메뉴 건너뛰기




Volumn 22, Issue 5, 1998, Pages 353-381

Anaerobic respiration with elemental sulfur and with disulfides

Author keywords

Disulfide respiration; Heterodisulfide reductase; Methanogenic archaea; Polysulfide reductase; Pyrodictium abyssi; Sulfur respiration; Wolinella succinogenes

Indexed keywords

DISULFIDE; FORMATE DEHYDROGENASE; OXIDOREDUCTASE; SULFUR;

EID: 0032449962     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(98)00035-7     Document Type: Article
Times cited : (249)

References (171)
  • 1
    • 0025035741 scopus 로고
    • Microbial anaerobic respiration
    • (Rose, A.H. and Tempest, D.W., Eds.), Academic Press, London
    • [1] Moodie, A.D. and Ingledew, W.J. (1990) Microbial anaerobic respiration. In: Advances in Microbiology and Physiology (Rose, A.H. and Tempest, D.W., Eds.), pp. 225-269. Academic Press, London.
    • (1990) Advances in Microbiology and Physiology , pp. 225-269
    • Moodie, A.D.1    Ingledew, W.J.2
  • 2
    • 0002809093 scopus 로고
    • Sulfate-reducing and sulfur-reducing bacteria
    • (Shively, J.M. and Barton, L.L., Eds.), Academic Press, London
    • [2] Fauque, G., LeGall, J. and Barton, L.L. (1991) Sulfate-reducing and sulfur-reducing bacteria. In: Variations in Autotrophic Life (Shively, J.M. and Barton, L.L., Eds.), pp. 271-337. Academic Press, London.
    • (1991) Variations in Autotrophic Life , pp. 271-337
    • Fauque, G.1    LeGall, J.2    Barton, L.L.3
  • 3
    • 0027175993 scopus 로고
    • Bacterial sulphur respiration
    • [3] Schauder, R. and Kröger, A. (1993) Bacterial sulphur respiration. Arch. Microbiol. 159, 491-497.
    • (1993) Arch. Microbiol. , vol.159 , pp. 491-497
    • Schauder, R.1    Kröger, A.2
  • 4
    • 0028673383 scopus 로고
    • Sulfur reductase from thiophilic sulfate-reducing bacteria
    • [4] Fauque, G.D. (1994) Sulfur reductase from thiophilic sulfate-reducing bacteria. Methods Enzymol. 243, 353-367.
    • (1994) Methods Enzymol. , vol.243 , pp. 353-367
    • Fauque, G.D.1
  • 5
    • 0028674123 scopus 로고
    • Sulfur reductases from spirilloid mesophilic sulfur-reducing bacteria
    • [5] Fauque, G.D., Klimmek, O. and Kröger, A. (1994) Sulfur reductases from spirilloid mesophilic sulfur-reducing bacteria. Methods Enzymol. 243, 367-383.
    • (1994) Methods Enzymol. , vol.243 , pp. 367-383
    • Fauque, G.D.1    Klimmek, O.2    Kröger, A.3
  • 6
  • 7
    • 0013565664 scopus 로고
    • A historical overview of methanogenesis
    • (Ferry, J.G., Ed.), Chapman and Hall, New York, NY
    • [7] Wolfe, R.S. (1993) A historical overview of methanogenesis. In: Methanogenesis (Ferry, J.G., Ed.), pp. 1-32. Chapman and Hall, New York, NY.
    • (1993) Methanogenesis , pp. 1-32
    • Wolfe, R.S.1
  • 8
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic archaea
    • [8] 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
  • 9
    • 0030838597 scopus 로고    scopus 로고
    • Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila
    • [9] 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
  • 10
    • 1842329756 scopus 로고    scopus 로고
    • Methanogenesis: Genes, genomes, and who's on first
    • [10] Reeve, J.N., Nölling, J., Morgan, R.M. and Smith, D.R. (1997) Methanogenesis: genes, genomes, and who's on first. J. Bacteriol. 179, 5975-5986.
    • (1997) J. Bacteriol. , vol.179 , pp. 5975-5986
    • Reeve, J.N.1    Nölling, J.2    Morgan, R.M.3    Smith, D.R.4
  • 11
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • [11] 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
  • 12
    • 0023029613 scopus 로고
    • Acidianus infernus gen. Nov., sp. Nov., and Acidianus brierleyi comb. nov.: Facultatively aerobic, extremely acidophilic thermophilic sulfur-metabolizing archaebacteria
    • [12] Segerer, A., Neuner, A., Kristjansson, J. and Stetter, K.O. (1986) Acidianus infernus gen. nov., sp. nov., and Acidianus brierleyi comb. nov.: facultatively aerobic, extremely acidophilic thermophilic sulfur-metabolizing archaebacteria. Int. J. Syst. Bacteriol. 36, 559-564.
    • (1986) Int. J. Syst. Bacteriol. , vol.36 , pp. 559-564
    • Segerer, A.1    Neuner, A.2    Kristjansson, J.3    Stetter, K.O.4
  • 13
    • 0025938528 scopus 로고
    • Stygiolobus azoricus gen. nov., sp. nov. represents a novel genus of anaerobic, extremely thermoacidophilic archaebacteria of the order Sulfolobales
    • [13] Segerer, A.H., Trincone, A., Gahrtz, M. and Stetter, K.O. (1991) Stygiolobus azoricus gen. nov., sp. nov. represents a novel genus of anaerobic, extremely thermoacidophilic archaebacteria of the order Sulfolobales. Int. J. Syst. Bacteriol. 41, 495-501.
    • (1991) Int. J. Syst. Bacteriol. , vol.41 , pp. 495-501
    • Segerer, A.H.1    Trincone, A.2    Gahrtz, M.3    Stetter, K.O.4
  • 14
    • 0002398586 scopus 로고
    • Pyrobaculum gen. nov., a new genus of neutrophilic rod-shaped archaebacteria from continental solfataras growing optimally at 100°C
    • [14] Huber, R., Kristjansson, J.-K. and Stetter, K.O. (1987) Pyrobaculum gen. nov., a new genus of neutrophilic rod-shaped archaebacteria from continental solfataras growing optimally at 100°C. Arch. Microbiol. 149, 95-101.
    • (1987) Arch. Microbiol. , vol.149 , pp. 95-101
    • Huber, R.1    Kristjansson, J.-K.2    Stetter, K.O.3
  • 15
    • 0020597976 scopus 로고
    • The archaebacterium Thermofilum pendens represents a novel genus of the thermophilic, anaerobic sulfur respiring Thermoproteales
    • [15] Zillig, W., Gierl, A., Wunder, S., Janekovic, D., Stetter, K.O. and Klenk, H.P. (1983) The archaebacterium Thermofilum pendens represents a novel genus of the thermophilic, anaerobic sulfur respiring Thermoproteales. Syst. Appl. Microbiol. 4, 79-87.
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 79-87
    • Zillig, W.1    Gierl, A.2    Wunder, S.3    Janekovic, D.4    Stetter, K.O.5    Klenk, H.P.6
  • 17
    • 0020701677 scopus 로고
    • Chemolithoautotrophic metabolism of anaerobic extremely thermophilic archaebacteria
    • [17] Fischer, F., Zillig, W., Stetter, K.O. and Schreiber, G. (1983) Chemolithoautotrophic metabolism of anaerobic extremely thermophilic archaebacteria. Nature 301, 511-513.
    • (1983) Nature , vol.301 , pp. 511-513
    • Fischer, F.1    Zillig, W.2    Stetter, K.O.3    Schreiber, G.4
  • 18
    • 0028104704 scopus 로고
    • 2 with sulfur or thiosulfate as electron acceptor in the anaerobic extremely hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicun proceeds via the citric acid cycle
    • 2 with sulfur or thiosulfate as electron acceptor in the anaerobic extremely hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicun proceeds via the citric acid cycle. Arch. Microbiol. 162, 286-294.
