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Volumn , Issue , 2007, Pages 215-240

Biochemical, genetic and genomic characterization of anaerobic electron transport pathways in sulphate-reducing Delta proteobacteria

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EID: 84928633096     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1017/CBO9780511541490.008     Document Type: Chapter
Times cited : (40)

References (76)
  • 1
    • 0033988688 scopus 로고    scopus 로고
    • A sequential electron transfer from hydrogenases to cytochromes in sulphate-reducing bacteria
    • Aubert, C., Brugna, M., Dolla, A., Bruschi, M. and Giudici-Orticoni, M. T. (2000). A sequential electron transfer from hydrogenases to cytochromes in sulphate-reducing bacteria. Biochim Biophys Acta, 1476, 85—92.
    • (2000) Biochim Biophys Acta , vol.1476 , pp. 85-92
    • Aubert, C.1    Brugna, M.2    Dolla, A.3    Bruschi, M.4    Giudici-Orticoni, M.T.5
  • 2
    • 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
    • Berks, B.C., Page, M. D., Richardson, D. J. et al. (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    Page, M.D.2    Richardson, D.J.3
  • 3
    • 0028671818 scopus 로고
    • Cytochrome c3 (Mr 26,000) isolated from sulphate-reducing bacteria and its relationship to other polyhemic cytochromes from
    • Bruschi, M. (1994). Cytochrome c3 (Mr 26,000) isolated from sulphate-reducing bacteria and its relationship to other polyhemic cytochromes from Desulfovibrio. Methods Enzym, 243, 140—155.
    • (1994) Desulfovibrio. Methods Enzym , vol.243 , pp. 140-155
    • Bruschi, M.1
  • 4
    • 0031971063 scopus 로고    scopus 로고
    • Molecular study and partial characterization of iron-only hydrogenase in desulfovibrio fructosovorans
    • Casalot, L., Hatchikian, C. E., Forget, N. et al. (1998). Molecular study and partial characterization of iron-only hydrogenase in Desulfovibrio fructosovorans. Anaerobe, 4, 45—55.
    • (1998) Anaerobe , vol.4 , pp. 45-55
    • Casalot, L.1    Hatchikian, C.E.2    Forget, N.3
  • 5
    • 0036181001 scopus 로고    scopus 로고
    • Evidence for a fourth hydrogenase in desulfovibrio fructosovorans
    • Casalot, L., De Luca, G., Dermoun, Z., Rousset, M. and De Philip, P. (2002). Evidence for a fourth hydrogenase in Desulfovibrio fructosovorans. J Bacteriol, 184, 853—856.
    • (2002) J Bacteriol , vol.184 , pp. 853-856
    • Casalot, L.1    De Luca, G.2    Dermoun, Z.3    Rousset, M.4    De Philip, P.5
  • 7
    • 0035162654 scopus 로고    scopus 로고
    • Solution structure of pyrobaculum aerophilum dsrc, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase
    • Cort, J. R., Mariappan, S. V. S., Kim, C.-Y. et al. (2001). Solution structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase. Eur J Biochem, 268, 55842—55850.
    • (2001) Eur J Biochem , vol.268 , pp. 55842-55850
    • Cort, J.R.1    Mariappan, S.2    Kim, C.-Y.3
  • 9
    • 0030584677 scopus 로고    scopus 로고
    • Crystal structure of a dimeric octaheme cytochrome c3 (M(r) 26,000) from desulfovibrio desulfuricans norway
    • Czjzek, M., Guerlesquin, F., Bruschi, M. and Haser, R. (1996). Crystal structure of a dimeric octaheme cytochrome c3 (M(r) 26,000) from Desulfovibrio desulfuricans Norway. Structure, 4, 395—404.
    • (1996) Structure , vol.4 , pp. 395-404
    • Czjzek, M.1    Guerlesquin, F.2    Bruschi, M.3    Haser, R.4
  • 10
    • 0036905068 scopus 로고    scopus 로고
    • The crystal structure of the hexadeca-heme cytochrome hmc and a structural model of its complex with cytochrome c3
    • Czjzek, M., Elantak, L., Zamboni, V. et al. (2002). The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c3. Structure, 10, 1677—1686.
    • (2002) Structure , vol.10 , pp. 1677-1686
    • Czjzek, M.1    Elantak, L.2    Zamboni, V.3
  • 11
    • 14544272337 scopus 로고    scopus 로고
    • Novel genes of the dsr gene cluster and evidence for close interaction of dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium allochromatium vinosum
    • Dahl, C., Engels, S., Pott-Sperling, A. S. et al. (2005). Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum. J Bacteriol, 187, 1392—1404.
