메뉴 건너뛰기




Volumn 150, Issue 7, 2004, Pages 2451-2463

A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ALCOHOL; ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; CARBON DIOXIDE; FERREDOXIN; FERROUS ION; FLAVINE MONONUCLEOTIDE; GLUCOSE; HYDROGEN; HYDROGENASE; IRON; PROTEIN NIFE; PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SULFUR; UNCLASSIFIED DRUG;

EID: 4344700076     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.27159-0     Document Type: Article
Times cited : (144)

References (52)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams, M. W. (1990). The structure and mechanism of iron-hydrogenases. Biochim Biophys Acta 1020, 115-145.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.1
  • 2
    • 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. & 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.1    Hedderich, R.2
  • 3
    • 0035197482 scopus 로고    scopus 로고
    • Carbohydrates in thermophile metabolism: Calculation of the standard molal thermodynamic properties of aqueous pentoses and hexoses at elevated temperatures and pressures
    • Amend, J. P. & Plyasunov, A. V. (2001). Carbohydrates in thermophile metabolism: calculation of the standard molal thermodynamic properties of aqueous pentoses and hexoses at elevated temperatures and pressures. Geochim Cosmochim Acta 65, 3901-3917.
    • (2001) Geochim. Cosmochim. Acta , vol.65 , pp. 3901-3917
    • Amend, J.P.1    Plyasunov, A.V.2
  • 4
    • 0035093350 scopus 로고    scopus 로고
    • Energetics of overall metabolic reactions of thermophilic and hyperthermophilic archaea and bacteria
    • Amend, J. P. & Shock, E. L. (2001). Energetics of overall metabolic reactions of thermophilic and hyperthermophilic archaea and bacteria. FEMS Microbiol Rev 25, 175-243.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 175-243
    • Amend, J.P.1    Shock, E.L.2
  • 5
    • 0036112438 scopus 로고    scopus 로고
    • A complete sequence of the T. tengcongensis genome
    • 18 other authors
    • Bao, Q., Tian, Y., Li, W. & 18 other authors (2002). A complete sequence of the T. tengcongensis genome. Genome Res 12, 689-700.
    • (2002) Genome Res. , vol.12 , pp. 689-700
    • Bao, Q.1    Tian, Y.2    Li, W.3
  • 6
    • 0020494651 scopus 로고
    • New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria
    • Beinert, H. & Albracht, S. P. J. (1982). New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochim Biophys Acta 683, 245-277.
    • (1982) Biochim. Biophys. Acta , vol.683 , pp. 245-277
    • Beinert, H.1    Albracht, S.P.J.2
  • 8
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm, R., Sauter, M. & 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
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0028074589 scopus 로고
    • Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39e and characterisation of the secondary-alcohol dehydrogenase as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase
    • Burdette, D. S. & Zeikus, J. G. (1994). Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39e and characterisation of the secondary-alcohol dehydrogenase as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase. Biochem J 302, 163-170.
    • (1994) Biochem. J. , vol.302 , pp. 163-170
    • Burdette, D.S.1    Zeikus, J.G.2
  • 12
    • 0029950256 scopus 로고    scopus 로고
    • Cloning and expression of the gene encoding the Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase and biochemical characterization of the enzyme
    • Burdette, D. S., Vieille, C. & Zeikus, J. G. (1996). Cloning and expression of the gene encoding the Thermoanaerobacter ethanolicus 39E secondary-alcohol dehydrogenase and biochemical characterization of the enzyme. Biochem J 316, 115-122.
    • (1996) Biochem. J. , vol.316 , pp. 115-122
    • Burdette, D.S.1    Vieille, C.2    Zeikus, J.G.3
  • 13
    • 0036209447 scopus 로고    scopus 로고
    • Physiological function of alcohol dehydrogenases and long-chain (C-30) fatty acids in alcohol tolerance of Thermoanaerobacter ethanolicus
    • Burdette, D. S., Jung, S. H., Shen, G. J., Hollingsworth, R. I. & Zeikus, J. G. (2002). Physiological function of alcohol dehydrogenases and long-chain (C-30) fatty acids in alcohol tolerance of Thermoanaerobacter ethanolicus. Appl Environ Microbiol 68, 1914-1918.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1914-1918
    • Burdette, D.S.1    Jung, S.H.2    Shen, G.J.3    Hollingsworth, R.I.4    Zeikus, J.G.5
  • 14
    • 0018437933 scopus 로고
    • A simple hydrogenase-linked assay for ferredoxin and flavodoxin
    • Chen, J.-S. & Blanchard, D. K. (1979). A simple hydrogenase-linked assay for ferredoxin and flavodoxin. Anal Biochem 93, 216-222.
    • (1979) Anal. Biochem. , vol.93 , pp. 216-222
    • Chen, J.-S.1    Blanchard, D.K.2
  • 15
    • 0032562238 scopus 로고    scopus 로고
    • Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli
    • De Luca, G., Asso, M., Belaich, J. P. & Dermoun, Z. (1998). Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli. Biochemistry 37, 2660-2665.