    • (1994) Arch. Microbiol. , vol.162 , pp. 286-294
    • Selig, M.1    Schönheit, P.2
  • 19
    • 0002163252 scopus 로고
    • Characteristics of Desulfurococcus amylolyticus n. sp. a new extremely thermophilic archaebacterium isolated from thermal springs of Kamchatka and Kunashir Island
    • [19] Bonch-Osmolovskaya, E.A., Slesarev, A.I., Miroshnichenko, M.L., Svetlichnaya, T.P. and Alekseev, V.A. (1988) Characteristics of Desulfurococcus amylolyticus n. sp. a new extremely thermophilic archaebacterium isolated from thermal springs of Kamchatka and Kunashir Island. Mikrobiologiya 57, 94-101.
    • (1988) Mikrobiologiya , vol.57 , pp. 94-101
    • Bonch-Osmolovskaya, E.A.1    Slesarev, A.I.2    Miroshnichenko, M.L.3    Svetlichnaya, T.P.4    Alekseev, V.A.5
  • 21
    • 85025384988 scopus 로고
    • Pyrodictium gen. nov., a new genus of submarine disc-shaped sulfur-reducing archaebacteria growing optimally at 105°C
    • [21] Stetter, K.O., König, H. and Stackebrandt, E. (1983) Pyrodictium gen. nov., a new genus of submarine disc-shaped sulfur-reducing archaebacteria growing optimally at 105°C. Syst. Appl. Microbiol. 4, 535-551.
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 535-551
    • Stetter, K.O.1    König, H.2    Stackebrandt, E.3
  • 22
    • 0032521625 scopus 로고    scopus 로고
    • Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from hyperthermophilic Pyrodictium abyssi
    • [22] Dirmeier, R., Keller, M., Frey, G., Huber, H. and Stetter, K.O. (1998) Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from hyperthermophilic Pyrodictium abyssi. Eur. J. Biochem. 252, 486-491.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 486-491
    • Dirmeier, R.1    Keller, M.2    Frey, G.3    Huber, H.4    Stetter, K.O.5
  • 23
    • 0031129435 scopus 로고    scopus 로고
    • Stetteria hydrogenophila, gen. nov. and sp. nov., a novel mixotrophic sulfur dependent crenarchacote isolated from Milos, Greece
    • [23] Jochimsen, B., Peinemann-Simon, S., Völker, H., Stüben, D., Botz, R., Stoffers, P., Dando, P.R. and Thomm, M. (1997) Stetteria hydrogenophila, gen. nov. and sp. nov., a novel mixotrophic sulfur dependent crenarchacote isolated from Milos, Greece. Extremophiles I, 67-73.
    • (1997) Extremophiles I , vol.1 , pp. 67-73
    • Jochimsen, B.1    Peinemann-Simon, S.2    Völker, H.3    Stüben, D.4    Botz, R.5    Stoffers, P.6    Dando, P.R.7    Thomm, M.8
  • 24
    • 0001999440 scopus 로고
    • Diversity of extremely thermophilic archaebacteria
    • (Brock, T.D., Ed.), John Wiley, New York, NY
    • [24] Stetter, K.O. (1986) Diversity of extremely thermophilic archaebacteria. In: Thermophiles: General, Molecular and Applied Microbiology (Brock, T.D., Ed.), pp. 39-74, John Wiley, New York, NY.
    • (1986) Thermophiles: General, Molecular and Applied Microbiology , pp. 39-74
    • Stetter, K.O.1
  • 25
    • 0031953266 scopus 로고    scopus 로고
    • Sulfur-inhibited Thermosphaera aggregans sp. nov., a new genus of hyperthermophilic archaea isolated after its prediction from environmentally derived 16S rRNA sequences
    • [25] Huber, R., Dyba, D., Huber, H., Burggraf, S. and Rachel, R. (1998) Sulfur-inhibited Thermosphaera aggregans sp. nov., a new genus of hyperthermophilic archaea isolated after its prediction from environmentally derived 16S rRNA sequences. Int. J. Syst. Bacteriol. 48, 31-38.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 31-38
    • Huber, R.1    Dyba, D.2    Huber, H.3    Burggraf, S.4    Rachel, R.5
  • 26
    • 0001142734 scopus 로고
    • Staphylothermus marinus sp. nov. represents a novel genus of extremely thermophilic submarine heterotrophic archaebaeteria growing up to 98°C
    • [26] Fiala, G., Stetter, K.O., Jannasch, H., Langworthy, T. and Madon, J. (1986) Staphylothermus marinus sp. nov. Represents a novel genus of extremely thermophilic submarine heterotrophic archaebaeteria growing up to 98°C. Syst. Appl. Microbiol. 8, 106-113.
    • (1986) Syst. Appl. Microbiol. , vol.8 , pp. 106-113
    • Fiala, G.1    Stetter, K.O.2    Jannasch, H.3    Langworthy, T.4    Madon, J.5
  • 28
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov., represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • [28] Fiala, G. and Stetter, K.O. (1986) Pyrococcus furiosus sp. nov., represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 145, 56-61.
    • (1986) Arch. Microbiol. , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 30
    • 0032076622 scopus 로고    scopus 로고
    • Thermococcus acidaminovorans sp. nov., a new hyperthermophilic alkalophilic archaeon growing on amino acids
    • [30] Dirmeier, R., Keller, M., Hafenbradl, D., Braun, F.-J., Rachel, R., Burggraf, S. and Stetter, K.O. (1998) Thermococcus acidaminovorans sp. nov., a new hyperthermophilic alkalophilic archaeon growing on amino acids. Extremophiles 2, 109-114.
    • (1998) Extremophiles , vol.2 , pp. 109-114
    • Dirmeier, R.1    Keller, M.2    Hafenbradl, D.3    Braun, F.-J.4    Rachel, R.5    Burggraf, S.6    Stetter, K.O.7
  • 31
    • 0025101757 scopus 로고
    • Thermococcus litoralis sp. nov.: A new species of extremely thermophilic marine archaebacteria
    • [31] Neuner, A., Jannasch, H., Belkin, S. and Stetter, K.O. (1990) Thermococcus litoralis sp. nov.: a new species of extremely thermophilic marine archaebacteria. Arch. Microbiol. 153, 205-207.
    • (1990) Arch. Microbiol. , vol.153 , pp. 205-207
    • Neuner, A.1    Jannasch, H.2    Belkin, S.3    Stetter, K.O.4
  • 32
    • 0000042905 scopus 로고
    • Caldococcus litoralis, gen. nov. Sp. nov. a new marine, extremely thermophilic, sulfur-reducing archaebacterium
    • [32] Svetlichnyi, V.A., Slesarev, A.I., Svetlichnaya, T.P. and Zavarzin, G.A. (1987) Caldococcus litoralis, gen. nov. sp. nov. a new marine, extremely thermophilic, sulfur-reducing archaebacterium. Mikrobiologiya 56, 831-838.
    • (1987) Mikrobiologiya , vol.56 , pp. 831-838
    • Svetlichnyi, V.A.1    Slesarev, A.I.2    Svetlichnaya, T.P.3    Zavarzin, G.A.4
  • 33
    • 11144313963 scopus 로고
    • Thermoplasma acidophilum and Thermoplasma volcanicum sp. nov. from solfatara fields
    • [33] Segerer, A., Langworthy, T. and Stetter, K.O. (1988) Thermoplasma acidophilum and Thermoplasma volcanicum sp. nov. from solfatara fields. System. Appl. Microbiol. 10, 161-171.
    • (1988) System. Appl. Microbiol. , vol.10 , pp. 161-171
    • Segerer, A.1    Langworthy, T.2    Stetter, K.O.3
  • 34
    • 0020643560 scopus 로고
    • Reduction of molecular sulphur by methanogenic archaea
    • [34] Stetter, K.O. and Gaag, G. (1983) Reduction of molecular sulphur by methanogenic archaea. Nature 305, 309-311.
    • (1983) Nature , vol.305 , pp. 309-311
    • Stetter, K.O.1    Gaag, G.2
  • 36
    • 0029932594 scopus 로고    scopus 로고
    • Formation of ammonium from nitrate during chemolithoautotrophic growth of the extremely thermophilic bacterium Ammonifex degensii gen. nov. sp. nov.
    • [36] Huber, R., Rossnagel, P., Woese, C.R., Rachel, R., Langwors thy, T. and Stetter, K.O. (1996) Formation of ammonium from nitrate during chemolithoautotrophic growth of the extremely thermophilic bacterium Ammonifex degensii gen. nov. sp. nov. Syst. Appl. Microbiol. 19, 40-49.