    • (2005) J Bacteriol , vol.187 , pp. 1392-1404
    • Dahl, C.1    Engels, S.2    Pott-Sperling, A.S.3
  • 12
    • 23744513697 scopus 로고    scopus 로고
    • Native and mutant nickel-iron hydrogenases: Unravelling structure and function
    • De Lacey, A. L., Fernandez, V. M. and Rousset, M. (2005). Native and mutant nickel-iron hydrogenases: unravelling structure and function. Coordin Chem Rev, 249, 1596—1608.
    • (2005) Coordin Chem Rev , vol.249 , pp. 1596-1608
    • De Lacey, A.L.1    Fernandez, V.M.2    Rousset, M.3
  • 13
    • 0032562238 scopus 로고    scopus 로고
    • Purification and characterization of the hnda subunit of nadp-reducing hydrogenase from desulfovibrio fructosovorans overproduced in escherichia coli
    • De Luca, G., Asso, M., Belaich, J. P. and Dermoun, Z. (1998). Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli. Biochemistry, 37, 2660—2665.
    • (1998) Biochemistry , vol.37 , pp. 2660-2665
    • De Luca, G.1    Asso, M.2    Belaich, J.P.3    Dermoun, Z.4
  • 14
    • 32544458823 scopus 로고    scopus 로고
    • Resonance raman fingerprinting of multiheme cytochromes from the cytochrome c3 family
    • Di Paolo, R. E., Pereira, P. M., Gomes, I. et al. (2006). Resonance Raman fingerprinting of multiheme cytochromes from the cytochrome c3 family. J Biol Inorg Chem, 11, 217—224
    • (2006) J Biol Inorg Chem , vol.11 , pp. 217-224
    • Di Paolo, R.E.1    Pereira, P.M.2    Gomes, I.3
  • 15
    • 0033851906 scopus 로고    scopus 로고
    • Deletion of the hmc operon of desulfovibrio vulgaris subsp. Vulgaris hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment
    • Dolla, A., Pohorelic, B. K. J., Voordouw, J. K. and Voordouw, G. (2000). Deletion of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment. Arch Microbiol, 174, 143—151.
    • (2000) Arch Microbiol , vol.174 , pp. 143-151
    • Dolla, A.1    Pohorelic, B.2    Voordouw, J.K.3    Voordouw, G.4
  • 16
    • 0037070204 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanothermobacter marburgensis contains an active-site 4fe-4s cluster that is directly involved in mediating heterodisulfide reduction
    • Duin, E. C., Madadi-Kahkesh, S., Hedderich, R., Clay, M. D. and Johnson, M. K. (2002). Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site 4Fe-4S cluster that is directly involved in mediating heterodisulfide reduction. FEBS Lett, 512, 263—268.
    • (2002) FEBS Lett , vol.512 , pp. 263-268
    • Duin, E.C.1    Madadi-Kahkesh, S.2    Hedderich, R.3    Clay, M.D.4    Johnson, M.K.5
  • 17
    • 27744601231 scopus 로고    scopus 로고
    • Role of the tetrahemic subunit in desulfovibrio vulgaris hildenborough formate dehydrogenase
    • Elantak, L., Dolla, A., Durand, M. C., Bianco, P. and Guerlesquin, F. (2005). Role of the tetrahemic subunit in Desulfovibrio vulgaris Hildenborough formate dehydrogenase. Biochemistry, 44, 14828—14834.
    • (2005) Biochemistry , vol.44 , pp. 14828-14834
    • Elantak, L.1    Dolla, A.2    Durand, M.C.3    Bianco, P.4    Guerlesquin, F.5
  • 18
    • 0032963901 scopus 로고    scopus 로고
    • Ab initio
    • structure solution of a dimeric cytochrome c3 from Desulfovibrio gigas containing disulfide bridges
    • Frazao, C., Sieker, L., Sheldrick, G. et al. (1999). Ab initio structure solution of a dimeric cytochrome c3 from Desulfovibrio gigas containing disulfide bridges. J Biol Inorg Chem, 4, 162—165.
    • (1999) J Biol Inorg Chem , vol.4 , pp. 162-165
    • Frazao, C.1    Sieker, L.2    Sheldrick, G.3
  • 19
    • 14644416571 scopus 로고    scopus 로고
    • Construction of a nife-hydrogenase deletion mutant of desulfovibrio vulgaris hildenborough
    • Goenka, A., Voordouw, J. K., Lubitz, W., Gartner, W. and Voordouw, G. (2005). Construction of a NiFe-hydrogenase deletion mutant of Desulfovibrio vulgaris Hildenborough. Biochem Soc Trans, 33, 59—60.
    • (2005) Biochem Soc Trans , vol.33 , pp. 59-60
    • Goenka, A.1    Voordouw, J.K.2    Lubitz, W.3    Gartner, W.4    Voordouw, G.5
  • 20
    • 0037964766 scopus 로고    scopus 로고
    • Nitrite reductase activity of sulphate-reducing bacteria prevents their inhibition by nitrate-reducing, sulfide-oxidising bacteria
    • Greene, E. A., Hubert, C., Nemati, M., Jenneman, G. E. and Voordouw, G. (2003). Nitrite reductase activity of sulphate-reducing bacteria prevents their inhibition by nitrate-reducing, sulfide-oxidising bacteria. Environ Microbiol, 5, 607—617.
