메뉴 건너뛰기




Volumn 2, Issue 4, 2010, Pages 489-499

Syntrophic butyrate and propionate oxidation processes: From genomes to reaction mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

PELOTOMACULUM THERMOPROPIONICUM; SYNTROPHOBACTER FUMAROXIDANS; SYNTROPHOMONAS WOLFEI; SYNTROPHUS ACIDITROPHICUS; THERMOTOGA MARITIMA;

EID: 78649756861     PISSN: None     EISSN: 17582229     Source Type: Journal    
DOI: 10.1111/j.1758-2229.2010.00147.x     Document Type: Review
Times cited : (258)

References (48)
  • 1
    • 54849405513 scopus 로고    scopus 로고
    • Covalent binding of flavins to RnfG and RnfD in the Rnf complex form Vibrio cholera
    • Backiel, J., Juárez, O., Zagorevski, D.V., Wang, Z., Nilges, M.J., and Barquera, B. (2008) Covalent binding of flavins to RnfG and RnfD in the Rnf complex form Vibrio cholera. Biochemistry-US 47: 11273-11284.
    • (2008) Biochemistry-US , vol.47 , pp. 11273-11284
    • Backiel, J.1    Juárez, O.2    Zagorevski, D.V.3    Wang, Z.4    Nilges, M.J.5    Barquera, B.6
  • 3
    • 0035319411 scopus 로고    scopus 로고
    • Pathway of propionate oxidation by a syntrophic culture of Smithella propionica and Methanospirillum hungatei
    • de Bok, F.A.M., Stams, A.J.M., Dijkema, C., and Boone, D.R. (2001) Pathway of propionate oxidation by a syntrophic culture of Smithella propionica and Methanospirillum hungatei. Appl Environ Microbiol 67: 1800-1804.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1800-1804
    • de Bok, F.A.M.1    Stams, A.J.M.2    Dijkema, C.3    Boone, D.R.4
  • 4
    • 0036731743 scopus 로고    scopus 로고
    • Biochemical evidence for formate transfer in syntrophic propionate-oxidizing cocultures of Syntrophobacter fumaroxidans and Methanospirillum hungatei
    • de Bok, F.A.M., Luijten, M.L.G.C., and Stams, A.J.M. (2002) Biochemical evidence for formate transfer in syntrophic propionate-oxidizing cocultures of Syntrophobacter fumaroxidans and Methanospirillum hungatei. Appl Environ Microbiol 68: 4247-4252.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4247-4252
    • de Bok, F.A.M.1    Luijten, M.L.G.C.2    Stams, A.J.M.3
  • 6
    • 0032929940 scopus 로고    scopus 로고
    • Crystal structures of the key anaerobic enzyme pyruvate: ferredoxin oxidoreductase, free and in complex with pyruvate
    • Chabrière, E., Charon, M.H., Volbeda, A., Pieulle, L., Hatchikian, E.C., and Fontecilla-Camps, J.C. (1999) Crystal structures of the key anaerobic enzyme pyruvate: ferredoxin oxidoreductase, free and in complex with pyruvate. Nat Struct Biol 6: 182-190.
    • (1999) Nat Struct Biol , vol.6 , pp. 182-190
    • Chabrière, E.1    Charon, M.H.2    Volbeda, A.3    Pieulle, L.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 8
    • 0002903163 scopus 로고
    • 2 and formate formation during syntrophic butyrate and propionate degradation
    • 2 and formate formation during syntrophic butyrate and propionate degradation. Anaerobe 1: 35-39.
    • (1995) Anaerobe , vol.1 , pp. 35-39
    • Dong, X.Z.1    Stams, A.J.M.2
  • 9
    • 0028153156 scopus 로고
    • Butyrate oxidation by Syntrophospora bryantii in coculture with different methanogens and in pure culture with pentenoate as electron-acceptor
    • Dong, X.Z., Cheng, G., and Stams, A.J.M. (1994) Butyrate oxidation by Syntrophospora bryantii in coculture with different methanogens and in pure culture with pentenoate as electron-acceptor. Appl Microbiol Biotechnol 42: 647-652.