    • (1996) Syst. Appl. Microbiol. , vol.19 , pp. 40-49
    • Huber, R.1    Rossnagel, P.2    Woese, C.R.3    Rachel, R.4    Langworthy, T.5    Stetter, K.O.6
  • 37
    • 0031854856 scopus 로고    scopus 로고
    • Desulfurobacterium thermolithotrophicum gen. nov., sp. nov., a novel autotrophic, sulphur-reducing bacterium isolated from a deep-sea hydrothermal vent
    • [37] L'Haridon, S., Cilia, V., Messner, P., Raguéntès, G., Gambacorta, A., Sleytr, U.B., Prieur, D. and Jeanthon, C. (1998) Desulfurobacterium thermolithotrophicum gen. nov., sp. nov., a novel autotrophic, sulphur-reducing bacterium isolated from a deep-sea hydrothermal vent. Int. J. Syst. Bacteriol. 48, 707-771.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 707-771
    • L'Haridon, S.1    Cilia, V.2    Messner, P.3    Raguéntès, G.4    Gambacorta, A.5    Sleytr, U.B.6    Prieur, D.7    Jeanthon, C.8
  • 38
    • 0017304611 scopus 로고
    • Desulfuromonas acetoxidans gen. nov. and sp. nov., a new anaerobic, sulfur-reducing, acetate oxidizing bacterium
    • [38] Pfennig, N. and Biebl, H. (1976) Desulfuromonas acetoxidans gen. nov. and sp. nov., a new anaerobic, sulfur-reducing, acetate oxidizing bacterium. Arch. Microbiol. 110, 3-12.
    • (1976) Arch. Microbiol. , vol.110 , pp. 3-12
    • Pfennig, N.1    Biebl, H.2
  • 39
    • 0028077780 scopus 로고
    • Phylogenetic analysis of five strains of Gram-negative, obligately anaerobic, sulfur-reducing bacteria and description of Desulfuromusa gen. nov., including Desulfuromusa kysingii sp. nov., Desulfuromusa bakii sp. nov., and Desulfuromusa succinoxidans sp. nov.
    • [39] Liesack, W. and Finster, K. (1994) Phylogenetic analysis of five strains of Gram-negative, obligately anaerobic, sulfur-reducing bacteria and description of Desulfuromusa gen. nov., including Desulfuromusa kysingii sp. nov., Desulfuromusa bakii sp. nov., and Desulfuromusa succinoxidans sp. nov. Int. J. Syst. Bacteriol. 44, 753-758.
    • (1994) Int. J. Syst. Bacteriol. , vol.44 , pp. 753-758
    • Liesack, W.1    Finster, K.2
  • 40
    • 0025169910 scopus 로고
    • Desulfurella acetivorans gen. nov. and sp. nov. a new thermophilic sulfur-reducing eubacterium
    • [40] Bonch-Osmolovskaya, E.A., Sokolova, T.G., Kostrikina, N.A. and Zavarzin, G.A. (1990) Desulfurella acetivorans gen. nov. and sp. nov. a new thermophilic sulfur-reducing eubacterium. Arch. Microbiol. 153, 151-155.
    • (1990) Arch. Microbiol. , vol.153 , pp. 151-155
    • Bonch-Osmolovskaya, E.A.1    Sokolova, T.G.2    Kostrikina, N.A.3    Zavarzin, G.A.4
  • 41
    • 0025041374 scopus 로고
    • Different mechanisms of acetate activation in Desulfurella acetivorans and Desulfuromonas acetoxidans
    • [41] Schmitz, R.A., Bonch-Osmolovskaya, E.A. and Thauer, R.K. (1990) Different mechanisms of acetate activation in Desulfurella acetivorans and Desulfuromonas acetoxidans. Arch. Microbiol. 154, 274-279.
    • (1990) Arch. Microbiol. , vol.154 , pp. 274-279
    • Schmitz, R.A.1    Bonch-Osmolovskaya, E.A.2    Thauer, R.K.3
  • 42
    • 0017618229 scopus 로고
    • Growth of sulfate-reducing bacteria with sulfur as electron acceptor
    • [42] Biebl, H. and Pfennig, N. (1977) Growth of sulfate-reducing bacteria with sulfur as electron acceptor. Arch. Microbiol. 112, 115-117.
    • (1977) Arch. Microbiol. , vol.112 , pp. 115-117
    • Biebl, H.1    Pfennig, N.2
  • 43
    • 0025282531 scopus 로고
    • Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the 'Thermotogales'
    • [43] Huber, R., Woese, C.R., Langworthy, T., Kristjansson, J. and Stetter, K.O. (1990) Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the 'Thermotogales'. Arch. Microbiol. 154, 105-111.
    • (1990) Arch. Microbiol. , vol.154 , pp. 105-111
    • Huber, R.1    Woese, C.R.2    Langworthy, T.3    Kristjansson, J.4    Stetter, K.O.5
  • 44
    • 0021906874 scopus 로고
    • Fervidobacterium nodosum gen. nov. and spec. nov., a new chemoorganotrophic, caldoactive, anaerobic bacterium
    • [44] Patel, B.K., Morgan, H.W. and Daniel, R.M. (1985) Fervidobacterium nodosum gen. nov. and spec. nov., a new chemoorganotrophic, caldoactive, anaerobic bacterium. Arch. Microbiol. 141, 63-69.
    • (1985) Arch. Microbiol. , vol.141 , pp. 63-69
    • Patel, B.K.1    Morgan, H.W.2    Daniel, R.M.3
  • 47
    • 0029992689 scopus 로고    scopus 로고
    • Growth of the facultative anaerobe Shewanella putrefaciens by elemental sulfur reduction
    • [47] Moser, D.P. and Nealson, K.H. (1996) Growth of the facultative anaerobe Shewanella putrefaciens by elemental sulfur reduction. Appl. Environ. Microbiol. 62, 2100-2105.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2100-2105
    • Moser, D.P.1    Nealson, K.H.2
  • 48
    • 0017381204 scopus 로고
    • Reduction of sulfur by Spirillum 5175 and syntrophism with Chlorobium
    • [48] Wolfe, R.S. and Pfennig, N. (1977) Reduction of sulfur by Spirillum 5175 and syntrophism with Chlorobium. Appl. Environ. Microbiol. 33, 427-433.
    • (1977) Appl. Environ. Microbiol. , vol.33 , pp. 427-433
    • Wolfe, R.S.1    Pfennig, N.2
  • 49
    • 0030853122 scopus 로고    scopus 로고
    • Sulfurospirillum arcachonense sp. nov., a new microaerophilic sulfur-reducing bacterium
    • [49] Finster, K., Liesack, W. and Tindall, B.J. (1997) Sulfurospirillum arcachonense sp. nov., a new microaerophilic sulfur-reducing bacterium. Int. J. Syst. Bacteriol. 47, 1212-1217.
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 1212-1217
    • Finster, K.1    Liesack, W.2    Tindall, B.J.3
  • 50
    • 0000040113 scopus 로고
    • Thermotoga thermarum sp. nov. and thermotoga neapolitana occurring in African continental solfataric springs
    • [50] Windberger, E., Huber, R., Trincone, A., Fricke, H. and Stetter, K.O. (1989) Thermotoga thermarum sp. nov. and Thermotoga neapolitana occurring in African continental solfataric springs. Arch. Microbiol. 151, 506-512.
    • (1989) Arch. Microbiol. , vol.151 , pp. 506-512
    • Windberger, E.1    Huber, R.2    Trincone, A.3    Fricke, H.4    Stetter, K.O.5
  • 51
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C
    • [51] Huber, R., Langworthy, T., König, H., Thomm, M., Woese, C.R., Sleytr, U.B. and Stetter, K.O. (1986) Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C. Arch. Microbiol. 144, 324-333.
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.2    König, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 52
    • 0001980444 scopus 로고
    • Thermosipho africanus gen. nov., represents a new genus of thermophilic eubacteria within the 'Thermotogales'
    • [52] Huber, R., Woese, C.R., Langworthy, T., Fricke, H. and Stetter, K.O. (1989) Thermosipho africanus gen. nov., represents a new genus of thermophilic eubacteria within the 'Thermotogales'. Syst. Appl. Microbiol. 12, 32-37.