    • (1998) Biochemistry , vol.37 , pp. 2660-2665
    • De Luca, G.1    Asso, M.2    Belaich, J.P.3    Dermoun, Z.4
  • 16
    • 0017843369 scopus 로고
    • Fermentation of fumarate and L-malate by Clostridium formicoaceticum
    • Dorn, M., Andreesen, J. R. & Gottschalk, G. (1978). Fermentation of fumarate and L-malate by Clostridium formicoaceticum. J Bacteriol 133, 26-32.
    • (1978) J. Bacteriol. , vol.133 , pp. 26-32
    • Dorn, M.1    Andreesen, J.R.2    Gottschalk, G.3
  • 17
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox, J. D., He, Y., Shelver, D., Roberts, G. P. & Ludden, P. W. (1996b). 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.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 18
    • 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. & 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
  • 19
    • 0031582715 scopus 로고    scopus 로고
    • Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules
    • Friedrich, T. & 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
  • 21
    • 2142697116 scopus 로고    scopus 로고
    • Energy-converting [NiFe] hydrogenases from archaea and extremophiles: Ancestors of complex I
    • Hedderich, R. (2004). Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. J Bioenerg Biomembr 36, 65-75.
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 65-75
    • Hedderich, R.1
  • 22
    • 0015788525 scopus 로고
    • Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia
    • Jungermann, K., Thauer, R. K., Leimenstoll, G. & Decker, K. (1973). Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia. Biochim Biophys Acta 305, 268-280.
    • (1973) Biochim. Biophys. Acta , vol.305 , pp. 268-280
    • Jungermann, K.1    Thauer, R.K.2    Leimenstoll, G.3    Decker, K.4
  • 23
    • 0028925554 scopus 로고
    • Carbon monoxide-dependent growth of Rhodospirillum rubrum
    • Kerby, R. L., Ludden, P. W. & Roberts, G. P. (1995). Carbon monoxide-dependent growth of Rhodospirillum rubrum. J Bacteriol 177, 2241-2244.
    • (1995) J. Bacteriol. , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 24
    • 0032521598 scopus 로고    scopus 로고
    • An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea
    • Künkel, A., Vorholt, J. A., Thauer, R. K. & 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
  • 25
    • 0001452722 scopus 로고
    • Colorimetric methods with glucose oxidase and peroxidase
    • Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie
    • Kunst, A., Draeger, B. & Ziegenhorn, J. (1981). Colorimetric methods with glucose oxidase and peroxidase. In Methods of Enzymatic Analysis, pp. 178-185. Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie.
    • (1981) Methods of Enzymatic Analysis , pp. 178-185
    • Kunst, A.1    Draeger, B.2    Ziegenhorn, J.3
  • 26
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • Malki, S., Saimmaime, I., De Luca, G., Rousset, M., Dermoun, Z. & Belaich, J. P. (1995). Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J Bacteriol 177, 2628-2636.
    • (1995) J. Bacteriol. , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.P.6
  • 27
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer, J., Bartoschek, S., Koch, J., Künkel, A. & 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
  • 28
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer, J., Kuettner, H. C., Zhang, J. K., Hedderich, R. & Metcalf, W. W. (2002). Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc Natl Acad Sci U S A 99, 5632-5637.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 29
    • 0037950633 scopus 로고    scopus 로고
    • Characterization of a [2Fe-2S] protein encoded in the iron-hydrogenase operon of Thermotoga maritima
    • Pan, G., Menon, A. L. & Adams, M. W. (2003). Characterization of a [2Fe-2S] protein encoded in the iron-hydrogenase operon of Thermotoga maritima. J Biol Inorg Chem 8, 469-474.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 469-474
    • Pan, G.1    Menon, A.L.2    Adams, M.W.3
  • 30
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1·8 angstrom resolution
    • Peters, J. W., Lanzilotta, W. N., Lemon, B. J. & Seefeldt, L. C. (1998). X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1·8 angstrom resolution. Science 282, 1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 31
    • 0034045136 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Sapra, R., Verhagen, M. & Adams, M. W. W. (2000). Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 182, 3423-3428.
    • (2000) J. Bacteriol. , vol.182 , pp. 3423-3428
    • Sapra, R.1    Verhagen, M.2    Adams, M.W.W.3
  • 32
    • 0037934657 scopus 로고    scopus 로고
    • A simple energy-conserving system: Proton reduction coupled to proton translocation
    • Sapra, R., Bagramyan, K. & Adams, M. W. (2003). A simple energy-conserving system: proton reduction coupled to proton translocation. Proc Natl Acad Sci U S A 100, 7545-7550.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7545-7550
    • Sapra, R.1    Bagramyan, K.2    Adams, M.W.3
  • 33
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • Sauter, M., Böhm, R. & Böck, A. (1992). Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol Microbiol 6, 1523-1532.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1523-1532
    • Sauter, M.1    Böhm, R.2    Böck, A.3
  • 34
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • Sawers, G. (1994). The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66, 57-88.