    • (2003) Environ Microbiol , vol.5 , pp. 607-617
    • Greene, E.A.1    Hubert, C.2    Nemati, M.3    Jenneman, G.E.4    Voordouw, G.5
  • 22
    • 0038782226 scopus 로고    scopus 로고
    • Gene expression analysis of energy metabolism mutants of desulfovibrio vulgaris hildenborough indicates an important role for alcohol dehydrogenase
    • Haveman, S. A., Brunelle, V., Voordouw, J. K. et al. (2003). Gene expression analysis of energy metabolism mutants of Desulfovibrio vulgaris Hildenborough indicates an important role for alcohol dehydrogenase. J Bacteriol, 195, 4345—4353.
    • (2003) J Bacteriol , vol.195 , pp. 4345-4353
    • Haveman, S.A.1    Brunelle, V.2    Voordouw, J.K.3
  • 23
    • 9244240775 scopus 로고    scopus 로고
    • Physiological and gene expression analysis of inhibition of desulfovibrio vulgaris hildenborough by nitrite
    • Haveman, S. A., Greene, E. A., Stilwell, C. P., Voordouw, J. K. and Voordouw, G. (2004). Physiological and gene expression analysis of inhibition of Desulfovibrio vulgaris Hildenborough by nitrite. J Bacteriol, 186, 7944—7950.
    • (2004) J Bacteriol , vol.186 , pp. 7944-7950
    • Haveman, S.A.1    Greene, E.A.2    Stilwell, C.P.3    Voordouw, J.K.4    Voordouw, G.5
  • 24
    • 23944460534 scopus 로고    scopus 로고
    • Gene expression analysis of theg mechanism of inhibition of desulfovibrio vulgaris hildenborough by nitrate-reducing, sulfide-oxidizing bacteria
    • Haveman, S. A., Greene, E.A. and Voordouw, G. (2005). Gene expression analysis of theg mechanism of inhibition of Desulfovibrio vulgaris Hildenborough by nitrate-reducing, sulfide-oxidizing bacteria. Environ Microbiol, 7, 1461—1465.
    • (2005) Environ Microbiol , vol.7 , pp. 1461-1465
    • Haveman, S.A.1    Greene, E.A.2    Voordouw, G.3
  • 25
    • 33745152320 scopus 로고    scopus 로고
    • Energetic consequences of nitrite stress in desulfovibrio vulgaris hildenborough, inferred from global transcriptional analysis
    • He, Q., Huang, K. H., He, Z. et al., (2006). Energetic Consequences of Nitrite Stress in Desulfovibrio vulgaris Hildenborough, Inferred from Global Transcriptional Analysis. Appl Environ Microbiol, 72, 4370—4381.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4370-4381
    • He, Q.1    Huang, K.H.2    He, Z.3
  • 26
    • 2342475768 scopus 로고    scopus 로고
    • The genome sequence of the anaerobic, sulphate-reducing bacterium desulfovibrio vulgaris hildenborough
    • Heidelberg, J. F., Seshadri, R., Haveman, S. A. et al. (2004). The genome sequence of the anaerobic, sulphate-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
  • 27
    • 0009790182 scopus 로고
    • Desulfovibrio vulgaris
    • hydrogenase — a nonheme iron enzyme lacking nickel that exhibits anomalous electron-paramagnetic-res and Mossbauer-spectra
    • Huynh, B. H., Czechowski, M. H., Kruger, H. J. et al. (1984). Desulfovibrio vulgaris hydrogenase — a nonheme iron enzyme lacking nickel that exhibits anomalous electron-paramagnetic-res and Mossbauer-spectra. Proc Natl Acad Sci-Biol, 81, 3728—3732.
    • (1984) Proc Natl Acad Sci-Biol , vol.81 , pp. 3728-3732
    • Huynh, B.H.1    Czechowski, M.H.2    Kruger, H.J.3
  • 28
    • 0242497560 scopus 로고    scopus 로고
    • New York: Wiley
    • Iverson, T. M., Hendrich, M. P., Arciero, D. M., Hooper, A. B. and Rees, D. C. (2001). Cytochrome cS54. In A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt (eds.), New York: Wiley. 136—146.
    • (2001) , pp. 136-146
    • Iverson, T.M.1    Hendrich, M.P.2    Arciero, D.M.3    Hooper, A.B.4    Rees, D.C.5
  • 29
    • 0033962472 scopus 로고    scopus 로고
    • Enhanced nitrogenase activity in strains of rhodobacter capsulatus that overexpress the rnf genes
    • Jeong, H. S. and Jouanneau, Y. (2000). Enhanced nitrogenase activity in strains of Rhodobacter capsulatus that overexpress the rnf genes. J Bacteriol, 182, 1208—1214.