    • (1989) Syst. Appl. Microbiol. , vol.12 , pp. 32-37
    • Huber, R.1    Woese, C.R.2    Langworthy, T.3    Fricke, H.4    Stetter, K.O.5
  • 53
    • 0030829566 scopus 로고    scopus 로고
    • Thermosipho melanesiensis sp. nov., a new thermophilic anaerobic bacterium belonging to the order Thermotogales, isolated from deep-sea hydrothermal vents in the Southwestern Pacific Ocean
    • [53] Antoine, E., Cilia, V., Meunier, J.R., Guezennec, J., Lesogeur, F. and Barbier, G. (1997) Thermosipho melanesiensis sp. nov., a new thermophilic anaerobic bacterium belonging to the order Thermotogales, isolated from deep-sea hydrothermal vents in the Southwestern Pacific Ocean. Int. J. Syst. Bacteriol. 47, 1118-1123.
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 1118-1123
    • Antoine, E.1    Cilia, V.2    Meunier, J.R.3    Guezennec, J.4    Lesogeur, F.5    Barbier, G.6
  • 55
    • 0003206888 scopus 로고    scopus 로고
    • Volcanoes, hydrothermal venting, and the origin of life
    • (Marti, J. and Ernst. G.J., Eds.). Cambridge University Press, in press
    • [55] Stetter, K.O. (1998) Volcanoes, hydrothermal venting, and the origin of life. In: Volcanoes and the Environment (Marti, J. and Ernst. G.J., Eds.). Cambridge University Press, in press.
    • (1998) Volcanoes and the Environment
    • Stetter, K.O.1
  • 56
    • 0027676205 scopus 로고
    • Hyperthermophilic archaea are thriving in deep North Sea and Alaskan oil reservoirs
    • [56] Stetter, K.O., Huber, R., Blöchl, E., Kurr, M., Eden, R.D., Fielder, M., Cash, H. and Vance, I. (1993) Hyperthermophilic archaea are thriving in deep North Sea and Alaskan oil reservoirs. Nature 365, 743-745.
    • (1993) Nature , vol.365 , pp. 743-745
    • Stetter, K.O.1    Huber, R.2    Blöchl, E.3    Kurr, M.4    Eden, R.D.5    Fielder, M.6    Cash, H.7    Vance, I.8
  • 57
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • [57] Stetter, K.O. (1996) Hyperthermophilic procaryotes. FEMS Microbiol. Rev. 18, 149-158.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 58
    • 0013593818 scopus 로고    scopus 로고
    • Primitive archaea and bacteria in the cycles of sulfur and nitrogen near the temperature limit of life
    • Progress in Microbial Ecology, Santos, Sao Paulo, Brazil, 1995 (Martins, M.T. et al., Eds.), SBM/ICOME, Sao Paulo
    • [58] Stetter, K.O. (1997) Primitive archaea and bacteria in the cycles of sulfur and nitrogen near the temperature limit of life. In: Progress in Microbial Ecology. Proceedings of Seventh International Symposium on Microbial Ecology, Santos, Sao Paulo, Brazil, 1995 (Martins, M.T. et al., Eds.), pp. 55-61. SBM/ICOME, Sao Paulo.
    • (1997) Proceedings of Seventh International Symposium on Microbial Ecology , pp. 55-61
    • Stetter, K.O.1
  • 59
    • 0002076521 scopus 로고
    • The genus Desulfuromonas and other Gram-negative sulfur-reducing eubacteria
    • Balows, A., Trüper, H.G., Dwarkin, M., Harder, W. and Schleifer, K.-H., Eds.
    • [59] Widdel, F. and Pfennig, N. (1991) The genus Desulfuromonas and other Gram-negative sulfur-reducing eubacteria. In: The Prokaryotes (Balows, A., Trüper, H.G., Dwarkin, M., Harder, W. and Schleifer, K.-H., Eds.), pp. 3379-3389.
    • (1991) The Prokaryotes , pp. 3379-3389
    • Widdel, F.1    Pfennig, N.2
  • 60
    • 0002351623 scopus 로고
    • Investigations on microbial sulfur respiration. I. Activation and reduction of elemental sulfur in several strains of eubacteria
    • [60] Zöphel, A., Kennedy, M.C., Beinert, Z.H. and Kroneck, P.M.H. (1988) Investigations on microbial sulfur respiration. I. Activation and reduction of elemental sulfur in several strains of eubacteria. Arch. Microbiol. 150, 72-77.
    • (1988) Arch. Microbiol. , vol.150 , pp. 72-77
    • Zöphel, A.1    Kennedy, M.C.2    Beinert, Z.H.3    Kroneck, P.M.H.4
  • 61
    • 0022628946 scopus 로고
    • ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans
    • [61] Paulsen, J., Kröger, A. and Thauer, R.K. (1986) ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans. Arch. Microbiol. 144, 78-83.
    • (1986) Arch. Microbiol. , vol.144 , pp. 78-83
    • Paulsen, J.1    Kröger, A.2    Thauer, R.K.3
  • 62
    • 0001342119 scopus 로고
    • Solubility of elemental sulfur in water at 298 K
    • [62] Boulégue, J. (1978) Solubility of elemental sulfur in water at 298 K. Phosphorus Sulfur 5, 127-128.
    • (1978) Phosphorus Sulfur , vol.5 , pp. 127-128
    • Boulégue, J.1
  • 63
    • 0001655308 scopus 로고
    • Optical spectra and equilibrium distribution of polysulfide ions in aqueous solution at 20°
    • [63] Giggenbach, W. (1972) Optical spectra and equilibrium distribution of polysulfide ions in aqueous solution at 20°. Inorg. Chem. 11, 1201-1207.
    • (1972) Inorg. Chem. , vol.11 , pp. 1201-1207
    • Giggenbach, W.1
  • 64
    • 0026018923 scopus 로고
    • Growth of Wolinella succinogenes with polysulphide as terminal acceptor of phosphorylative electron transport
    • [64] Klimmek, O., Kröger, A., Steudel, R. and Holdt, G. (1991) Growth of Wolinella succinogenes with polysulphide as terminal acceptor of phosphorylative electron transport. Arch. Microbiol. 155, 177-182.
    • (1991) Arch. Microbiol. , vol.155 , pp. 177-182
    • Klimmek, O.1    Kröger, A.2    Steudel, R.3    Holdt, G.4
  • 65
    • 0000240553 scopus 로고
    • Hydrogen sulphide ionization and sulphur hydrolysis in high temperature solution
    • [65] Ellis, A.J. and Giggenbach, W. (1971) Hydrogen sulphide ionization and sulphur hydrolysis in high temperature solution. Geochim. Cosmochim. Acta 35, 247-260.
    • (1971) Geochim. Cosmochim. Acta , vol.35 , pp. 247-260
    • Ellis, A.J.1    Giggenbach, W.2
  • 66
    • 84981833621 scopus 로고
    • Die acidität der sulfane und die zusammensetzung wässeriger polysulfidlösungen
    • [66] Schwarzenbach, G. and Fischer, A. (1960) Die Acidität der Sulfane und die Zusammensetzung wässeriger Polysulfidlösungen. Helv. Chim. Acta 43, 1365-1388.
    • (1960) Helv. Chim. Acta , vol.43 , pp. 1365-1388
    • Schwarzenbach, G.1    Fischer, A.2
  • 67
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • [67] Thauer, R.K., Jungermann, K. and 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
  • 68
    • 0014139748 scopus 로고
    • The standard redox potential of cysteine-cystine from the thiol-disulphide exchange reaction with glutathione and lipoic acid
    • [68] Jocelyn, P.C. (1967) The standard redox potential of cysteine-cystine from the thiol-disulphide exchange reaction with glutathione and lipoic acid. Eur. J. Biochem. 2, 327-331.
    • (1967) Eur. J. Biochem. , vol.2 , pp. 327-331
    • Jocelyn, P.C.1
  • 69
    • 0013565585 scopus 로고
    • Dissertation Nr 3871, ETH Zürich
    • [69] Schnorf, U. (1966) Dissertation Nr 3871, ETH Zürich.