    • (1994) Appl Microbiol Biotechnol , vol.42 , pp. 647-652
    • Dong, X.Z.1    Cheng, G.2    Stams, A.J.M.3
  • 10
    • 0037286346 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of two tungstenand selenium-containing formate dehydrogenases from Eubacterium acidaminophilum that are associated with components of an iron-only hydrogenase
    • Graentzdoerffer, A., Rauh, D., Pich, A., and Andreesen, J.R. (2003) Molecular and biochemical characterization of two tungstenand selenium-containing formate dehydrogenases from Eubacterium acidaminophilum that are associated with components of an iron-only hydrogenase. Arch Microbiol 179: 116-130.
    • (2003) Arch Microbiol , vol.179 , pp. 116-130
    • Graentzdoerffer, A.1    Rauh, D.2    Pich, A.3    Andreesen, J.R.4
  • 11
    • 0023009059 scopus 로고
    • Energetics of beta-oxidation - reduction potentials of general fatty acyl-CoA dehydrogenase, electron-transfer flavoprotein, and fatty acyl-CoA substrates
    • Gustafson, W.G., Feinberg, B.A., and Mcfarland, J.T. (1986) Energetics of beta-oxidation - reduction potentials of general fatty acyl-CoA dehydrogenase, electron-transfer flavoprotein, and fatty acyl-CoA substrates. J Biol Chem 261: 7733-7741.
    • (1986) J Biol Chem , vol.261 , pp. 7733-7741
    • Gustafson, W.G.1    Feinberg, B.A.2    Mcfarland, J.T.3
  • 12
    • 2342475768 scopus 로고    scopus 로고
    • The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough
    • Heidelberg, J.F., Seshadri, R., Haveman, S.A., Hemme, C.L., Paulsen, I.T., Kolonay, J.F., et al. (2004) The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Nat Biotechnol 22: 554-559.
    • (2004) Nat Biotechnol , vol.22 , pp. 554-559
    • Heidelberg, J.F.1    Seshadri, R.2    Haveman, S.A.3    Hemme, C.L.4    Paulsen, I.T.5    Kolonay, J.F.6
  • 13
    • 38649143651 scopus 로고    scopus 로고
    • Energy conservation via electron-transferring flavoprotein in anaerobic bacteria
    • Herrmann, G., Jayamani, E., Mai, G., and Buckel, W. (2008) Energy conservation via electron-transferring flavoprotein in anaerobic bacteria. J Bacteriol 190: 784-791.
    • (2008) J Bacteriol , vol.190 , pp. 784-791
    • Herrmann, G.1    Jayamani, E.2    Mai, G.3    Buckel, W.4
  • 14
    • 0035675972 scopus 로고    scopus 로고
    • Apparent minimum free energy requirements for methanogenic archaea and sulfate-reducing bacteria in an anoxic marine sediment
    • Hoehler, T.M., Alperin, M.J., Albert, D.B., and Martens, C.S. (2001) Apparent minimum free energy requirements for methanogenic archaea and sulfate-reducing bacteria in an anoxic marine sediment. FEMS Microbiol Ecol 38: 33-41.
    • (2001) FEMS Microbiol Ecol , vol.38 , pp. 33-41
    • Hoehler, T.M.1    Alperin, M.J.2    Albert, D.B.3    Martens, C.S.4
  • 15
    • 29144460324 scopus 로고    scopus 로고
    • Coaggregation facilitates interspecies hydrogen transfer between Pelotomaculum thermopropionicum and Methanothermobacter thermoautotrophicus
    • Ishii, S., Kosaka, T., Hori, K., Hotta, Y., and Watanabe, K. (2005) Coaggregation facilitates interspecies hydrogen transfer between Pelotomaculum thermopropionicum and Methanothermobacter thermoautotrophicus. Appl Environ Microbiol 71: 7838-7845.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7838-7845
    • Ishii, S.1    Kosaka, T.2    Hori, K.3    Hotta, Y.4    Watanabe, K.5
  • 16
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: structure of formate dehydrogenase-N
    • Jormakka, M., Törnroth, S., Byrne, B., and Iwata, S. (2002) Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295: 1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Törnroth, S.2    Byrne, B.3    Iwata, S.4
  • 17
    • 40449133247 scopus 로고    scopus 로고
    • The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota
    • Kosaka, T., Kato, S., Shimoyama, T., Ishii, S., Abe, T., and Watanabe, K. (2008) The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota. Genome Res 18: 442-448.