    • (2000) J Bacteriol , vol.182 , pp. 1208-1214
    • Jeong, H.S.1    Jouanneau, Y.2
  • 30
    • 0030220251 scopus 로고    scopus 로고
    • Identification of the hmcf and topology of the hmcb subunit of the hmc complex of
    • Keon, R. G. and Voordouw, G. (1996). Identification of the HmcF and topology of the HmcB subunit of the Hmc complex of Desulfovibrio vulgaris. Anaerobe, 2, 231.
    • (1996) Desulfovibrio Vulgaris. Anaerobe , vol.2
    • Keon, R.G.1    Voordouw, G.2
  • 31
    • 0030986002 scopus 로고    scopus 로고
    • Deletion of two downstream genes alters expression of the hmc operon of desulfovibrio vulgaris subsp. Vulgaris hildenborough
    • Keon, R. G., Fu, R. and Voordouw, G. (1997). Deletion of two downstream genes alters expression of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough. Arch Microbiol, 167, 376—383.
    • (1997) Arch Microbiol , vol.167 , pp. 376-383
    • Keon, R.G.1    Fu, R.2    Voordouw, G.3
  • 32
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon
    • Klenk, H. P., Clayton, R. A., Tomb, J. F. et al. (1997). The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature, 390, 364—370.
    • (1997) Archaeoglobus Fulgidus. Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3
  • 33
    • 0038540118 scopus 로고    scopus 로고
    • A reducing system of the superoxide sensor soxr in
    • Koo, M. S., Lee, J. H., Rah, S. Y. et al. (2003). A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J, 22, 2614—2622.
    • (2003) Escherichia Coli. EMBO J , vol.22 , pp. 2614-2622
    • Koo, M.S.1    Lee, J.H.2    Rah, S.Y.3
  • 34
    • 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 energy-coupling 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 energy-coupling NADH oxidoreductases. Biochemistry, 36, 5509—5521.
    • (1997) Biochemistry , vol.36 , pp. 5509-5521
    • Kumagai, H.1    Fujiwara, T.2    Matsubara, H.3    Saeki, K.4
  • 35
    • 0031055712 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanol-grown cells of methanosarcina barkeri is not a flavoenzyme
    • Kunkel, 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
    • Kunkel, A.1    Vaupel, M.2    Heim, S.3    Thauer, R.K.4    Hedderich, R.5
  • 36
    • 0034858150 scopus 로고    scopus 로고
    • A paramagnetic species with unique epr characteristics in the active site of heterodisulfide reductase from methanogenic archaea
    • Madadi-Kahkesh, S., Duin, E. C., Heim, S. et al. (2001). A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. Eur J Biochem, 268, 2566—2577.
    • (2001) Eur J Biochem , vol.268 , pp. 2566-2577
    • Madadi-Kahkesh, S.1    Duin, E.C.2    Heim, S.3
  • 37
    • 0031039226 scopus 로고    scopus 로고
    • Physiological characteristics and growth behavior of single and double hydrogenase mutants of
    • Malki, S., Deluca, G., Fardeau, M. L. et al. (1997). Physiological characteristics and growth behavior of single and double hydrogenase mutants of Desulfovibrio fructosovorans. Arch Microbiol, 167, 38—45.
    • (1997) Desulfovibrio Fructosovorans. Arch Microbiol , vol.167 , pp. 38-45
    • Malki, S.1    Deluca, G.2    Fardeau, M.L.3
  • 38
    • 85047695985 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound enzyme complex from the sulphate-reducing archaeon archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea
    • Mander, G. J., Duin, E. C., Linder, D., Stetter, K. O. and Hedderich, R. (2002). Purification and characterization of a membrane-bound enzyme complex from the sulphate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea. Eur J Biochem, 269, 1895—1904.
    • (2002) Eur J Biochem , vol.269 , pp. 1895-1904
    • Mander, G.J.1    Duin, E.C.2    Linder, D.3    Stetter, K.O.4    Hedderich, R.5
  • 39
    • 0033081499 scopus 로고    scopus 로고
    • The primary and three-dimensional structures of a nine-haem cytochrome c from desulfovibrio desulfuricans atcc 27774 reveal a new member of the hmc family
    • Matias, P. M., Coelho, R., Pereira, I. A. et al. (1999). The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family. Structure, 7, 119—130.
    • (1999) Structure , vol.7 , pp. 119-130
    • Matias, P.M.1    Coelho, R.2    Pereira, I.A.3
  • 40
    • 0032836538 scopus 로고    scopus 로고
    • Nine-haem cytochrome c from desulfovibrio desulfuricans atcc 27774: Primary sequence determination, crystallographic refinement at 1.8 and modelling studies of its interaction with the tetrahaem cytochrome c3
    • Matias, P. M., Saraiva, L. M., Soares, C. M. et al. (1999b). Nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774: primary sequence determination, crystallographic refinement at 1.8 and modelling studies of its interaction with the tetrahaem cytochrome c3. J Biol Inorg Chem, 4, 478—494.