    • (1966)
    • Schnorf, U.1
  • 70
    • 0027486711 scopus 로고
    • Polysulphide as a possible substrate for sulphur-reducing bacteria
    • [70] Schauder, R. and Müller E. (1993) Polysulphide as a possible substrate for sulphur-reducing bacteria. Arch. Microbiol. 160, 377-382.
    • (1993) Arch. Microbiol. , vol.160 , pp. 377-382
    • Schauder, R.1    Müller, E.2
  • 71
    • 0032053559 scopus 로고    scopus 로고
    • The function of the periplasmic Sud protein in polysulfide respiration of Wolinella succinogenes
    • [71] Klimmek, O., Kreis, V., Klein, C., Simon, J., Wittershagen, A. and Kröger, A. (1998) The function of the periplasmic Sud protein in polysulfide respiration of Wolinella succinogenes. Eur. J. Biochem. 253, 263-269.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 263-269
    • Klimmek, O.1    Kreis, V.2    Klein, C.3    Simon, J.4    Wittershagen, A.5    Kröger, A.6
  • 72
    • 0029016693 scopus 로고
    • The function of Wolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor
    • [72] Krafft, T., Groß, R. and Kröger, A. (1995) The function of Wolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor. Eur. J. Biochem. 230, 601-606.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 601-606
    • Krafft, T.1    Groß, R.2    Kröger, A.3
  • 73
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100°C
    • [73] Adams, M.W.W. (1993) Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47, 627-658.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 627-658
    • Adams, M.W.W.1
  • 74
    • 0030042711 scopus 로고    scopus 로고
    • Growth of Wolinella succinogenes with elemental sulfur in the absence of polysulfide
    • [74] Ringel, M., Groß, R., Krafft, T., Kröger, A. and Schauder, R. (1996) Growth of Wolinella succinogenes with elemental sulfur in the absence of polysulfide. Arch. Microbiol. 165, 62-64.
    • (1996) Arch. Microbiol. , vol.165 , pp. 62-64
    • Ringel, M.1    Groß, R.2    Krafft, T.3    Kröger, A.4    Schauder, R.5
  • 75
    • 0000927154 scopus 로고
    • The electrochemical proton potential generated by the sulphur respiration of Wolinella succinogenes
    • [75] Wloczyk, C., Kröger, A., Göbel, T., Holdt, G. and Steudel, R. (1989) The electrochemical proton potential generated by the sulphur respiration of Wolinella succinogenes. Arch. Microbiol. 152, 600-605.
    • (1989) Arch. Microbiol. , vol.152 , pp. 600-605
    • Wloczyk, C.1    Kröger, A.2    Göbel, T.3    Holdt, G.4    Steudel, R.5
  • 76
    • 0020322828 scopus 로고
    • Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source
    • [76] Bronder, M., Mell, H., Stupperich, E. and Kröger, A. (1982) Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source. Arch. Microbiol. 131, 216-223.
    • (1982) Arch. Microbiol. , vol.131 , pp. 216-223
    • Bronder, M.1    Mell, H.2    Stupperich, E.3    Kröger, A.4
  • 77
    • 0020323003 scopus 로고
    • Cell yields of Vibrio succinogenes growing with formate and fumarate as sole carbon and energy sources in chemostat culture
    • [77] Mell, H., Bronder, M. and Kröger A. (1982) Cell yields of Vibrio succinogenes growing with formate and fumarate as sole carbon and energy sources in chemostat culture. Arch. Microbiol. 131, 224-228.
    • (1982) Arch. Microbiol. , vol.131 , pp. 224-228
    • Mell, H.1    Bronder, M.2    Kröger, A.3
  • 78
    • 0019432486 scopus 로고
    • Phosphorylative fumarate reduction in Vibrio succinogenes: Stoichiometry of ATP synthesis
    • [78] Kröger, A. and Winkler, E. (1981) Phosphorylative fumarate reduction in Vibrio succinogenes: Stoichiometry of ATP synthesis. Arch. Microbiol. 129, 100-104.
    • (1981) Arch. Microbiol. , vol.129 , pp. 100-104
    • Kröger, A.1    Winkler, E.2
  • 79
    • 0023647453 scopus 로고
    • Correlation of the turnover number of the ATP synthase in liposomes with the proton flux and the proton potential across the membrane
    • [79] Brune, A., Spillecke, J. and Kröger, A. (1987) Correlation of the turnover number of the ATP synthase in liposomes with the proton flux and the proton potential across the membrane. Biochim. Biophys. Acta 893, 499-507.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 499-507
    • Brune, A.1    Spillecke, J.2    Kröger, A.3
  • 80
    • 0001350244 scopus 로고
    • Isolation of the sulphur reductase and reconstitution of the sulphur respiration of Wolinella succinogenes
    • [80] Schröder, I., Kröger, A. and Macy, J.M. (1988) Isolation of the sulphur reductase and reconstitution of the sulphur respiration of Wolinella succinogenes. Arch. Microbiol. 149, 572-579.
    • (1988) Arch. Microbiol. , vol.149 , pp. 572-579
    • Schröder, I.1    Kröger, A.2    Macy, J.M.3
  • 81
    • 0026550359 scopus 로고
    • Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase
    • [81] Krafft, T., Bokranz, M., Klimmek, O., Schröder, I., Fahrenhotz, F., Kojro, E. and Kröger, A. (1992) Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase. Eur. J. Biochem. 206, 503-510.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 503-510
    • Krafft, T.1    Bokranz, M.2    Klimmek, O.3    Schröder, I.4    Fahrenhotz, F.5    Kojro, E.6    Kröger, A.7
  • 82
    • 0027996165 scopus 로고
    • Polysulphide reductase and formate dehydrogenase from Wolinella succinogenes contain molybdopterin guanine dinucleotide
    • [82] Jankielewiez, A., Schmitz, R.A., Klimmek, O. and Kröger, A. (1994) Polysulphide reductase and formate dehydrogenase from Wolinella succinogenes contain molybdopterin guanine dinucleotide. Arch. Microbiol. 162, 238-242.
    • (1994) Arch. Microbiol. , vol.162 , pp. 238-242
    • Jankielewiez, A.1    Schmitz, R.A.2    Klimmek, O.3    Kröger, A.4
  • 83
    • 0013620682 scopus 로고    scopus 로고
    • Dissertation, FB Biologie, University of Frankfurt
    • [83] Klimmek, O. (1996) Dissertation, FB Biologie, University of Frankfurt.
    • (1996)
    • Klimmek, O.1
  • 85
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • [85] Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K.V. and Rees, D.C. (1996) Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science 272, 1615-1621.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 86
    • 0031043109 scopus 로고    scopus 로고
    • Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
    • [86] Boyington, J.C., Gladyshev, V.N., Khangulov, S.V., Stadtman, T.C. and Sun, P.D. (1997) Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275, 1305-1308.
    • (1997) Science , vol.275 , pp. 1305-1308
    • Boyington, J.C.1    Gladyshev, V.N.2    Khangulov, S.V.3    Stadtman, T.C.4    Sun, P.D.5
  • 87
    • 0031811217 scopus 로고    scopus 로고
    • Two membrane anchors of Wolinella succinogenes hydrogenase and their function in fumarate and polysulfide respiration
    • [87] Groß, R., Simon, J., Theis, F. and Kröger, A. (1998) Two membrane anchors of Wolinella succinogenes hydrogenase and their function in fumarate and polysulfide respiration. Arch. Microbiol. 170, 50-58.
    • (1998) Arch. Microbiol. , vol.170 , pp. 50-58
    • Groß, R.1    Simon, J.2    Theis, F.3    Kröger, A.4
  • 88
    • 0013593621 scopus 로고
    • The function of menaquinone in bacterial electron transport
    • (Lenaz, G., Ed.), John Wiley, Chichester
    • [88] Kröger, A. and Unden, G. (1985) The function of menaquinone in bacterial electron transport. In: Coenzyme Q (Lenaz, G., Ed.), pp. 285-300. John Wiley, Chichester.