    • (2008) Genome Res , vol.18 , pp. 442-448
    • Kosaka, T.1    Kato, S.2    Shimoyama, T.3    Ishii, S.4    Abe, T.5    Watanabe, K.6
  • 19
    • 2942546160 scopus 로고    scopus 로고
    • The prokaryotic selenoproteome
    • Kryukov, G.V., and Gladyshev, V.N. (2004) The prokaryotic selenoproteome. EMBO Rep 5: 538-543.
    • (2004) EMBO Rep , vol.5 , pp. 538-543
    • Kryukov, G.V.1    Gladyshev, V.N.2
  • 20
    • 0030297252 scopus 로고    scopus 로고
    • Purification and characterization of malate dehydrogenase from the syntrophic propionate-oxidizing bacterium strain MPOB
    • van Kuijk, B.L.M., and Stams, A.J.M. (1996) Purification and characterization of malate dehydrogenase from the syntrophic propionate-oxidizing bacterium strain MPOB. FEMS Microbiol Lett 144: 141-144.
    • (1996) FEMS Microbiol Lett , vol.144 , pp. 141-144
    • van Kuijk, B.L.M.1    Stams, A.J.M.2
  • 21
    • 0031981523 scopus 로고    scopus 로고
    • Investigation of the fumarate metabolism of the syntrophic propionate-oxidizing bacterium strain MPOB
    • van Kuijk, B.L.M., Schlösser, E., and Stams, A.J.M. (1998) Investigation of the fumarate metabolism of the syntrophic propionate-oxidizing bacterium strain MPOB. Arch Microbiol 169: 346-352.
    • (1998) Arch Microbiol , vol.169 , pp. 346-352
    • van Kuijk, B.L.M.1    Schlösser, E.2    Stams, A.J.M.3
  • 22
    • 0030905547 scopus 로고    scopus 로고
    • Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energycoupling NADH oxidoreductases
    • Kumagai, H., Fujiwara, T., Matsubara, H., and Saeki, K. (1997) Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energycoupling NADH oxidoreductases. Biochemistry-US 36: 5509-5521.
    • (1997) Biochemistry-US , vol.36 , pp. 5509-5521
    • Kumagai, H.1    Fujiwara, T.2    Matsubara, H.3    Saeki, K.4
  • 23
    • 0037122937 scopus 로고    scopus 로고
    • Succinate: quinone oxidoreductases: an overview
    • Lancaster, C.R.D. (2002) Succinate: quinone oxidoreductases: an overview. Biotech Biophys Acta Bioenerg 1553: 1-6.
    • (2002) Biotech Biophys Acta Bioenerg , vol.1553 , pp. 1-6
    • Lancaster, C.R.D.1
  • 24
    • 38649099718 scopus 로고    scopus 로고
    • Coupled ferredoxin and crotonyl coenzyme a (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri
    • Li, F., Hinderberger, J., Seedorf, H., Zhang, J., Buckel, W., and Thauer, R.K. (2008) Coupled ferredoxin and crotonyl coenzyme a (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. J Bacteriol 190: 843-850.
    • (2008) J Bacteriol , vol.190 , pp. 843-850
    • Li, F.1    Hinderberger, J.2    Seedorf, H.3    Zhang, J.4    Buckel, W.5    Thauer, R.K.6
  • 25
    • 0018364444 scopus 로고
    • Anaerobic bacterium that degrades fatty acids in syntrophic association with methanogens
    • McInerney, M.J., Bryant, M.P., and Pfennig, N. (1979) Anaerobic bacterium that degrades fatty acids in syntrophic association with methanogens. Arch Microbiol 122: 129-135.