    • (1994) Antonie van Leeuwenhoek , vol.66 , pp. 57-88
    • Sawers, G.1
  • 36
    • 0028356024 scopus 로고
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: Involvement of the Emden-Meyerhof pathway
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: involvement of the Emden-Meyerhof pathway. Arch Microbiol 161, 460-470.
    • (1994) Arch. Microbiol. , vol.161 , pp. 460-470
    • Schröder, C.1    Selig, M.2    Schönheit, P.3
  • 39
    • 0036436922 scopus 로고    scopus 로고
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans. Eur J Biochem 269, 5712-5721.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5712-5721
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 40
    • 0025894923 scopus 로고
    • Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hypothermal environments of Kunashir island
    • Svetlichny, V. A., Sokolova, T. G., Gerhardt, M., Ringpfeil, M., Kostrikina, N. A. & Zavarzin, G. A. (1991). Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hypothermal environments of Kunashir island. Syst Appl Microbiol 14, 254-260.
    • (1991) Syst. Appl. Microbiol. , vol.14 , pp. 254-260
    • Svetlichny, V.A.1    Sokolova, T.G.2    Gerhardt, M.3    Ringpfeil, M.4    Kostrikina, N.A.5    Zavarzin, G.A.6
  • 41
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multi-subunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins
    • Tersteegen, A. & Hedderich, R. (1999). Methanobacterium thermoautotrophicum encodes two multi-subunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Eur J Biochem 264, 930-943.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2
  • 42
    • 0011369410 scopus 로고
    • Regulation of ATP-synthesis in glucose fermenting bacteria involved in interspecies hydrogen transfer
    • Edited by G. Gottschalk. Stuttgart & New York: Gustav Fischer Verlag
    • Tewes, F. J. & Thauer, R. K. (1980). Regulation of ATP-synthesis in glucose fermenting bacteria involved in interspecies hydrogen transfer. In Anaerobes and Anaerobic Infections, pp. 97-104. Edited by G. Gottschalk. Stuttgart & New York: Gustav Fischer Verlag.
    • (1980) Anaerobes and Anaerobic Infections , pp. 97-104
    • Tewes, F.J.1    Thauer, R.2
  • 43
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., Jungermann, K. & Decker, K. (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
  • 44
    • 12244253037 scopus 로고    scopus 로고
    • Substrate and product inhibition of hydrogen production by the extreme thermophile, Caldicellulosiruptor saccharolyticus
    • van Niel, E. W., Claassen, P. A. & Stams, A. J. (2003). Substrate and product inhibition of hydrogen production by the extreme thermophile, Caldicellulosiruptor saccharolyticus. Biotechnol Bioeng 81, 255-262.
    • (2003) Biotechnol. Bioeng. , vol.81 , pp. 255-262
    • van Niel, E.W.1    Claassen, P.A.2    Stams, A.J.3
  • 45
    • 0032799575 scopus 로고    scopus 로고
    • The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: Amino acid sequence analyses versus biochemical characterization
    • Verhagen, M. F., O'Rourke, T. & Adams, M. W. (1999). The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. Biochim Biophys Acta 1412, 212-229.
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 212-229
    • Verhagen, M.F.1    O'Rourke, T.2    Adams, M.W.3
  • 46
    • 0035371934 scopus 로고    scopus 로고
    • Heterologous expression and properties of the gamma-subunit of the Fe-only hydrogenase from Thermotoga maritima
    • Verhagen, M. F., O'Rourke, T. W., Menon, A. L. & Adams, M. W. (2001). Heterologous expression and properties of the gamma-subunit of the Fe-only hydrogenase from Thermotoga maritima. Biochim Biophys Acta 1505, 209-219.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 209-219
    • Verhagen, M.F.1    O'Rourke, T.W.2    Menon, A.L.3    Adams, M.W.4
  • 47
  • 48
    • 0942265390 scopus 로고    scopus 로고
    • An analysis of the proteomic profile for Thermoanaerobacter tengcongensis under optimal culture conditions
    • 11 other authors
    • Wang, J., Xue, Y., Feng, X. & 11 other authors (2004). An analysis of the proteomic profile for Thermoanaerobacter tengcongensis under optimal culture conditions, Proteomics 4, 136-150.
    • (2004) Proteomics , vol.4 , pp. 136-150
    • Wang, J.1    Xue, Y.2    Feng, X.3
  • 49
    • 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. & 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
  • 50
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H. & Stock, A. M. (2001). Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem Sci 26, 369-376.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 51
    • 0034884397 scopus 로고    scopus 로고
    • Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China
    • Xue, Y., Xu, Y., Liu, Y., Ma, Y. & Zhou, P. (2001). Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China. Int J Syst Evol Microbiol 51, 1335-1341.
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 1335-1341
    • Xue, Y.1    Xu, Y.2    Liu, Y.3    Ma, Y.4    Zhou, P.5
  • 52
    • 0034773042 scopus 로고    scopus 로고
    • The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: Comparisons of phylogenetically related enzymes
    • Yano, T. & Ohnishi, T. (2001). The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: comparisons 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.