    • (1985) Coenzyme Q , pp. 285-300
    • Kröger, A.1    Unden, G.2
  • 90
    • 0029094712 scopus 로고
    • The electron transfer from hydrogenase and formate dehydrogenase to polysulfide reductase in the membrane of Wolinella succinogenes
    • [90] Jankielewicz, A., Klimmek, O. and Kröger, A. (1995) The electron transfer from hydrogenase and formate dehydrogenase to polysulfide reductase in the membrane of Wolinella succinogenes. Biochim. Biophys. Acta 1231, 157-162.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 157-162
    • Jankielewicz, A.1    Klimmek, O.2    Kröger, A.3
  • 91
    • 0000291826 scopus 로고
    • Rates of diffusion controlled reactions in one, two and three dimensions
    • [91] Hardt, S.L. (1979) Rates of diffusion controlled reactions in one, two and three dimensions. Biophys. Chem. 10, 239-243.
    • (1979) Biophys. Chem. , vol.10 , pp. 239-243
    • Hardt, S.L.1
  • 92
    • 0023808978 scopus 로고
    • The multicollisional, obstructed, long-range diffusional nature of mitochondrial electron transport
    • [92] Chazotte, B. and Hackenbrock, C.R. (1988) The multicollisional, obstructed, long-range diffusional nature of mitochondrial electron transport. Biol. Chem. 28, 14359-14367.
    • (1988) Biol. Chem. , vol.28 , pp. 14359-14367
    • Chazotte, B.1    Hackenbrock, C.R.2
  • 93
    • 0022821997 scopus 로고
    • Reconstitution of a functional electron transport chain from purified formate dehydrogenase and fumarate reductase complex
    • [93] Unden, G. and Kröger, A. (1986) Reconstitution of a functional electron transport chain from purified formate dehydrogenase and fumarate reductase complex. Methods Enzymol. 126, 387-399.
    • (1986) Methods Enzymol. , vol.126 , pp. 387-399
    • Unden, G.1    Kröger, A.2
  • 95
    • 0028944291 scopus 로고
    • Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop
    • [95] Berks, B.C., Dudley Page, M., Richardson, D.J., Reilly, A., Cavill, A., Outen, F. and Ferguson, S.J. (1995) Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop. Mol. Microbiol. 15, 319-331.
    • (1995) Mol. Microbiol. , vol.15 , pp. 319-331
    • Berks, B.C.1    Dudley Page, M.2    Richardson, D.J.3    Reilly, A.4    Cavill, A.5    Outen, F.6    Ferguson, S.J.7
  • 96
    • 0027411256 scopus 로고
    • Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors
    • [96] Lorenzen, J.P., Kröger, A. and Unden, G. (1993) Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors. Arch. Microbiol. 159, 477-483.
    • (1993) Arch. Microbiol. , vol.159 , pp. 477-483
    • Lorenzen, J.P.1    Kröger, A.2    Unden, G.3
  • 98
    • 0028798864 scopus 로고
    • Periplasmic sulphide dehydrogenase (Sud) from Wolinella succinogenes: Isolation, nucleotide sequence of the sud gene and its expression in Escherichia coli
    • [98] Kreis-Kleinschmidt, V., Fahrenholz, F., Kojro, E. and Kröger, A. (1995) Periplasmic sulphide dehydrogenase (Sud) from Wolinella succinogenes: Isolation, nucleotide sequence of the sud gene and its expression in Escherichia coli. Eur. J. Biochem. 227, 137-142.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 137-142
    • Kreis-Kleinschmidt, V.1    Fahrenholz, F.2    Kojro, E.3    Kröger, A.4
  • 99
    • 0028218045 scopus 로고
    • The direction of the proton exchange associated with the redox reactions of menaquinone during the electron transport in Wolinella succinogenes
    • [99] Geisler, V., Ullmann, R. and Kröger, A. (1994) The direction of the proton exchange associated with the redox reactions of menaquinone during the electron transport in Wolinella succinogenes. Biochim. Biophys. Acta 1184, 219-226.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 219-226
    • Geisler, V.1    Ullmann, R.2    Kröger, A.3
  • 100
    • 0027163125 scopus 로고
    • Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor
    • [100] Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W.W. (1993) Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90, 5341-5344.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5341-5344
    • Ma, K.1    Schicho, R.N.2    Kelly, R.M.3    Adams, M.W.W.4
  • 101
    • 0027945387 scopus 로고
    • Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: A new multifunctional enzyme involved in the reduction of elemental sulfur
    • [101] Ma, K. and Adams, M.W. (1994) Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J. Bacteriol. 176, 6509-6517.
    • (1994) J. Bacteriol. , vol.176 , pp. 6509-6517
    • Ma, K.1    Adams, M.W.2
  • 105
    • 0029688839 scopus 로고    scopus 로고
    • Respiratory metabolism in hyperthermophilic organisms: Hydrogenases, sulfur reductases, and electron transport factors that function at temperatures exceeding 100°C
    • [105] Maier, R.J. (1996) Respiratory metabolism in hyperthermophilic organisms: hydrogenases, sulfur reductases, and electron transport factors that function at temperatures exceeding 100°C. Adv. Prot. Chem. 48, 35-73.
    • (1996) Adv. Prot. Chem. , vol.48 , pp. 35-73
    • Maier, R.J.1
  • 106
    • 0026064181 scopus 로고
    • Purification and characterization of the hydrogen uptake hydrogenase from the hyperthermophilic archaebacteruim Pyrodictium brockii
    • [106] Pihl, T.D. and Maier, R.J. (1991) Purification and characterization of the hydrogen uptake hydrogenase from the hyperthermophilic archaebacteruim Pyrodictium brockii. J. Bacteriol. 173, 1839-1844.
    • (1991) J. Bacteriol. , vol.173 , pp. 1839-1844
    • Pihl, T.D.1    Maier, R.J.2
  • 107
    • 0026557724 scopus 로고
    • Hydrogen-oxidizing electron transport components in the hyperthermophilic archaebacterium Pyrodictium brockii
    • [107] Pihl, T.D., Black, L.K., Schulman, B.A. and Maier, R.J. (1992) Hydrogen-oxidizing electron transport components in the hyperthermophilic archaebacterium Pyrodictium brockii. J. Bacteriol. 174, 137-143.
    • (1992) J. Bacteriol. , vol.174 , pp. 137-143
    • Pihl, T.D.1    Black, L.K.2    Schulman, B.A.3    Maier, R.J.4
  • 108
    • 0025237789 scopus 로고
    • 2 to the heterodisulfide of 2-mercaptoethane-sulfonate and 7-mercaptoheptanoylthreonine phosphate in vesicle preparations of the methanogenic bacterium strain Göl
    • 2 to the heterodisulfide of 2-mercaptoethane-sulfonate and 7-mercaptoheptanoylthreonine phosphate in vesicle preparations of the methanogenic bacterium strain Göl. FEBS Lett. 263, 57-60.
    • (1990) FEBS Lett. , vol.263 , pp. 57-60
    • Peinemann, S.1    Hedderich, R.2    Blaut, M.3    Thauer, R.K.4    Gottschalk, G.5
  • 110
    • 0025979785 scopus 로고
    • 2:Heterodisulfide oxidoreductase, a second energy-conserving system in the methanogenic strain Gö l
    • 2:heterodisulfide oxidoreductase, a second energy-conserving system in the methanogenic strain Gö l. Arch. Microbiol. 155, 272-277.
    • (1991) Arch. Microbiol. , vol.155 , pp. 272-277
    • Deppenmeier, U.1    Blaut, M.2    Gottschalk, G.3
  • 111
    • 0031921345 scopus 로고    scopus 로고
    • Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Göl
    • [111] Abken, H.-J., Tietze, M., Brodersen, J., Bäumer, S., Beifuss, U. and Deppenmeier, U. (1998) Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Göl. 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
  • 112
    • 0002806157 scopus 로고
    • Diversity and taxonomy of methanogens
    • (Ferry, J.G., Ed.), Chapman and Hall, New-York, NY
    • [112] Boone, D.R., Whitman, W.B. and Rouvière, P. (1993) Diversity and taxonomy of methanogens. In: Methanogenesis (Ferry, J.G., Ed.), pp. 35-80. Chapman and Hall, New-York, NY.