    • (1999) J Biol Inorg Chem , vol.4 , pp. 478-494
    • Matias, P.M.1    Saraiva, L.M.2    Soares, C.M.3
  • 41
    • 0037033048 scopus 로고    scopus 로고
    • Sulphate respiration in desulfovibrio vulgaris hildenborough: Structure of the 16-heme cytochrome c hmca at 2.5a resolution and a view of its role in transmembrane electron transfer
    • Matias, P. M., Coelho, A. V., Valente, F. M. A. et al. (2002). Sulphate respiration in Desulfovibrio vulgaris Hildenborough: structure of the 16-heme cytochrome c HmcA at 2.5A resolution and a view of its role in transmembrane electron transfer. J Biol Chem, 277, 47907—47916.
    • (2002) J Biol Chem , vol.277 , pp. 47907-47916
    • Matias, P.M.1    Coelho, A.V.2    Valente, F.3
  • 42
    • 20444385906 scopus 로고    scopus 로고
    • Sulphate respiration from hydrogen in desulfovibrio bacteria: A structural biology overview
    • Matias, P. M., Pereira, I. A., Soares, C. M. and Carrondo, M. A. (2005). Sulphate respiration from hydrogen in Desulfovibrio bacteria: a structural biology overview. Prog Biophys Mol Biol, 89, 292—329.
    • (2005) Prog Biophys Mol Biol , vol.89 , pp. 292-329
    • Matias, P.M.1    Pereira, I.A.2    Soares, C.M.3    Carrondo, M.A.4
  • 43
    • 0028308306 scopus 로고
    • Cloning, sequencing, and mutational analysis of the hyb operon encoding escherichia coli hydrogenase 2
    • Menon, N. K., Chatelus, C. Y., Dervartanian, M. et al. (1994). Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2. J Bacteriol, 176, 4416—4423.
    • (1994) J Bacteriol , vol.176 , pp. 4416-4423
    • Menon, N.K.1    Chatelus, C.Y.2    Dervartanian, M.3
  • 44
    • 0042835773 scopus 로고    scopus 로고
    • Crystal structure of dissimilatory sulfite reductase d (Dsrd) protein — possible interaction with b- and z-dna by its winged helix motif
    • Mizuno, N., Voordouw, G., Miki, K., Sarai, A. and Higuchi, Y. (2003). Crystal structure of dissimilatory sulfite reductase D (DsrD) protein — possible interaction with B- and Z-DNA by its winged helix motif. Structure, 11, 1133—1140.
    • (2003) Structure , vol.11 , pp. 1133-1140
    • Mizuno, N.1    Voordouw, G.2    Miki, K.3    Sarai, A.4    Higuchi, Y.5
  • 46
    • 0019802315 scopus 로고
    • Hydrogen cycling as a general mechanism for energy coupling in the sulphate-reducing bacteria, desulfovibrio sp
    • Odom, J. M. and Peck Jr., H. D. (1981). Hydrogen cycling as a general mechanism for energy coupling in the sulphate-reducing bacteria, Desulfovibrio sp. FEMS Microbiol Lett, 12, 47—50.
    • (1981) FEMS Microbiol Lett , vol.12 , pp. 47-50
    • Odom, J.M.1    Peck, H.D.2
  • 47
    • 0034739244 scopus 로고    scopus 로고
    • Characterization of a heme c nitrite reductase from a non-ammonifying microorganism, desulfovibrio vulgaris hildenborough
    • Pereira, I. A. C., Romao, C.V., Xavier, A. V., Legall, J. andTeixeira, M. (2000). Characterization of a heme c nitrite reductase from a non-ammonifying microorganism, Desulfovibrio vulgaris Hildenborough. Biochim Biophys Acta, 1481, 119—130.
    • (2000) Biochim Biophys Acta , vol.1481 , pp. 119-130
    • Pereira, I.1    Romao, C.V.2    Xavier, A.V.3    Legall, J.A.4    Teixeira, M.5
  • 48
    • 30344468701 scopus 로고    scopus 로고
    • Multi-heme c cytochromes and enzymes
    • R. B. King, John Wiley & Sons
    • Pereira, I. A. C. and Xavier, A. V. (2005). Multi-Heme c cytochromes and enzymes. In R. B. King (ed.), Encyclopedia of inorganic chemistry, 2nd edn. John Wiley & Sons.
    • (2005) Encyclopedia of Inorganic Chemistry
    • Pereira, I.1    Xavier, A.V.2
  • 49
    • 33748680507 scopus 로고    scopus 로고
    • The tmc complex from desulfovibrio vulgaris hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation
    • Pereira, P. M., Teixeira, M., Xavier, A. V. et al., (2006). The Tmc complex from Desulfovibrio vulgaris Hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation. Biochemistry, 45, 10359—10367.
