메뉴 건너뛰기




Volumn 6, Issue 3, 2000, Pages 187-196

Electron transfer in the dissimilatory iron-reducing bacterium Geobacter metallireducens

Author keywords

Anaerobic respiration; Cytochrome c; Fe(III) reduction; Geobacteraceae; NADH dehydrogenase

Indexed keywords

2 OXOGLUTARIC ACID; BENZOIC ACID; CYTOCHROME; IRON; ISOCITRATE DEHYDROGENASE; MALATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PARAQUAT; SUCCINATE DEHYDROGENASE;

EID: 0034212464     PISSN: 10759964     EISSN: None     Source Type: Journal    
DOI: 10.1006/anae.2000.0333     Document Type: Article
Times cited : (41)

References (54)
  • 2
    • 0025890073 scopus 로고
    • Dissimilatory Fe(III) and Mn(IV) reduction
    • Lovely D. R. Dissimilatory Fe(III) and Mn(IV) reduction. Microbiol Rev. 55:1991;259-287.
    • (1991) Microbiol Rev , vol.55 , pp. 259-287
    • Lovely, D.R.1
  • 3
    • 0030867481 scopus 로고    scopus 로고
    • Microbial Fe(III) reduction in subsurface environments
    • Lovely D. R. Microbial Fe(III) reduction in subsurface environments. FEMS Microbiol Lett. 20:1997;305-313.
    • (1997) FEMS Microbiol Lett , vol.20 , pp. 305-313
    • Lovely, D.R.1
  • 4
    • 70350402562 scopus 로고
    • The chemistry of submerged soils
    • Ponnamperuma F. N. The chemistry of submerged soils. Adv Agron. 24:1972;29-96.
    • (1972) Adv Agron , vol.24 , pp. 29-96
    • Ponnamperuma, F.N.1
  • 5
    • 0028132223 scopus 로고
    • Iron and manganese in anaerobic respiration: Environmental significance, physiology, and regulation
    • Nealson K. H., Saffarini D. Iron and manganese in anaerobic respiration: environmental significance, physiology, and regulation. Ann Rev Microbiol. 48:1994;311-343.
    • (1994) Ann Rev Microbiol , vol.48 , pp. 311-343
    • Nealson, K.H.1    Saffarini, D.2
  • 7
    • 0025363083 scopus 로고
    • Anaerobic oxidation of toluene, phenol, and p -cresol by the dissimilatory iron-reducing organism, GS-15
    • Lovley D. R., Lonergan D. J. Anaerobic oxidation of toluene, phenol, and p -cresol by the dissimilatory iron-reducing organism, GS-15. Appl Environ Microbiol. 56:1990;1858-1864.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1858-1864
    • Lovley, D.R.1    Lonergan, D.J.2
  • 9
    • 0027341088 scopus 로고
    • Dissimilatory Fe(III) reduction by the marine microorganism Desulfuromonas acetoxidans
    • Roden E. E., Lovley D. R. Dissimilatory Fe(III) reduction by the marine microorganism Desulfuromonas acetoxidans. Appl Environ Microbiol. 59:1993;734-742.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 734-742
    • Roden, E.E.1    Lovley, D.R.2
  • 11
    • 0032190289 scopus 로고    scopus 로고
    • Quinone moieties act as electron acceptors in the reduction of humic substances by humics-reducing microorganisms
    • Scott D. T., McKnight D. M., Blunt-Harris E. L., Kolesar S. E., Lovley D. R. Quinone moieties act as electron acceptors in the reduction of humic substances by humics-reducing microorganisms. Environ Sci Technol. 32:1998;2984-2989.
    • (1998) Environ Sci Technol , vol.32 , pp. 2984-2989
    • Scott, D.T.1    McKnight, D.M.2    Blunt-Harris, E.L.3    Kolesar, S.E.4    Lovley, D.R.5
  • 12
    • 0023498339 scopus 로고
    • Anaerobic production of magnetite by a dissimilatory iron-reducing microorganism
    • Lovley D. R., Stolz J. F., Nord G. L., Phillips E. J.P. Anaerobic production of magnetite by a dissimilatory iron-reducing microorganism. Nature. 330:1987;252-254.
    • (1987) Nature , vol.330 , pp. 252-254
    • Lovley, D.R.1    Stolz, J.F.2    Nord, G.L.3    Phillips, E.J.P.4
  • 13
    • 0025832543 scopus 로고
    • Acetate catabolism in the dissimilatory iron-reducing isolate GS-15
    • Champine J. E., Goodwin S. Acetate catabolism in the dissimilatory iron-reducing isolate GS-15. J Bacteriol. 173:1991;2704-2706.
    • (1991) J Bacteriol , vol.173 , pp. 2704-2706
