메뉴 건너뛰기




Volumn 45, Issue 34, 2006, Pages 10359-10367

The Tmc complex from Desulfovibrio vulgaris Hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; ELECTRON TRANSITIONS; MICROORGANISMS; OXIDATION; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 33748680507     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0610294     Document Type: Article
Times cited : (42)

References (43)
  • 2
    • 30344448239 scopus 로고
    • Mineralization of organic matter in the sea-bed-the role of sulphate reduction
    • Jørgensen, B. B. (1982) Mineralization of organic matter in the sea-bed-the role of sulphate reduction, Nature 390, 364-370.
    • (1982) Nature , vol.390 , pp. 364-370
    • Jørgensen, B.B.1
  • 3
    • 20444385906 scopus 로고    scopus 로고
    • Sulphate respiration from hydrogen in Desulfovibrio bacteria: A structural biology overview
    • Matias, P. M.; Pereira, I. A. C., 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.C.2    Soares, C.M.3    Carrondo, M.A.4
  • 8
    • 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
  • 9
    • 30344465022 scopus 로고    scopus 로고
    • Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex - A membrane-bound redox complex involved in sulfate respiration
    • Pires, R. H., Venceslau, S. S., Morais, F., Teixeira, M., Xavier, A. V., and Pereira, I. A. C. (2006) Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex-a membrane-bound redox complex involved in sulfate respiration, Biochemistry 45, 249-262.
    • (2006) Biochemistry , vol.45 , pp. 249-262
    • Pires, R.H.1    Venceslau, S.S.2    Morais, F.3    Teixeira, M.4    Xavier, A.V.5    Pereira, I.A.C.6
  • 10
    • 85047695985 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound enzyme complex from the sulfate-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 sulfate-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
  • 11
    • 26444599659 scopus 로고    scopus 로고
    • Clustered genes related to sulfale respiration in uncultured prokaryotes support the theory of their concomitant horizontal transfer
    • Mussmann, M., Richter, M., Lombardot, T., Meyerdierks, A., Kuever, J., Kube, M., Glockner, F. O., and Amann, R. (2005) Clustered genes related to sulfale respiration in uncultured prokaryotes support the theory of their concomitant horizontal transfer, J. Bacteriol. 187, 7126-7137.
    • (2005) J. Bacteriol. , vol.187 , pp. 7126-7137
    • Mussmann, M.1    Richter, M.2    Lombardot, T.3    Meyerdierks, A.4    Kuever, J.5    Kube, M.6    Glockner, F.O.7    Amann, R.8
  • 12
    • 30344468701 scopus 로고    scopus 로고
    • Multi-heme c cytochromes and enzymes
    • (King, R. B., Ed.) John Wiley & Sons, New York
    • Pereira, I. A. C., and Xavier, A. V. (2005) Multi-Heme c Cytochromes and Enzymes, in Encyclopedia of Inorganic Chemistry (King, R. B., Ed.) John Wiley & Sons, New York.
    • (2005) Encyclopedia of Inorganic Chemistry
    • Pereira, I.A.C.1    Xavier, A.V.2
  • 13
    • 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., Keon, R. G., Fu, R., and Voordouw, G. (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    Keon, R.G.4    Fu, R.5    Voordouw, G.6
  • 14
    • 0037033048 scopus 로고    scopus 로고
    • Sulfate respiration in Desulfovibrio vulgaris Hildenborough: Structure of the 16-heme cytochrome c HmcA at 2.5 Å resolution and a view of its role in transmembrane electron transfer
    • Matias, P. M., Coelho, A. V., Valente, F. M. A., D., P., LeGall, J., Xavier, A. V., Pereira, I. A. C., and Carrondo, M. A. (2002) Sulfate respiration in Desulfovibrio vulgaris Hildenborough: Structure of the 16-heme cytochrome c HmcA at 2.5 Å 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.M.A.3    P, D.4    LeGall, J.5    Xavier, A.V.6    Pereira, I.A.C.7    Carrondo, M.A.8
  • 16
    • 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. 67, 376-383.
    • (1997) Arch. Microbiol. , vol.67 , pp. 376-383
    • Keon, R.G.1    Fu, R.2    Voordouw, G.3
  • 17
    • 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.K.J.2    Voordouw, J.K.3    Voordouw, G.4
  • 18
    • 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
  • 19
    • 0031756314 scopus 로고    scopus 로고
    • Electron transfer between hydrogenases and mono and multiheme cytochromes in Desulfovibrio spp
    • Pereira, I. A. C., Romão, C. V., Xavier, A. V., LeGall, J., and Teixeira, M. (1998) Electron transfer between hydrogenases and mono and multiheme cytochromes in Desulfovibrio spp., J. Biol. Inorg. Chem. 3, 494-498.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 494-498
    • Pereira, I.A.C.1    Romão, C.V.2    Xavier, A.V.3    Legall, J.4    Teixeira, M.5
  • 20
    • 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
  • 21