    • (2006) Biochemistry , vol.45 , pp. 10359-10367
    • Pereira, P.M.1    Teixeira, M.2    Xavier, A.V.3
  • 50
    • 0026524433 scopus 로고
    • The third subunit of desulfoviridin-type dissimilatory sulfite reductases
    • Pierik, A. J., Duyvis, M. G., van Helvoort, J. M. L. M., Wolbert, R. B. G. and Hagen, W. R. (1992). The third subunit of desulfoviridin-type dissimilatory sulfite reductases. Eur J Biochem, 205, 111 — 115.
    • (1992) Eur J Biochem , vol.205
    • Pierik, A.J.1    Duyvis, M.G.2    Van Helvoort, J.3    Wolbert, R.4    Hagen, W.R.5
  • 51
    • 27344457171 scopus 로고    scopus 로고
    • The type i/type ii cytochrome c3 complex: An electron transfer link in the hydrogen-sulphate reduction pathway
    • Pieulle, L., Morelli, X., Gallice, P. et al. (2005). The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulphate reduction pathway. J Mol Biol, 354, 73—90.
    • (2005) J Mol Biol , vol.354 , pp. 73-90
    • Pieulle, L.1    Morelli, X.2    Gallice, P.3
  • 52
    • 0042266274 scopus 로고    scopus 로고
    • A novel membrane-bound respiratory complex from
    • Desulfovibrio desulfuricans ATCC 27774
    • Pires, R. H., Lourenco, A. I., Morais, F. et al. (2003). A novel membrane-bound respiratory complex from Desulfovibrio desulfuricans ATCC 27774. Biochim Biophys Acta, 1605, 67—82.
    • (2003) Biochim Biophys Acta , vol.1605 , pp. 67-82
    • Pires, R.H.1    Lourenco, A.I.2    Morais, F.3
  • 53
    • 30344465022 scopus 로고    scopus 로고
    • Characterization of the desulfovibrio desulfuricans atcc 27774 dsrmkjop complex — a membrane-bound redox complex involved in the sulphate respiratory pathway
    • Pires, R. H., Venceslau, S., Morais, F. et al. (2006). Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex — a membrane-bound redox complex involved in the sulphate respiratory pathway. Biochemistry, 45, 249—262.
    • (2006) Biochemistry , vol.45 , pp. 249-262
    • Pires, R.H.1    Venceslau, S.2    Morais, F.3
  • 54
    • 0036174874 scopus 로고    scopus 로고
    • Effects of deletion of genes encoding fe-only hydrogenase of desulfovibrio vulgaris hildenborough on hydrogen and lactate metabolism
    • Pohorelic, B. K., Voordouw, J. K., Lojou, E. et al. (2002). Effects of deletion of genes encoding Fe-only hydrogenase of Desulfovibrio vulgaris Hildenborough on hydrogen and lactate metabolism. J Bacteriol, 184, 679—686.
    • (2002) J Bacteriol , vol.184 , pp. 679-686
    • Pohorelic, B.K.1    Voordouw, J.K.2    Lojou, E.3
  • 55
    • 4344713183 scopus 로고    scopus 로고
    • The genome of desulfotalea psychrophila, a sulphate-reducing bacterium from permanently cold arctic sediments
    • Rabus, R., Ruepp, A., Frickey, T. et al. (2004). The genome of Desulfotalea psychrophila, a sulphate-reducing bacterium from permanently cold Arctic sediments. Environ Microbiol, 6, 887—902.
    • (2004) Environ Microbiol , pp. 887-902
    • Rabus, R.1    Ruepp, A.2    Frickey, T.3
  • 57
    • 0031558763 scopus 로고    scopus 로고
    • Characterization of the nife hydrogenase from the sulphate reducer desulfovibrio vulgaris hildenborough
    • Romao, C. V., Pereira, I. A., Xavier, A. V., Legall, J. and Teixeira, M. (1997). Characterization of the NiFe hydrogenase from the sulphate reducer Desulfovibrio vulgaris Hildenborough. Biochem Biophys Res Commun, 240, 75—79.
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 75-79
    • Romao, C.V.1    Pereira, I.A.2    Xavier, A.V.3    Legall, J.4    Teixeira, M.5
  • 58
    • 0027323851 scopus 로고
    • The hmc operon of desulfovibrio vulgaris subsp. Vulgaris hildenborough encodes a potential transmembrane redox protein complex
    • Rossi, M., Pollock, W. B., Reij, M. W. et al. (1993). The hmc operon of Desulfovibrio vulgaris subsp. 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.2    Reij, M.W.3
  • 59
    • 0024993705 scopus 로고
    • Cloning and sequencing of the locus encoding the large and small subunit genes of the periplasmic nife hydrogenase from
    • Rousset, M., Dermoun, Z., Hatchikian, C. E. and Belaich, J. P. (1990). Cloning and sequencing of the locus encoding the large and small subunit genes of the periplasmic Nife hydrogenase from Desulfovibrio fructosovorans. Gene, 94, 95 — 101.