    • Champine, J.E.1    Goodwin, S.2
  • 14
    • 0025777420 scopus 로고
    • Electron transport in the dissimilatory iron reducer, GS-15
    • Gorby Y. A., Lovley D. R. Electron transport in the dissimilatory iron reducer, GS-15. Appl Environ Microbiol. 57:1991;867-870.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 867-870
    • Gorby, Y.A.1    Lovley, D.R.2
  • 15
    • 0027523571 scopus 로고
    • Geobacter metallireducens gen nov. sp. nov., a microorganism capable of coupling the complete oxidation of organic compounds to the reduction of iron and other minerals
    • Lovley D. R., Giovannoni S. J., White D. C., Champine J. E., Phillips E. J.P., Gorby Y. A., Goodwin S. Geobacter metallireducens gen nov. sp. nov., a microorganism capable of coupling the complete oxidation of organic compounds to the reduction of iron and other minerals. Arch Microbiol. 159:1993;336-344.
    • (1993) Arch Microbiol , vol.159 , pp. 336-344
    • Lovley, D.R.1    Giovannoni, S.J.2    White, D.C.3    Champine, J.E.4    Phillips, E.J.P.5    Gorby, Y.A.6    Goodwin, S.7
  • 16
    • 0032796162 scopus 로고    scopus 로고
    • 7from the metal-reducing bacterium, Geobacter metallireducens
    • 7from the metal-reducing bacterium, Geobacter metallireducens. FEMS Microbiol Lett. 175:1999;205-210.
    • (1999) FEMS Microbiol Lett , vol.175 , pp. 205-210
    • Afkar, E.1    Fukumori, Y.2
  • 17
    • 0032448328 scopus 로고    scopus 로고
    • A periplasmic and extracellular c -type cytochrome of Geobacter sulfurreducens acts as a ferric iron reductase and as electron carrier to other acceptors or to partner bacteria
    • Seeliger S., Cord-Ruwisch R., Schink B. A periplasmic and extracellular c -type cytochrome of Geobacter sulfurreducens acts as a ferric iron reductase and as electron carrier to other acceptors or to partner bacteria. J Bacteriol. 180:1998;3686-3691.
    • (1998) J Bacteriol , vol.180 , pp. 3686-3691
    • Seeliger, S.1    Cord-Ruwisch, R.2    Schink, B.3
  • 18
    • 0031664567 scopus 로고    scopus 로고
    • Localization and solubilization of the iron(III) reductase of Geobacter sulfurreducens
    • Gaspard S., Vazquez F., Holliger C. Localization and solubilization of the iron(III) reductase of Geobacter sulfurreducens. Appl Environ Microbiol. 64:1998;3188-3194.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3188-3194
    • Gaspard, S.1    Vazquez, F.2    Holliger, C.3
  • 20
    • 0019435502 scopus 로고
    • Influence of corrinoid antagonists on methanogen metabolism
    • Kenealy W., Zeikus J. G. Influence of corrinoid antagonists on methanogen metabolism. J Bacteriol. 146:1981;133-140.
    • (1981) J Bacteriol , vol.146 , pp. 133-140
    • Kenealy, W.1    Zeikus, J.G.2
  • 21
    • 0025252193 scopus 로고
    • Solubilization of native membrane proteins
    • Hjelmeland L. M. Solubilization of native membrane proteins. Meth Enzymol. 182:1990;253-264.
    • (1990) Meth Enzymol , vol.182 , pp. 253-264
    • Hjelmeland, L.M.1
  • 23
    • 0023430823 scopus 로고
    • Membrane topography of anaerobic carbon monoxide oxidation in Rhodocyclus gelatinosus
    • Champine J. E., Uffen R. L. Membrane topography of anaerobic carbon monoxide oxidation in Rhodocyclus gelatinosus. J Bacteriol. 169:1987;4784-4789.
    • (1987) J Bacteriol , vol.169 , pp. 4784-4789
    • Champine, J.E.1    Uffen, R.L.2
  • 24
    • 0019414485 scopus 로고
    • Procedures and conditions for application of the pyridine hemochrome method to photosynthetically grown cells ofRhodopseudomonas sphaeroides
    • Takaichi S., Morita S. Procedures and conditions for application of the pyridine hemochrome method to photosynthetically grown cells ofRhodopseudomonas sphaeroides. J Biochim. 89:1981;1513-1519.
    • (1981) J Biochim , vol.89 , pp. 1513-1519
    • Takaichi, S.1    Morita, S.2
  • 25
    • 0000737547 scopus 로고
    • Preparation and properties of three pure crystalline bacterial haem proteins
