메뉴 건너뛰기




Volumn 47, Issue 3, 2008, Pages 957-964

Disulfide bond-dependent mechanism of protection against oxidative stress in pyruvate-ferredoxin oxidoreductase of anaerobic Desulfovibrio bacteria

Author keywords

[No Author keywords available]

Indexed keywords

CLUSTER ANALYSIS; COENZYMES; OXIDATION; OXIDATIVE STRESS; OXYGEN; REACTION KINETICS;

EID: 38349131590     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7014713     Document Type: Article
Times cited : (32)

References (42)
  • 1
    • 0013901576 scopus 로고
    • A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium
    • Evans, M. C., Buchanan, B. B., and Arnon, D. I. (1966) A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium, Proc. Natl. Acad. Sci. U.S.A. 55 (4), 928-934.
    • (1966) Proc. Natl. Acad. Sci. U.S.A , vol.55 , Issue.4 , pp. 928-934
    • Evans, M.C.1    Buchanan, B.B.2    Arnon, D.I.3
  • 2
    • 0030937675 scopus 로고    scopus 로고
    • Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum
    • Tersteegen, A., Linder, D., Thauer, R. K., and Hedderich, R. (1997) Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum, Eur. J. Biochem. 244 (3), 862-868.
    • (1997) Eur. J. Biochem , vol.244 , Issue.3 , pp. 862-868
    • Tersteegen, A.1    Linder, D.2    Thauer, R.K.3    Hedderich, R.4
  • 4
    • 0037861912 scopus 로고    scopus 로고
    • The anabolic pyruvate oxidoreductase from Methanococcus maripaludis
    • Lin, W. C., Yang, Y. L., and Whitman, W. B. (2003) The anabolic pyruvate oxidoreductase from Methanococcus maripaludis, Arch. Microbiol. 179 (6), 444-456.
    • (2003) Arch. Microbiol , vol.179 , Issue.6 , pp. 444-456
    • Lin, W.C.1    Yang, Y.L.2    Whitman, W.B.3
  • 5
    • 0034666137 scopus 로고    scopus 로고
    • The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway
    • Furdui, C., and Ragsdale, S. W. (2000) The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway, J. Biol. Chem. 275 (37), 28494-28499.
    • (2000) J. Biol. Chem , vol.275 , Issue.37 , pp. 28494-28499
    • Furdui, C.1    Ragsdale, S.W.2
  • 6
    • 0030050611 scopus 로고    scopus 로고
    • Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima
    • Kletzin, A., and Adams, M. W. (1996) Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima, J. Bacteriol. 178 (1), 248-257.
    • (1996) J. Bacteriol , vol.178 , Issue.1 , pp. 248-257
    • Kletzin, A.1    Adams, M.W.2
  • 7
    • 0029784085 scopus 로고    scopus 로고
    • 2-Oxoacid: Ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7
    • Zhang, Q., Iwasaki, T., Wakagi, T., and Oshima, T. (1996) 2-Oxoacid: Ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7, J. Biochem. (Tokyo, Jpn.) 120 (3), 587-599.
    • (1996) J. Biochem. (Tokyo, Jpn.) , vol.120 , Issue.3 , pp. 587-599
    • Zhang, Q.1    Iwasaki, T.2    Wakagi, T.3    Oshima, T.4
  • 8
    • 0029042173 scopus 로고
    • Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus
    • Pieulle, L., Guigliarelli, B., Asso, M., Dole, F., Bernadac, A., and Hatchikian, E. C. (1995) Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus, Biochim. Biophys. Acta 1250 (1), 49-59.
    • (1995) Biochim. Biophys. Acta , vol.1250 , Issue.1 , pp. 49-59
    • Pieulle, L.1    Guigliarelli, B.2    Asso, M.3    Dole, F.4    Bernadac, A.5    Hatchikian, E.C.6
  • 10