    • (1979) Arch Microbiol , vol.122 , pp. 129-135
    • McInerney, M.J.1    Bryant, M.P.2    Pfennig, N.3
  • 26
    • 0019420777 scopus 로고
    • Syntrophomonas wolfei gen. nov. sp. nov, an anaerobic, syntrophic fatty acid-oxidizing bacterium
    • McInerney, M.J., Bryant, M.P., Hespell, R.B., and Costerton, J.W. (1981) Syntrophomonas wolfei gen. nov. sp. nov, an anaerobic, syntrophic fatty acid-oxidizing bacterium. Appl Environ Microbiol 41: 1029-1039.
    • (1981) Appl Environ Microbiol , vol.41 , pp. 1029-1039
    • McInerney, M.J.1    Bryant, M.P.2    Hespell, R.B.3    Costerton, J.W.4
  • 29
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D.H., Sabina, J., Zuker, M., and Turner, D.H. (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J Mol Biol 288: 911-940.
    • (1999) J Mol Biol , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 31
    • 70349096859 scopus 로고    scopus 로고
    • Involvement of NADH: acceptor oxidoreductase and butyryl-CoA dehydrogenase in reversed electron transport during syntrophic butyrate oxidation by Syntrophomonas wolfei
    • Müller, N., Schleheck, C., and Schink, B. (2009) Involvement of NADH: acceptor oxidoreductase and butyryl-CoA dehydrogenase in reversed electron transport during syntrophic butyrate oxidation by Syntrophomonas wolfei. J Bacteriol 191: 6167-6177.
    • (2009) J Bacteriol , vol.191 , pp. 6167-6177
    • Müller, N.1    Schleheck, C.2    Schink, B.3
  • 32
    • 43749117318 scopus 로고    scopus 로고
    • Stochastic rotational catalysis of proton pumping F-ATPase
    • Nakanishi-Matsui, M., and Futai, M. (2008) Stochastic rotational catalysis of proton pumping F-ATPase. Philos Trans R Soc Lond B Biol Sci 363: 2135-2142.
    • (2008) Philos Trans R Soc Lond B Biol Sci , vol.363 , pp. 2135-2142
    • Nakanishi-Matsui, M.1    Futai, M.2
  • 34
    • 0034153610 scopus 로고    scopus 로고
    • Bacterial respiration: a flexible process for a changing environment
    • Richardson, D.J. (2000) Bacterial respiration: a flexible process for a changing environment. Microbiology 146: 551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 35
    • 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
  • 36
    • 42349106001 scopus 로고    scopus 로고
    • Syntrophism among prokaryotes
    • Schink, B., and Stams, A.J.M. (2006) Syntrophism among prokaryotes. Prokaryotes 2: 309-335.
    • (2006) Prokaryotes , vol.2 , pp. 309-335
    • Schink, B.1    Stams, A.J.M.2
  • 37
    • 67649413347 scopus 로고    scopus 로고
    • The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production
    • Schut, G.J., and Adams, M.W.W. (2009) The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J Bacteriol 191: 4451-4457.
    • (2009) J Bacteriol , vol.191 , pp. 4451-4457
    • Schut, G.J.1    Adams, M.W.W.2
  • 38
    • 67651202726 scopus 로고    scopus 로고
    • Electron transfer in syntrophic communities of anaerobic bacteria and archaea
    • Stams, A.J.M., and Plugge, C.M. (2009) Electron transfer in syntrophic communities of anaerobic bacteria and archaea. Nat Rev Microbiol 7: 568-577.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 568-577
    • Stams, A.J.M.1    Plugge, C.M.2
  • 39
    • 0000988148 scopus 로고
    • Metabolism of chemotrophic anaerobes: old views and new aspects
    • Thauer, R.K., and Morris, J.G. (1984) Metabolism of chemotrophic anaerobes: old views and new aspects. Symp Soc Gen Microbiol 36 (Part 2): 123-168.