    • (1993) Methanogenesis , pp. 35-80
    • Boone, D.R.1    Whitman, W.B.2    Rouvière, P.3
  • 114
    • 0028351576 scopus 로고
    • Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri
    • [114] Heiden, S., Hedderich, R., Setzke, E. and Thauer, R.K. (1994) Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri. Eur. J. Biochem. 221, 855-861.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 855-861
    • Heiden, S.1    Hedderich, R.2    Setzke, E.3    Thauer, R.K.4
  • 115
    • 0031055712 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanol grown cells of Methanosarcina barkeri is not a flavoenzyme
    • [115] 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 flavoenzyme. 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
  • 116
    • 0032516483 scopus 로고    scopus 로고
    • Purification and properties of the heme-and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila
    • [116] 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
  • 118
    • 0028009865 scopus 로고
    • Purification and characterization of membrane-bound hydrogenase from Methanosarcina barkeri MS
    • [118] 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
  • 119
    • 0028890441 scopus 로고
    • Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Göl, both encoding a membrane-bound hydrogenase and a cytochrome b
    • [119] Deppenmeier, U., Blaut, M., Lentes, S., Herzberg, C. and Gottschalk, G. (1995) Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Göl, 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
  • 121
    • 0028790975 scopus 로고
    • Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Göl
    • [121] Deppenmeier, U. (1995) Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Göl. Arch. Microbiol. 164, 370-376.
    • (1995) Arch. Microbiol. , vol.164 , pp. 370-376
    • Deppenmeier, U.1
  • 126
    • 0028168710 scopus 로고
    • 2:Quinone oxidoreductase from Archaeoglobus fulgidus: Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters
    • 2:quinone oxidoreductase from Archaeoglobus fulgidus: Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters. Eur. J. Biochem. 223, 503-511.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 503-511
    • Kunow, J.1    Linder, D.2    Stetter, K.O.3    Thauer, R.K.4
  • 128
    • 0025189332 scopus 로고
    • 2-dependent heterodisulfide reductase in methanogenic bacterium strain Göl and Methanolobus tindarius
    • 2-dependent heterodisulfide reductase in methanogenic bacterium strain Göl 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
  • 130
    • 0023107043 scopus 로고
    • Hydrogen metabolism during methanogenesis from acetate by Methanosarcina barkeri
    • [130] Krzycki, J.A., Morgan, J.B., Conrad, R. and Zeikus, J.G. (1987) Hydrogen metabolism during methanogenesis from acetate by Methanosarcina barkeri. FEMS Microbiol. Lett. 40, 193-198.
    • (1987) FEMS Microbiol. Lett. , vol.40 , pp. 193-198
    • Krzycki, J.A.1    Morgan, J.B.2    Conrad, R.3    Zeikus, J.G.4
  • 131
    • 0023932844 scopus 로고
    • Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila
    • [131] 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 acetate-grown Methanosarcina thermophila. J. Bacteriol. 263, 4075-4079.
    • (1988) J. Bacteriol. , vol.263 , pp. 4075-4079
    • Terlesky, K.C.1    Ferry, J.G.2
  • 132
    • 0025045750 scopus 로고
    • Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS)
    • [132] Fischer, R. and Thauer, R.K. (1990) Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS). FEBS Lett. 269, 368-372.
    • (1990) FEBS Lett. , vol.269 , pp. 368-372
    • Fischer, R.1    Thauer, R.K.2
  • 133
    • 0022779582 scopus 로고
    • 2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri
    • 2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri. Eur. J. Biochem. 159, 393-398.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 393-398
    • Bott, M.1    Eikmanns, B.2    Thauer, R.K.3
  • 135
    • 0032521598 scopus 로고
    • An E. coli hydrogenase 3 type hydrogenase in methanogenic archaea
    • [135] Künkel, A., Vorholt, J.A., Thauer, R.K. and Hedderich, R. (1995) An E. coli hydrogenase 3 type hydrogenase in methanogenic archaea. Eur. J. Biochem. 252, 467-476.
    • (1995) Eur. J. Biochem. , vol.252 , pp. 467-476
    • Künkel, A.1    Vorholt, J.A.2    Thauer, R.K.3    Hedderich, R.4
  • 136
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodaspirillum rubrum and the gene encoding the large subunit of the enzyme
    • [136] Fox, J.D., Kerby, R.L., Roberts, G.P. and Ludden, P.W. (1996) Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodaspirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178, 1515-1524.
    • (1996) J. Bacteriol. , vol.178 , pp. 1515-1524
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 137
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenylase components
    • [137] Böhm, R., Sauter, M. and Böck, A. (1990) Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenylase components. Mol. Microbiol. 4, 231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 138
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative prolon-translocation formate hydrogen lyase system
    • [138] Andrews, S.C., Berks, B.C., McClay, J., Ambler, A., Quail, M.A., Golby, P. and Guest, J.R. (1997) A 12-cistron Escherichia coli operon (hyf) encoding a putative prolon-translocation formate hydrogen lyase 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    Guest, J.R.7
  • 139
    • 0013619718 scopus 로고    scopus 로고
    • Diploma thesis, Universität Marburg
    • [139] Meuer, J. (1998) Diploma thesis, Universität Marburg.
    • (1998)
    • Meuer, J.1
  • 140
    • 0028130513 scopus 로고
    • Characterization of a CO:Heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila
    • [140] 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
  • 141
    • 0029820084 scopus 로고    scopus 로고
    • Characterization of an iron-sulfur flavoprotein from Methanosarcina thermophila
    • [141] Latimer, M.T., Painter, M.H. and Ferry, J.G. (1996) Characterization of an iron-sulfur flavoprotein from Methanosarcina thermophila. J. Biol. Chem. 271, 24023-24028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24023-24028
    • Latimer, M.T.1    Painter, M.H.2    Ferry, J.G.3
  • 142
    • 0025187801 scopus 로고
    • Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
    • [142] Hedderich, R., Berkessel, A. and Thauer, R.K. (1990) Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). 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
  • 143
    • 0028177028 scopus 로고
    • 2:Heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum: Composition and properties
    • 2:heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum: composition and properties. Eur. J. Biochem. 220, 139-148.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 139-148
    • Setzke, E.1    Hedderich, R.2    Heiden, S.3    Thauer, R.K.4
  • 144
    • 0028136101 scopus 로고
    • The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine nucleotide-dependent thioredoxin reductases
    • [144] Hedderich, R., Koch, J., Linder, D. and Thauer, R.K. (1994) The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine nucleotide-dependent thioredoxin reductases. Eur. J. Biochem. 225, 253-261.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 253-261
    • Hedderich, R.1    Koch, J.2    Linder, D.3    Thauer, R.K.4
  • 146
    • 0026502227 scopus 로고
    • Isolation and characterization of polyferredoxin from Methanobacterium thermoautotrophicum. The mvhB gene product or the methylviologen-reducing hydrogenase operon
    • [146] Hedderich, R., Albracht, S.P.J., Linder, D., Koch, J. and Thauer, R.K. (1992) Isolation and characterization of polyferredoxin from Methanobacterium thermoautotrophicum. The mvhB gene product or the methylviologen-reducing hydrogenase operon. FEBS Lett. 298, 65-68.
    • (1992) FEBS Lett. , vol.298 , pp. 65-68
    • Hedderich, R.1    Albracht, S.P.J.2    Linder, D.3    Koch, J.4    Thauer, R.K.5
  • 147
    • 0026693115 scopus 로고
    • Identification and isolation of the polyferredoxin from Methanobactirium thermoautotraphicum strain ΔH
    • [147] Steigerwald, V.J., Pihl, T.D. and Reeve, J.N. (1992) Identification and isolation of the polyferredoxin from Methanobactirium thermoautotraphicum strain ΔH. Proc. Natl. Acad. Sci. USA 89, 6929-6933.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6929-6933
    • Steigerwald, V.J.1    Pihl, T.D.2    Reeve, J.N.3
  • 150
    • 0031016808 scopus 로고    scopus 로고
    • Hydrogen regulation of growth, growth yields, and methane gene transcription in Methanobacterium thermoautotrophicum ΔH
    • [150] Morgan, R.M., Pihl, T.D., Nölling, J. and Reeve, J.N. (1997) Hydrogen regulation of growth, growth yields, and methane gene transcription in Methanobacterium thermoautotrophicum ΔH. J. Bacteriol. 179, 889-898.