    • 0030884074 scopus 로고    scopus 로고
    • Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability
    • Pieulle, L., Magro, V., and Hatchikian, E. C. (1997) Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability, J. Bacteriol. 179 (18), 5684-5692.
    • (1997) J. Bacteriol , vol.179 , Issue.18 , pp. 5684-5692
    • Pieulle, L.1    Magro, V.2    Hatchikian, E.C.3
  • 11
    • 13044283040 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus
    • Pieulle, L., Chabriere, E., Hatchikian, C., Fontecilla-Camps, J. C., and Charon, M. H. (1999) Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus, Acta Crystallogr., Sect. D: Biol. Crystallogr. 55 (1), 329-331.
    • (1999) Acta Crystallogr., Sect. D: Biol. Crystallogr , vol.55 , Issue.1 , pp. 329-331
    • Pieulle, L.1    Chabriere, E.2    Hatchikian, C.3    Fontecilla-Camps, J.C.4    Charon, M.H.5
  • 12
    • 0032929940 scopus 로고    scopus 로고
    • Crystal structures of the key anaerobic enzyme pyruvate/ferredoxin oxidoreductase, free and in complex with pyruvate
    • Chabriere, E., Charon, M. H., Volbeda, A., Pieulle, L., Hatchikian, E. C., and Fontecilla-Camps, J. C. (1999) Crystal structures of the key anaerobic enzyme pyruvate/ferredoxin oxidoreductase, free and in complex with pyruvate, Nat. Struct. Biol. 6 (2), 182-190.
    • (1999) Nat. Struct. Biol , vol.6 , Issue.2 , pp. 182-190
    • Chabriere, E.1    Charon, M.H.2    Volbeda, A.3    Pieulle, L.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 16
    • 0004233143 scopus 로고
    • 2nd ed, pp, Cambridge University Press, Cambridge, U.K
    • Postgate, J. R. (1984) The Sulphate-Reducing Bacteria, 2nd ed., pp 12-13, Cambridge University Press, Cambridge, U.K.
    • (1984) The Sulphate-Reducing Bacteria , pp. 12-13
    • Postgate, J.R.1
  • 17
    • 0001762863 scopus 로고
    • Effect of phosphate on the corrosion of carbon steel and on the composition of corrosion products in two-stage continuous cultures of Desulfovibrio desulfuricans
    • Weimer, P. J., Van Kavelaar, M. J., Michel, C. B., and Ng, T. K. (1988) Effect of phosphate on the corrosion of carbon steel and on the composition of corrosion products in two-stage continuous cultures of Desulfovibrio desulfuricans, Appl. Environ. Microbiol. 54 (2), 386-396.
    • (1988) Appl. Environ. Microbiol , vol.54 , Issue.2 , pp. 386-396
    • Weimer, P.J.1    Van Kavelaar, M.J.2    Michel, C.B.3    Ng, T.K.4
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77 (1), 51-59.
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 20
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster
    • Nakamura, M., Saeki, K., and Takahashi, Y. (1999) Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster, J. Biochem. (Tokyo, Jpn.) 126 (1), 10-18.
    • (1999) J. Biochem. (Tokyo, Jpn.) , vol.126 , Issue.1 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (London, U.K.) 227 (5259), 680-685.
    • (1970) Nature (London, U.K.) , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent, J. Biol. Chem. 193 (1), 265-275.
    • (1951) J. Biol. Chem , vol.193 , Issue.1 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 23
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A., and Weinstein, D. (1976) Assay of proteins in the presence of interfering materials, Anal. Biochem. 70 (1), 241-250.