    • (1984) Symp Soc Gen Microbiol , vol.36 , Issue.PART 2 , pp. 123-168
    • Thauer, R.K.1    Morris, J.G.2
  • 40
    • 0017343370 scopus 로고
    • Energy-conservation in chemotropic anaerobic bacteria
    • Thauer, R.K., Jungermann, K., and Decker, K. (1977) Energy-conservation in chemotropic 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
  • 41
    • 0027937285 scopus 로고
    • Evidence of reversed electron-transport in syntrophic butyrate or benzoate oxidation by Syntrophomonas wolfei and Syntrophus buswellii
    • Wallrabenstein, C., and Schink, B. (1994) Evidence of reversed electron-transport in syntrophic butyrate or benzoate oxidation by Syntrophomonas wolfei and Syntrophus buswellii. Arch Microbiol 162: 136-142.
    • (1994) Arch Microbiol , vol.162 , pp. 136-142
    • Wallrabenstein, C.1    Schink, B.2
  • 42
    • 0022534306 scopus 로고
    • Preparation of cell-free-extracts and the enzymes involved in fatty-acid metabolism in Syntrophomonas wolfei
    • Wofford, N.Q., Beaty, P.S., and McInerney, M.J. (1986) Preparation of cell-free-extracts and the enzymes involved in fatty-acid metabolism in Syntrophomonas wolfei. J Bacteriol 167: 179-185.
    • (1986) J Bacteriol , vol.167 , pp. 179-185
    • Wofford, N.Q.1    Beaty, P.S.2    McInerney, M.J.3
  • 43
    • 33749988488 scopus 로고    scopus 로고
    • Syntrophomonas cellicola sp nov., a spore-forming syntrophic bacterium isolated from a distilled-spirit-fermenting cellar, and assignment of Syntrophospora bryantii to Syntrophomonas bryantii comb. nov
    • Wu, C.G., Liu, X.L., and Dong, X.Z. (2006) Syntrophomonas cellicola sp nov., a spore-forming syntrophic bacterium isolated from a distilled-spirit-fermenting cellar, and assignment of Syntrophospora bryantii to Syntrophomonas bryantii comb. nov. Int J Syst Evol Microbiol 56: 2331-2335.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 2331-2335
    • Wu, C.G.1    Liu, X.L.2    Dong, X.Z.3
  • 44
    • 33744957049 scopus 로고    scopus 로고
    • Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis type-II NADH-menaquinone oxidoreductase (NDH-2)
    • Yano, T., Li, L.S., Weinstein, E., Teh, J.S., and Rubin, H. (2006) Steady-state kinetics and inhibitory action of antitubercular phenothiazines on Mycobacterium tuberculosis type-II NADH-menaquinone oxidoreductase (NDH-2). J Biol Chem 281: 11456-11463.
    • (2006) J Biol Chem , vol.281 , pp. 11456-11463
    • Yano, T.1    Li, L.S.2    Weinstein, E.3    Teh, J.S.4    Rubin, H.5
  • 45
    • 20744437008 scopus 로고    scopus 로고
    • An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genes
    • Zhang, Y., and Gladyshev, V.N. (2005) An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genes. Bioinformatics 21: 2580-2589.
    • (2005) Bioinformatics , vol.21 , pp. 2580-2589
    • Zhang, Y.1    Gladyshev, V.N.2
  • 46
    • 0027460195 scopus 로고
    • Assignment of fatty acid-beta-oxidizing syntrophic bacteria to Syntrophomonadaceae fam. nov. on the basis of 16S rRNA sequence analyses
    • Zhao, H.X., Yang, D.C., Woese, C.R., and Bryant, M.P. (1993) Assignment of fatty acid-beta-oxidizing syntrophic bacteria to Syntrophomonadaceae fam. nov. on the basis of 16S rRNA sequence analyses. Int J Syst Bacteriol 43: 630-630.
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 630-1630
    • Zhao, H.X.1    Yang, D.C.2    Woese, C.R.3    Bryant, M.P.4
  • 48
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.