    • (1990) Desulfovibrio Fructosovorans. Gene , vol.94
    • Rousset, M.1    Dermoun, Z.2    Hatchikian, C.E.3    Belaich, J.P.4
  • 60
    • 0035973869 scopus 로고    scopus 로고
    • In the facultative sulphate/nitrate reducer desulfovibrio desulfuricans atcc 27774, the nine-haem cytochrome c is part of a membrane-bound redox complex mainly expressed in sulphate-grown cells
    • Saraiva, L. M., Da Costa, P. N., Conte, C., Xavier, A. V. and Legall, J. (2001). In the facultative sulphate/nitrate reducer Desulfovibrio desulfuricans ATCC 27774, the nine-haem cytochrome c is part of a membrane-bound redox complex mainly expressed in sulphate-grown cells. Biochim Biophys Acta, 1520, 63—70.
    • (2001) Biochim Biophys Acta , vol.1520 , pp. 63-70
    • Saraiva, L.M.1    Da Costa, P.N.2    Conte, C.3    Xavier, A.V.4    Legall, J.5
  • 61
    • 0027131592 scopus 로고
    • Identification of a new class of nitrogen-fixation genes in rhodobacter capsulatus — a putative membrane complex involved in electron-transport to nitrogenase
    • Schmehl, M., Jahn, A., Vilsendorf, A. M. Z. et al. (1993). Identification of a new class of nitrogen-fixation genes in Rhodobacter capsulatus — a putative membrane complex involved in electron-transport to nitrogenase. Mol Gen Genet, 241, 602—615.
    • (1993) Mol Gen Genet , vol.241 , pp. 602-615
    • Schmehl, M.1    Jahn, A.2    Vilsendorf, A.3
  • 62
    • 0028787109 scopus 로고
    • Purification and characterization of the formate dehydrogenase from desulfovibrio vulgaris hildenborough
    • Sebban, C., Blanchard, L., Bruschi, M. and Guerlesquin, F. (1995). Purification and characterization of the formate dehydrogenase from Desulfovibrio vulgaris Hildenborough. FEMS Microbiol Lett, 133, 143—149.
    • (1995) FEMS Microbiol Lett , vol.133 , pp. 143-149
    • Sebban, C.1    Blanchard, L.2    Bruschi, M.3    Guerlesquin, F.4
  • 63
    • 14844301641 scopus 로고    scopus 로고
    • Direct interaction of coenzyme m with the active-site fe-s cluster of heterodisulfide reductase
    • Shokes, J. E., Duin, E. C., Bauer, C. et al. (2005). Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase. FEBS Lett, 579, 1741—1744.
    • (2005) FEBS Lett , vol.579 , pp. 1741-1744
    • Shokes, J.E.1    Duin, E.C.2    Bauer, C.3
  • 64
    • 0020084735 scopus 로고
    • Oxygen-labile lactate dehydrogenase activity in desulfovibrio desulfuricans
    • Stams, A. J. M. and Hansen, T. A. (1982). Oxygen-labile lactate dehydrogenase activity in Desulfovibrio desulfuricans. FEMS Microbiol Lett, 13, 389—394.
    • (1982) FEMS Microbiol Lett , vol.13 , pp. 389-394
    • Stams, A.1    Hansen, T.A.2
  • 65
    • 2142644598 scopus 로고    scopus 로고
    • Modeling electron transfer thermodynamics in protein complexes: Interaction between two cytochromes c(3)
    • Teixeira, V. H., Baptista, A. M. and Soares, C. M. (2004). Modeling electron transfer thermodynamics in protein complexes: interaction between two cytochromes c(3). Biophys J, 86, 2773—2785.
    • (2004) Biophys J , vol.86 , pp. 2773-2785
    • Teixeira, V.H.1    Baptista, A.M.2    Soares, C.M.3
  • 66
    • 0035814790 scopus 로고    scopus 로고
    • Three-dimensional structure of the nonaheme cytochrome c from desulfovibrio desulfuricans essex in the fe(Iii) state at 1.89 a resolution
    • Umhau, S., Fritz, G., Diederichs, K. et al. (2001). Three-dimensional structure of the nonaheme cytochrome c from Desulfovibrio desulfuricans Essex in the Fe(III) state at 1.89 A resolution. Biochemistry, 40, 1308—1316.
    • (2001) Biochemistry , vol.40 , pp. 1308-1316
    • Umhau, S.1    Fritz, G.2    Diederichs, K.3
  • 67
    • 0035804166 scopus 로고    scopus 로고
    • A membrane-bound cytochrome c3: A type ii cytochrome c3 from desulfovibrio vulgaris hildenborough
    • Valente, F. M. A., Saraiva, L. M., Legall, J. et al. (2001). A membrane-bound cytochrome c3: a type II cytochrome c3 from Desulfovibrio vulgaris Hildenborough. Chembiochem, 2, 895—905.