    • (1976) Anal. Biochem , vol.70 , Issue.1 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 24
    • 2342475768 scopus 로고    scopus 로고
    • Heidelberg, J. F., Seshadri, R., Haveman, S. A., Hemme, C. L., Paulsen, I. T., Kolonay, J. F., Eisen, J. A., Ward, N., Methe, B., Brinkac, L. M., Daugherty, S. C., Deboy, R. T., Dodson, R. J., Durkin, A. S., Madupu, R., Nelson, W. C., Sullivan, S. A., Fouts, D., Haft, D. H., Selengut, J., Peterson, J. D., Davidsen, T. M., Zafar, N., Zhou, L., Radune, D., Dimitrov, G., Hance, M., Tran, K., Khouri, H., Gill, J., Utterback, T. R., Feldblyum, T. V., Wall, J. D., Voordouw, G., and Fraser, C. M. (2004) The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough, Nat. Biotechnol. 22 (5), 554-559.
    • Heidelberg, J. F., Seshadri, R., Haveman, S. A., Hemme, C. L., Paulsen, I. T., Kolonay, J. F., Eisen, J. A., Ward, N., Methe, B., Brinkac, L. M., Daugherty, S. C., Deboy, R. T., Dodson, R. J., Durkin, A. S., Madupu, R., Nelson, W. C., Sullivan, S. A., Fouts, D., Haft, D. H., Selengut, J., Peterson, J. D., Davidsen, T. M., Zafar, N., Zhou, L., Radune, D., Dimitrov, G., Hance, M., Tran, K., Khouri, H., Gill, J., Utterback, T. R., Feldblyum, T. V., Wall, J. D., Voordouw, G., and Fraser, C. M. (2004) The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough, Nat. Biotechnol. 22 (5), 554-559.
  • 26
    • 0034890121 scopus 로고    scopus 로고
    • Aging and oxidation of reactive protein sulfhydryls
    • Thomas, J. A., and Mallis, R. J. (2001) Aging and oxidation of reactive protein sulfhydryls, Exp. Gerontol. 36 (9), 1519-1526.
    • (2001) Exp. Gerontol , vol.36 , Issue.9 , pp. 1519-1526
    • Thomas, J.A.1    Mallis, R.J.2
  • 27
    • 0024828942 scopus 로고
    • Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 Å resolution
    • Fukuyama, K., Matsubara, H., Tsukihara, T., and Katsube, Y. (1989) Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 Å resolution, J. Mol. Biol. 210 (2), 383-398.
    • (1989) J. Mol. Biol , vol.210 , Issue.2 , pp. 383-398
    • Fukuyama, K.1    Matsubara, H.2    Tsukihara, T.3    Katsube, Y.4
  • 28
    • 0035119660 scopus 로고    scopus 로고
    • Valine 77 of heterocystous ferredoxin FdxH2 in Anabaena variabilis strain ATCC 29413 is critical for its oxygen sensitivity
    • Singh, B. B., Curdt, I., Shomburg, D., Bisen, P. S., and Bohme, H. (2001) Valine 77 of heterocystous ferredoxin FdxH2 in Anabaena variabilis strain ATCC 29413 is critical for its oxygen sensitivity, Mol. Cell. Biochem. 217 (1-2), 137-142.
    • (2001) Mol. Cell. Biochem , vol.217 , Issue.1-2 , pp. 137-142
    • Singh, B.B.1    Curdt, I.2    Shomburg, D.3    Bisen, P.S.4    Bohme, H.5
  • 30
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Åslund, F., and Storz, G. (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation, Science (Washington, DC, U.S.) 13, 1718-1722.
    • (1998) Science (Washington, DC, U.S.) , vol.13 , pp. 1718-1722
    • Zheng, M.1    Åslund, F.2    Storz, G.3
  • 31
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol disulfide status
    • Åslund, F., Zheng, M., Beckwith, J., and Stor, G. (1999) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol disulfide status, Proc. Natl. Acad. Sci. U.S.A. 96, 6161-6165.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 6161-6165