    • (1997) J. Bacteriol. , vol.179 , pp. 889-898
    • Morgan, R.M.1    Pihl, T.D.2    Nölling, J.3    Reeve, J.N.4
  • 152
    • 0031582715 scopus 로고    scopus 로고
    • Modular evolution of the respiratory NADH:Ubiquinone oxidoreductase and the origin of its modules
    • [152] 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
  • 154
    • 0028234206 scopus 로고
    • The energetics of bacterial growth: A reassessment
    • [154] Neijssel, O.E. and Teixera de Mattos, M.J. (1994) The energetics of bacterial growth: a reassessment. Mol. Microbiol. 13, 179-182.
    • (1994) Mol. Microbiol. , vol.13 , pp. 179-182
    • Neijssel, O.E.1    Teixera De Mattos, M.J.2
  • 155
    • 0025877458 scopus 로고
    • Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic archaea
    • [155] Schwörer, B. and Thauer, R.K. (1991) Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic archaea. Arch. Microbiol. 155, 459-465.
    • (1991) Arch. Microbiol. , vol.155 , pp. 459-465
    • Schwörer, B.1    Thauer, R.K.2
  • 156
    • 0030957417 scopus 로고    scopus 로고
    • The [NiFe] hydrogenases of Methanococcus voltae. Genes, enzymes and regulation
    • [156] Sorgenfrei, O., Müller, S., Pfeiffer, M., Sniezko, I. and Klein, A. (1997) The [NiFe] hydrogenases of Methanococcus voltae. genes, enzymes and regulation. Arch. Microbiol. 167, 189-195.
    • (1997) Arch. Microbiol. , vol.167 , pp. 189-195
    • Sorgenfrei, O.1    Müller, S.2    Pfeiffer, M.3    Sniezko, I.4    Klein, A.5
  • 158
    • 0032053552 scopus 로고    scopus 로고
    • Thiol:Fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum: Identification of the catalytic sites for fumarate reduction and thiol oxidation
    • [158] Heim, S., Künkel, A., Thauer, R.K. and Hedderich, R. (1998) Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum: identification of the catalytic sites for fumarate reduction and thiol oxidation. Eur. J. Biochem. 253, 292-299.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 292-299
    • Heim, S.1    Künkel, A.2    Thauer, R.K.3    Hedderich, R.4
  • 159
    • 0029781334 scopus 로고    scopus 로고
    • The function and properties of the iron-sulfur center in spinach ferredoxin:Thioredoxin reductase: A new biological role for iron-sulfur clusters
    • [159] Staples, C.R., Ameyibor, E., Fu, W., Gardet-Salvi, L., Stritt-Etter, A.-L., Schürmann, P., Knaff, D.B. and Johnson, M.K. (1996) The function and properties of the iron-sulfur center in spinach ferredoxin:thioredoxin reductase: a new biological role for iron-sulfur clusters. Biochemistry 35, 11425-11434.
    • (1996) Biochemistry , vol.35 , pp. 11425-11434
    • Staples, C.R.1    Ameyibor, E.2    Fu, W.3    Gardet-Salvi, L.4    Stritt-Etter, A.-L.5    Schürmann, P.6    Knaff, D.B.7    Johnson, M.K.8
  • 161
    • 0028785378 scopus 로고
    • Flavoprotein structure and mechanism. 6. Mechanism and structure of thioredoxin reductase from Escherichia coli
    • [161] Williams, C.H. Jr. (1995) Flavoprotein structure and mechanism. 6. Mechanism and structure of thioredoxin reductase from Escherichia coli. FASEB J. 9, 1267-1276.
    • (1995) FASEB J. , vol.9 , pp. 1267-1276
    • Williams C.H., Jr.1
  • 162
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • [162] Kunst et al. (1997) The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst1
  • 163
    • 0013565892 scopus 로고    scopus 로고
    • EMBL accession number z97991
    • [163] Oliver, K. and Harris, D., EMBL accession number z97991.
    • Oliver, K.1    Harris, D.2
  • 165
    • 0031894326 scopus 로고    scopus 로고
    • Unusual organization of the genes coding for HydSL, the stable [NiFe] hydrogenase in the photosynthetic bacterium Thiocapsa roseopersicina BBS
    • [165] Rakhely, G., Colbeau, A., Garin, J., Vignais, P.M. and Kovacs, K.L. (1998) Unusual organization of the genes coding for HydSL, the stable [NiFe] hydrogenase in the photosynthetic bacterium Thiocapsa roseopersicina BBS. J. Bacteriol. 180, 1460-1465.
    • (1998) J. Bacteriol. , vol.180 , pp. 1460-1465
    • Rakhely, G.1    Colbeau, A.2    Garin, J.3    Vignais, P.M.4    Kovacs, K.L.5
  • 166
    • 1842332148 scopus 로고    scopus 로고
    • A succinate dehydrogenase with novel structure and properties from the hyperthermophilic archaeon Sulfolobus acidocaldarius: Genetic and biophysical characterization
    • [166] Janssen, S., Schäfer, G., Anemüller, S. and Moll, R. (1997) A succinate dehydrogenase with novel structure and properties from the hyperthermophilic archaeon Sulfolobus acidocaldarius: genetic and biophysical characterization. J. Bacteriol. 179, 5560-5569.
    • (1997) J. Bacteriol. , vol.179 , pp. 5560-5569
    • Janssen, S.1    Schäfer, G.2    Anemüller, S.3    Moll, R.4
  • 167
    • 0031812609 scopus 로고    scopus 로고
    • CyanoBase, a WWW database containing the complete nucleotide sequence of the genome of Synechocystis sp. strain PCC6803
    • [167] Nakamura, Y., Kaneko, T., Hirosawa, M., Miyajima, N. and Tabata, S. (1998) CyanoBase, a WWW database containing the complete nucleotide sequence of the genome of Synechocystis sp. strain PCC6803. Nucleic Acids Res. 26, 63-67.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 63-67
    • Nakamura, Y.1    Kaneko, T.2    Hirosawa, M.3    Miyajima, N.4    Tabata, S.5
  • 168
    • 0027323851 scopus 로고
    • The hme operon of Desulfovibrio vulgaris subspec. vulgaris Hildenborough encodes a potential transmembrane redox protein complex
    • [168] Rossi, M., Pollock, W.B.R., Reij, M.W., Keon, R.G., Fu, R. and Voordouw, G. (1993) The hme operon of Desulfovibrio vulgaris subspec. vulgaris Hildenborough encodes a potential transmembrane redox protein complex. J. Bacteriol. 175, 4699-4711.
    • (1993) J. Bacteriol. , vol.175 , pp. 4699-4711
    • Rossi, M.1    Pollock, W.B.R.2    Reij, M.W.3    Keon, R.G.4    Fu, R.5    Voordouw, G.6
  • 169
    • 0031855745 scopus 로고    scopus 로고
    • Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
    • [169] Poll, A.S. and Dahl, C. (1998) Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. Microbiology 144, 1881-1894.
    • (1998) Microbiology , vol.144 , pp. 1881-1894
    • Poll, A.S.1    Dahl, C.2
  • 170
    • 0024025050 scopus 로고
    • Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12
    • [170] Cole, ST., Eiglmeier, K., Ahemd, S., Honore, N., Elmers, L., Anderson, W.F. and Weiner, J.H. (1988) Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12. J. Bacteriol. 170, 2448-2456.
    • (1988) J. Bacteriol. , vol.170 , pp. 2448-2456
    • Cole, S.T.1    Eiglmeier, K.2    Ahemd, S.3    Honore, N.4    Elmers, L.5    Anderson, W.F.6    Weiner, J.H.7
  • 171
    • 0029670395 scopus 로고    scopus 로고
    • Glc Locus of Escherichia coli: Characterization of genes encoding the subunits of glycolate oxidase and glc regulator protein
    • [171] Pellicer, M., Badia, J., Aguilar, J. and Baldoma, L. (1996) glc Locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and glc regulator protein. J. Bacteriol. 178, 2051-2059.
    • (1996) J. Bacteriol. , vol.178 , pp. 2051-2059
    • Pellicer, M.1    Badia, J.2    Aguilar, J.3    Baldoma, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.