    • (2001) Chembiochem , vol.2 , pp. 895-905
    • Valente, F.1    Saraiva, L.M.2    Legall, J.3
  • 68
    • 27944451793 scopus 로고    scopus 로고
    • Hydrogenases in desulfovibrio vulgaris hildenborough: Structural and physiologic characterisation of the membrane-bound nifese hydrogenase
    • Valente, F. M. A., Oliveira, A. S. F., Gnadt, N. et al. (2005). Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound NiFeSe hydrogenase. J Biol Inorg Chem, 10, 667—682.
    • (2005) J Biol Inorg Chem , vol.10 , pp. 667-682
    • Valente, F.1    Oliveira, A.2    Gnadt, N.3
  • 69
    • 33646260195 scopus 로고    scopus 로고
    • Selenium is involved in regulation of periplasmic hydrogenase gene expression in desulfovibrio vulgaris hildenborough
    • Valente, F. M. A., Almeida, C. C., Pacheco, I. et al., (2006). Selenium is involved in regulation of periplasmic hydrogenase gene expression in Desulfovibrio vulgaris Hildenborough. J Bacteriol, 188, 3228—3235.
    • (2006) J Bacteriol , vol.188 , pp. 3228-3235
    • Valente, F.1    Almeida, C.C.2    Pacheco, I.3
  • 70
    • 0017812528 scopus 로고
    • Separation of hydrogenase from intact cells of desulfovibrio vulgaris — purification and properties
    • Van der Westen, H. M., Mayhew, S.G. and Veeger, C. (1978). Separation of hydrogenase from intact cells of Desulfovibrio vulgaris — purification and properties. FEBS Lett, 86, 122—126.
    • (1978) FEBS Lett , vol.86 , pp. 122-126
    • Van Der Westen, H.M.1    Mayhew, S.G.2    Veeger, C.3
  • 71
    • 2142653130 scopus 로고    scopus 로고
    • Molecular biology of microbial hydrogenases
    • Vignais, P. M. and Colbeau, A. (2004). Molecular biology of microbial hydrogenases. Curr Issues Mol Biol, 6, 159—188.
    • (2004) Curr Issues Mol Biol , vol.6 , pp. 159-188
    • Vignais, P.M.1    Colbeau, A.2
  • 72
    • 0028889166 scopus 로고
    • Crystal structure of the nickel-iron hydrogenase from
    • Volbeda, A., Charon, M. H., Piras, C. et al. (1995). Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature, 373, 580—587.
    • (1995) Desulfovibrio Gigas. Nature , vol.373 , pp. 580-587
    • Volbeda, A.1    Charon, M.H.2    Piras, C.3
  • 73
    • 23644451968 scopus 로고    scopus 로고
    • Structure-function relationships of nickel-iron sites in hydrogenase and a comparison with the active sites of other nickel-iron enzymes
    • Volbeda, A. and Fontecilla-Camps, J.C. (2005). Structure-function relationships of nickel-iron sites in hydrogenase and a comparison with the active sites of other nickel-iron enzymes. Coordin Chem Rev, 249, 1609—1619.
    • (2005) Coordin Chem Rev , vol.249 , pp. 1609-1619
    • Volbeda, A.1    Fontecilla-Camps, J.C.2
  • 74
    • 0025681925 scopus 로고
    • Distribution ofhydrogenase genes in desulfovibrio sAnd their use in identification of species from the oil field environment
    • Voordouw, G., Niviere, V., Ferris, F. G., Fedorak, P. M. and Westlake, D. W. S. (1990). Distribution ofhydrogenase genes in Desulfovibrio sand their use in identification of species from the oil field environment. Appl Environ Microbiol, 56, 3748—3754.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 3748-3754
    • Voordouw, G.1    Niviere, V.2    Ferris, F.G.3    Fedorak, P.M.4    Westlake, D.5
  • 75
    • 0036837968 scopus 로고    scopus 로고
    • Carbon monoxide cycling by desulfovibrio vulgaris hildenborough
    • Voordouw, G. (2002). Carbon monoxide cycling by Desulfovibrio vulgaris Hildenborough. J Bacteriol, 184, 5903—5911.
    • (2002) J Bacteriol , vol.184 , pp. 5903-5911
    • Voordouw, G.1
  • 76
    • 3543041902 scopus 로고    scopus 로고
    • Thermodynamic and choreographic constraints for energy transduction by cytochrome c oxidase
    • Xavier, A. V. (2004). Thermodynamic and choreographic constraints for energy transduction by cytochrome c oxidase. Biochim Biophys Acta, 1658, 23—30.
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 23-30
    • Xavier, A.V.1


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