    • Horio T., Kamen M. D. Preparation and properties of three pure crystalline bacterial haem proteins. Biochim Biophys Acta. 48:1961;266-286.
    • (1961) Biochim Biophys Acta , vol.48 , pp. 266-286
    • Horio, T.1    Kamen, M.D.2
  • 26
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of mid-point potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton P. L. Redox potentiometry: determination of mid-point potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54:1978;411-435.
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 27
    • 0000347821 scopus 로고
    • Determination of membrane protein concentration
    • J. C. Venter, Harrison L. C. New York: Alan R. Liss, Inc.
    • Clark S. Determination of membrane protein concentration. Venter J. C., Harrison L. C. Receptor purification procedures. 1984;149-161 Alan R. Liss, Inc. New York.
    • (1984) Receptor Purification Procedures , pp. 149-161
    • Clark, S.1
  • 29
    • 46149130370 scopus 로고
    • Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes
    • Goodhew C. F., Brown K. R., Pettigrew G. W. Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes. Biochem Biophys Acta. 852:1986;288-294.
    • (1986) Biochem Biophys Acta , vol.852 , pp. 288-294
    • Goodhew, C.F.1    Brown, K.R.2    Pettigrew, G.W.3
  • 30
  • 31
    • 0030868337 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of two new cytochromes isolated from Desulfuromonas acetoxidans
    • Bruschi M., Woudstra M., Guigliarelli B., Asso M., Lojou E., Petillot Y., Abergel C. Biochemical and spectroscopic characterization of two new cytochromes isolated from Desulfuromonas acetoxidans. Biochem. 36:1997;10601-10608.
    • (1997) Biochem , vol.36 , pp. 10601-10608
    • Bruschi, M.1    Woudstra, M.2    Guigliarelli, B.3    Asso, M.4    Lojou, E.5    Petillot, Y.6    Abergel, C.7
  • 32
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 157:1982;105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 33
    • 0023744739 scopus 로고
    • Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki
    • Ogata M. S., Kondo, Okawara N., Yagi T. Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki. J Biochem. 103:1988;121-125.
    • (1988) J Biochem , vol.103 , pp. 121-125
    • Ogata, M.S.1    Kondo2    Okawara, N.3    Yagi, T.4
  • 35
    • 0001614967 scopus 로고
    • The dissimilatory sulfate- and sulfur-reducing bacteria
    • A. Balows, H. G. Truper, M. Dworkin, W. Harder, Schleifer K. New York: Springer-Verlag
    • Widdel F., Hansen T. A. The dissimilatory sulfate- and sulfur-reducing bacteria. Balows A., Truper H. G., Dworkin M., Harder W., Schleifer K. The Prokaryotes. 1992;583-624 Springer-Verlag, New York.
    • (1992) The Prokaryotes , pp. 583-624
    • Widdel, F.1    Hansen, T.A.2
  • 36
    • 0020463708 scopus 로고
    • Thermoacidophilic archaebacteria contain bacterial-type ferredoxins acting as electron acceptors of 2-oxoacid:ferredoxin oxidoreductases
    • Kerscher L., Nowitzki S., Oesterhelt D. Thermoacidophilic archaebacteria contain bacterial-type ferredoxins acting as electron acceptors of 2-oxoacid:ferredoxin oxidoreductases. Eur J Biochem. 128:1982;223-230.
    • (1982) Eur J Biochem , vol.128 , pp. 223-230
    • Kerscher, L.1    Nowitzki, S.2    Oesterhelt, D.3
  • 37
    • 0014497163 scopus 로고
    • Citrate and glyoxylate cycle in the halophile, Halobacterium salinarium
    • Aitken D. M., Brown A. D. Citrate and glyoxylate cycle in the halophile, Halobacterium salinarium. Biochim Biophys Acta. 177:1969;351-354.
    • (1969) Biochim Biophys Acta , vol.177 , pp. 351-354
    • Aitken, D.M.1    Brown, A.D.2
  • 38
    • 0024387798 scopus 로고
    • Purification and characterization of the pyruvate-ferredoxin oxidoreductase from Clostridium acetobutylicum
