiquinone oxidoreductase established by photoaffinity labeling
    • Schuler F. and Casida J. E. (2001) Functional coupling of PSST and ND1 subunits in NADH: Ubiquinone oxidoreductase established by photoaffinity labeling. Biochim. Biophys. Acta 1506: 79-87
    • (2001) Biochim. Biophys. Acta , vol.1506 , pp. 79-87
    • Schuler, F.1    Casida, J.E.2
  • 95
    • 0034680865 scopus 로고    scopus 로고
    • Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (complex I)
    • Albracht S. P. J. and Hedderich R. (2000) Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (complex I). FEBS Lett. 485: 1-6
    • (2000) FEBS Lett. , vol.485 , pp. 1-6
    • Albracht, S.P.J.1    Hedderich, R.2
  • 96
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich T. and Scheide D. (2000) The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479: 1-5
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 98
    • 0034604568 scopus 로고    scopus 로고
    • Function of conserved acidic residues in the PSST homologue of complex I (NADH: Ubiquinone oxidoreductase from Yarrowia lipolytica
    • Ahlers P. M., Zwicker K., Kerscher S. and Brandt U. (2000) Function of conserved acidic residues in the PSST homologue of complex I (NADH: Ubiquinone oxidoreductase from Yarrowia lipolytica. J. Biol. Chem. 275: 23577-23582
    • (2000) J. Biol. Chem. , vol.275 , pp. 23577-23582
    • Ahlers, P.M.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 99
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • Ohnishi T (1998) Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta 1364: 186-206
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 100
    • 0020354803 scopus 로고
    • Occurrence of α-tocopherolquinone and α-Tocopherolquinol in microorganisms
    • Hughes P. E. and Tove S. B. (1982) Occurrence of α-tocopherolquinone and α-Tocopherolquinol in microorganisms. J. Bacteriol. 151: 1397-1402
    • (1982) J. Bacteriol. , vol.151 , pp. 1397-1402
    • Hughes, P.E.1    Tove, S.B.2
  • 102
    • 0032588194 scopus 로고    scopus 로고
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett. 451: 157-161
    • (1999) FEBS Lett. , vol.451 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 104
    • 0028023673 scopus 로고
    • The mechanism of proton and electron transport in mitochondrial complex I
    • Esposti M. D. and Ghelli A. (1994) The mechanism of proton and electron transport in mitochondrial complex I. Biochim. Biophys. Acta 1187: 116-120
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 116-120
    • Esposti, M.D.1    Ghelli, A.2
  • 105
    • 0031033436 scopus 로고    scopus 로고
    • Proton-translocation by membranebound NADH: Ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction
    • Brandt U. (1997) Proton-translocation by membranebound NADH: Ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction. Biochim. Biophys. Acta 1318: 79-91
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 79-91
    • Brandt, U.1
  • 106
    • 0034782745 scopus 로고    scopus 로고
    • Complex I: A chimaera of a redox and conformation-driven proton pump?
    • Friedrich T. (2001) Complex I: A chimaera of a redox and conformation-driven proton pump? J. Bioenerg. Biomembr. 33: 169-177
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 169-177
    • Friedrich, T.1
  • 108
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox J. D., He Y. P., Shelver D., Roberts G. P. and Ludden P. W. (1996) Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178: 6200-6208
    • (1996) J. Bacteriol. , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.P.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 109
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
    • Fox J. D., Kerby R. L., Roberts G. P. and Ludden P.W. (1996) Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178: 1515-1521
    • (1996) J. Bacteriol. , vol.178 , pp. 1515-1521
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 110
    • 0030613533 scopus 로고    scopus 로고
    • 2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea
    • 2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. Eur. J. Biochem. 248: 919-924
    • (1997) Eur. J. Biochem. , vol.248 , pp. 919-924
    • Vorholt, J.A.1    Thauer, R.K.2
  • 111
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm R., Sauter M. and Böck A (1990) Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4: 231-243
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 112
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Andrews S. C., Berks B. C., McClay J., Ambler A., Quail M. A., Golby P. et al. (1997) A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143: 3633-3647
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.