    • Åslund, F.1    Zheng, M.2    Beckwith, J.3    Stor, G.4
  • 32
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob, U., Muse, W., Eser, M., and Bardwell, J. C. A. (1999) Chaperone activity with a redox switch, Cell 96, 341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.A.4
  • 33
    • 33748757442 scopus 로고    scopus 로고
    • Transcriptional activation of dehalorespiration: Identification of redox-active cysteines regulating dimerization and DNA binding
    • Pop, S. M., Gupta, N., Ashraf, S., Raza, A. S., and Ragsdale, S. W. (2006) Transcriptional activation of dehalorespiration: Identification of redox-active cysteines regulating dimerization and DNA binding, J. Biol. Chem. 281, 26382-26390.
    • (2006) J. Biol. Chem , vol.281 , pp. 26382-26390
    • Pop, S.M.1    Gupta, N.2    Ashraf, S.3    Raza, A.S.4    Ragsdale, S.W.5
  • 34
    • 21644446649 scopus 로고    scopus 로고
    • Spectroscopic characterization of site-specific [Fe(4)S(4)] cluster chemistry in ferredoxin. Thioredoxin reductase: Implications for the catalytic mechanism
    • Walters, E. M., Garcia-Serres, R., Jameson, G. N., Glauser, D. A., Bourquin, F., Manieri, W., Schürmann, P., Johnson, M. K., and Huynh, B. H. (2005) Spectroscopic characterization of site-specific [Fe(4)S(4)] cluster chemistry in ferredoxin. Thioredoxin reductase: implications for the catalytic mechanism, J. Am. Chem. Soc. 127 (26), 9612-9624.
    • (2005) J. Am. Chem. Soc , vol.127 , Issue.26 , pp. 9612-9624
    • Walters, E.M.1    Garcia-Serres, R.2    Jameson, G.N.3    Glauser, D.A.4    Bourquin, F.5    Manieri, W.6    Schürmann, P.7    Johnson, M.K.8    Huynh, B.H.9
  • 36
    • 0035062654 scopus 로고    scopus 로고
    • How does oxygen inhibit central metabolism in the obligate anaerobe
    • Pan, N., and Imlay, J. A. (2001) How does oxygen inhibit central metabolism in the obligate anaerobe Bacteroides thetaiotaomicron?, Mol. Microbiol. 39 (6), 1562-1571.
    • (2001) Bacteroides thetaiotaomicron?, Mol. Microbiol , vol.39 , Issue.6 , pp. 1562-1571
    • Pan, N.1    Imlay, J.A.2
  • 37
    • 33748747128 scopus 로고    scopus 로고
    • Oxygen defense in sulfate-reducing bacteria
    • Dolla, A., Fournier, M., and Dermoun, Z. (2006) Oxygen defense in sulfate-reducing bacteria, J. Biotechnol. 126 (1), 87-100.
    • (2006) J. Biotechnol , vol.126 , Issue.1 , pp. 87-100
    • Dolla, A.1    Fournier, M.2    Dermoun, Z.3
  • 38
    • 0004233143 scopus 로고
    • 2nd ed, p, Cambridge University Press, Cambridge, U.K
    • Postgate, J. R. (1984) The Sulphate-Reducing Bacteria, 2nd ed., p 208, Cambridge University Press, Cambridge, U.K.
    • (1984) The Sulphate-Reducing Bacteria , pp. 208
    • Postgate, J.R.1
  • 39
    • 0029869132 scopus 로고    scopus 로고
    • Anaerobes response to oxygen: The sulfate-reducing bacteria
    • Le Gall, J., and Xavier, A. V. (1996) Anaerobes response to oxygen: The sulfate-reducing bacteria, Anaerobe 2 (1), 1-9.
    • (1996) Anaerobe , vol.2 , Issue.1 , pp. 1-9
    • Le Gall, J.1    Xavier, A.V.2
  • 42
    • 0012293235 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlo, CA
    • DeLano, W. L. (2002) PyMOL, DeLano Scientific, San Carlo, CA.
    • (2002) PyMOL
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.