    • Meinecke B., Bertram J., Gottschalk G. Purification and characterization of the pyruvate-ferredoxin oxidoreductase from Clostridium acetobutylicum. Arch Microbiol. 152:1989;244-250.
    • (1989) Arch Microbiol , vol.152 , pp. 244-250
    • Meinecke, B.1    Bertram, J.2    Gottschalk, G.3
  • 40
    • 0024418766 scopus 로고
    • Biochemistry of acetate catabolism in anaerobic chemotrophic bacteria
    • Thauer R. K., Moeller-Zinkhan D., Spormann A. M. Biochemistry of acetate catabolism in anaerobic chemotrophic bacteria. Annu Rev Microbiol. 43:1989;43-67.
    • (1989) Annu Rev Microbiol , vol.43 , pp. 43-67
    • Thauer, R.K.1    Moeller-Zinkhan, D.2    Spormann, A.M.3
  • 42
    • 0002226697 scopus 로고
    • Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase
    • Kremer D. R., Nienhuis-Kuiper H. E., Timmer C. J., Hansen T. A. Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase. Arch Microbiol. 151:1989;34-39.
    • (1989) Arch Microbiol , vol.151 , pp. 34-39
    • Kremer, D.R.1    Nienhuis-Kuiper, H.E.2    Timmer, C.J.3    Hansen, T.A.4
  • 43
    • 0023726308 scopus 로고
    • Citric-acid cycle, 50 years on. Modifications and an alternative pathway in anaerobic bacteria
    • Thauer R. Citric-acid cycle, 50 years on. Modifications and an alternative pathway in anaerobic bacteria. Eur J Biochem. 176:1988;497-508.
    • (1988) Eur J Biochem , vol.176 , pp. 497-508
    • Thauer, R.1
  • 45
    • 0028050079 scopus 로고
    • Geobacter sulfurreducens sp. nov., a hydrogen- and acetate-oxidizing dissimilatory metal-reducing microorganism
    • Caccavo J. R., Lonergan D. J., Lovley D. L., Davis M., Stolz J. F., McInerny M. Geobacter sulfurreducens sp. nov., a hydrogen- and acetate-oxidizing dissimilatory metal-reducing microorganism. Appl Environ Microbiol. 60:1994;3752-3759.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3752-3759
    • Caccavo, J.R.1    Lonergan, D.J.2    Lovley, D.L.3    Davis, M.4    Stolz, J.F.5    McInerny, M.6
  • 46
    • 0029583199 scopus 로고
    • Desulfuromonas palmitatis sp. nov., a marine dissimilatory Fe (III) reducer that can oxidize long-chain fatty acids
    • Coates J. D., Lonergan D. J., Phillips E. J.P., Jenter H. L., Lovley D. R. Desulfuromonas palmitatis sp. nov., a marine dissimilatory Fe (III) reducer that can oxidize long-chain fatty acids. Arch Microbiol. 164:1995;406-413.
    • (1995) Arch Microbiol , vol.164 , pp. 406-413
    • Coates, J.D.1    Lonergan, D.J.2    Phillips, E.J.P.3    Jenter, H.L.4    Lovley, D.R.5
  • 47
    • 0027531127 scopus 로고
    • Evidence for a novel nitrate reductase in the dissimilatory iron-reducing bacterium Geobacter metallireducens
    • Naik R. R., Murillo F. M., Stolz J. F. Evidence for a novel nitrate reductase in the dissimilatory iron-reducing bacterium Geobacter metallireducens. FEMS Microbiol Lett. 106:1993;53-58.
    • (1993) FEMS Microbiol Lett , vol.106 , pp. 53-58
    • Naik, R.R.1    Murillo, F.M.2    Stolz, J.F.3
  • 51
    • 0018305317 scopus 로고
    • The redox properties and heme environment of cytochrome c -551.5 from Desulfuromonas acetoxidans
    • Feichtner M. D., Kassner R. J. The redox properties and heme environment of cytochrome c -551.5 from Desulfuromonas acetoxidans. Biochim Biophys Acta. 579:1979;269-278.
    • (1979) Biochim Biophys Acta , vol.579 , pp. 269-278
    • Feichtner, M.D.1    Kassner, R.J.2
  • 53
    • 0023134480 scopus 로고
    • Amino-terminal amino acid sequences of electron transfer proteins from Gram-negative bacteria as indicators of their cellular localization: The sulfate-reducing bacteria
    • LeGall J., Peck H. D. Jr. Amino-terminal amino acid sequences of electron transfer proteins from Gram-negative bacteria as indicators of their cellular localization: the sulfate-reducing bacteria. FEMS Microbio Rev. 46:1987;122-126.
    • (1987) FEMS Microbio Rev , vol.46 , pp. 122-126
    • LeGall, J.1    Peck H.D., Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.