    • 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., Coelho, A. V., Thompson, A. W., Sieker, L. C., Gall, J. L., and Carrondo, M. A. (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    Coelho, A.V.4    Thompson, A.W.5    Sieker, L.C.6    Gall, J.L.7    Carrondo, M.A.8
  • 24
    • 0009790182 scopus 로고
    • Desulfovibrio vulgaris hydrogenase - A nonheme iron enzyme lacking nickel that exhibits anomalous electron-paramagnetic-resonance and Mossbauer-spectra
    • Huynh, B. H., Czechowski, M. H., Kruger, H. J., Dervartanian, D. V., Peck, H. D., and Legall, J. (1984) Desulfovibrio vulgaris hydrogenase-a nonheme iron enzyme lacking nickel that exhibits anomalous electron-paramagnetic- resonance and Mossbauer-spectra, Proc. Natl. Acad. Sci. U.S.A. 81, 3728-3732.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3728-3732
    • Huynh, B.H.1    Czechowski, M.H.2    Kruger, H.J.3    Dervartanian, D.V.4    Peck, H.D.5    Legall, J.6
  • 26
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra, Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 27
    • 0027407150 scopus 로고
    • Pitfalls in assigning heme axial coordination by EPR. c-Type cytochromes with atypical Met-His ligation
    • Teixeira, M., Campos, A. P., Aguiar, A. P., Costa, H. S., Santos, H., Turner, D. L., and Xavier, A. V. (1993) Pitfalls in assigning heme axial coordination by EPR. c-Type cytochromes with atypical Met-His ligation, FEBS Lett. 317, 233-236.
    • (1993) FEBS Lett. , vol.317 , pp. 233-236
    • Teixeira, M.1    Campos, A.P.2    Aguiar, A.P.3    Costa, H.S.4    Santos, H.5    Turner, D.L.6    Xavier, A.V.7
  • 28
    • 0025647235 scopus 로고
    • Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis
    • Lemma, E., Unden, G., and Kroger, A. (1990) Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis, Arch. Microbiol. 155, 62-67.
    • (1990) Arch. Microbiol. , vol.155 , pp. 62-67
    • Lemma, E.1    Unden, G.2    Kroger, A.3
  • 29
    • 0033615642 scopus 로고    scopus 로고
    • Ubiquinone at center N is responsible for triphasic reduction of cytochrome b in the cytochrome bc(1) complex
    • Snyder, C. H., and Trumpower, B. L. (1999) Ubiquinone at center N is responsible for triphasic reduction of cytochrome b in the cytochrome bc(1) complex, J Biol. Chem. 274, 31209-31216.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31209-31216
    • Snyder, C.H.1    Trumpower, B.L.2
  • 30
    • 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., Voordouw, G., Heidelberg, J. F., and Rabus, R. (2003) Gene expression analysis of energy metabolism mutants of Desulfovibrio vulgaris Hildenborough indicates an important role for alcohol dehydrogenase, J. Bacteriol. 185, 4345-4353.
    • (2003) J. Bacteriol. , vol.185 , pp. 4345-4353
    • Haveman, S.A.1    Brunelle, V.2    Voordouw, J.K.3    Voordouw, G.4    Heidelberg, J.F.5    Rabus, R.6
  • 31
    • 13944268797 scopus 로고    scopus 로고
    • A novel method for accurate operon predictions in all sequenced prokaryotes
    • Price, M. N., Huang, K. H., Aim, E. J., and Arkin, A. P. (2005) A novel method for accurate operon predictions in all sequenced prokaryotes, Nucleic Acids Res. 33, 880-892.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 880-892
    • Price, M.N.1    Huang, K.H.2    Aim, E.J.3    Arkin, A.P.4
  • 32
    • 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
  • 33
    • 0037434849 scopus 로고    scopus 로고
    • Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme
    • Duin, E. C., Bauer, C., Jaun, B., and Hedderich, R. (2003) Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme, FEBS Lett. 538, 81-84.
    • (2003) FEBS Lett. , vol.538 , pp. 81-84
    • Duin, E.C.1    Bauer, C.2    Jaun, B.3    Hedderich, R.4
  • 35
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and von Heijne, G. (2000) How proteins adapt to a membrane-water interface, Trends Biochem. Sci. 25, 429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 36
    • 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
  • 37
    • 3142758742 scopus 로고    scopus 로고
    • (57)Fe ENDOR spectroscopy on the iron-sulfur cluster involved in substrate reduction of heterodisulflde reductase
    • Bennati, M., Weiden, N., Dinse, K. P., and Hedderich, R. (2004) (57)Fe ENDOR spectroscopy on the iron-sulfur cluster involved in substrate reduction of heterodisulflde reductase, J. Am. Chem. Soc. 126, 8378-8379.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8378-8379
    • Bennati, M.1    Weiden, N.2    Dinse, K.P.3    Hedderich, R.4
  • 38
    • 14844301641 scopus 로고    scopus 로고
    • Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulflde reductase
    • Shokes, J. E., Duin, E. C., Bauer, C., Jaun, B., Hedderich, R., Koch, J., and Scott, R. A. (2005) Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulflde 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    Jaun, B.4    Hedderich, R.5    Koch, J.6    Scott, R.A.7
  • 42
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.