메뉴 건너뛰기




Volumn 4, Issue 1, 1998, Pages 45-55

Molecular study and partial characterization of iron-only hydrogenase in Desulfovibrio fructosovorans

Author keywords

Desulfovibrio fructosovorans; Iron only hydrogenase; Phylogeny; Purification; Sulfate reducing bacterium

Indexed keywords

BACTERIAL ENZYME; FERREDOXIN; HYDROGENASE; IRON; OLIGONUCLEOTIDE; SIGNAL PEPTIDE;

EID: 0031971063     PISSN: 10759964     EISSN: None     Source Type: Journal    
DOI: 10.1006/anae.1997.0137     Document Type: Article
Times cited : (26)

References (40)
  • 2
    • 0017819828 scopus 로고
    • Growth yields and growth rates ofDesulfovibrios vulgaris
    • Badziong W., Thauer R. K. Growth yields and growth rates ofDesulfovibrios vulgaris. Arch Microbiol. 117:1978;209-214.
    • (1978) Arch Microbiol , vol.117 , pp. 209-214
    • Badziong, W.1    Thauer, R.K.2
  • 3
    • 0019802315 scopus 로고
    • Hydrogen cycling as a general mechanism for energy coupling in the sulphate-reducingDesulfovibrio
    • Odom J. M., Peck H. D. Hydrogen cycling as a general mechanism for energy coupling in the sulphate-reducingDesulfovibrio. FEMS Microbiol Lett. 12:1981;47-50.
    • (1981) FEMS Microbiol Lett , vol.12 , pp. 47-50
    • Odom, J.M.1    Peck, H.D.2
  • 4
    • 0001614967 scopus 로고
    • The dissimilatory sulphate and sulfur reducing bacteria
    • New York: Springer-Verlag
    • Widdel F., Hansen T. H. The dissimilatory sulphate and sulfur reducing bacteria. The Prokaryotes-1993. 1992;Springer-Verlag, New York.
    • (1992) The Prokaryotes-1993
    • Widdel, F.1    Hansen, T.H.2
  • 5
    • 0021197001 scopus 로고
    • Hydrogenase, electron-transfert proteins, and energy coupling in the sulphate-reducing bacteriaDesulfovibrio
    • Odom J. M., Peck H. D. Hydrogenase, electron-transfert proteins, and energy coupling in the sulphate-reducing bacteriaDesulfovibrio. Annu Rev Microbiol. 38:1984;551-592.
    • (1984) Annu Rev Microbiol , vol.38 , pp. 551-592
    • Odom, J.M.1    Peck, H.D.2
  • 6
    • 0026612820 scopus 로고
    • H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea
    • Zirngirbl C., Van Dongen W., Schworer B., Von Bunau R., Richter M., Klein A., Thauer R. K. H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea. Eur J Biochem. 208:1992;511-520.
    • (1992) Eur J Biochem , vol.208 , pp. 511-520
    • Zirngirbl, C.1    Van Dongen, W.2    Schworer, B.3    Von Bunau, R.4    Richter, M.5    Klein, A.6    Thauer, R.K.7
  • 8
    • 0000003202 scopus 로고
    • Evolution of hydrogenase genes
    • Voordouw G. Evolution of hydrogenase genes. Adv Inorganic Chem. 38:1992;397-422.
    • (1992) Adv Inorganic Chem , vol.38 , pp. 397-422
    • Voordouw, G.1
  • 10
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams M. W.W. The structure and mechanism of iron-hydrogenases. Biochimica et Biophysica acta. 1020:1990;115-145.
    • (1990) Biochimica et Biophysica Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 11
    • 0021804386 scopus 로고
    • Nucleotide sequence of the gene encoding the hydrogenase fromDesulfovibrio vulgaris
    • Voordouw G., Brenner S. Nucleotide sequence of the gene encoding the hydrogenase fromDesulfovibrio vulgaris. Eur J Biochem. 148:1985;515-520.
    • (1985) Eur J Biochem , vol.148 , pp. 515-520
    • Voordouw, G.1    Brenner, S.2
  • 12
    • 0024322748 scopus 로고
    • Organization of the genes encoding [Fe] hydrogenase inDesulfovibrio vulgarisoxamicus
    • Voordouw G., Strang J. D., Wilson F. R. Organization of the genes encoding [Fe] hydrogenase inDesulfovibrio vulgarisoxamicus. J Bacteriol. 171:1989;3881-3889.
    • (1989) J Bacteriol , vol.171 , pp. 3881-3889
    • Voordouw, G.1    Strang, J.D.2    Wilson, F.R.3
  • 13
    • 0022530699 scopus 로고
    • The iron-sulfur composition of the active site of hydrogenase fromDesulfovibrio vulgaris
    • Hagen W. R., Van Berkel-Arts A., Kruse-Wolters K. M., Voordouw G., Veeger C. The iron-sulfur composition of the active site of hydrogenase fromDesulfovibrio vulgaris. FEBS Lett. 203:1986;59-63.
    • (1986) FEBS Lett , vol.203 , pp. 59-63
    • Hagen, W.R.1    Van Berkel-Arts, A.2    Kruse-Wolters, K.M.3    Voordouw, G.4    Veeger, C.5
  • 14
    • 0025120224 scopus 로고
    • Characterization of the nickel-iron periplasmic hydrogenase fromDesulfovibrio fructosovorans
    • Hatchikian E. C., Traore A. S., Fernandez V. M., Cammack R. Characterization of the nickel-iron periplasmic hydrogenase fromDesulfovibrio fructosovorans. Eur J Biochem. 187:1990;635-643.
    • (1990) Eur J Biochem , vol.187 , pp. 635-643
    • Hatchikian, E.C.1    Traore, A.S.2    Fernandez, V.M.3    Cammack, R.4
  • 15
    • 0024993705 scopus 로고
    • Cloning and sequencing of the locus encoding the large and small subunits genes of the periplasmic [NiFe] hydrogenase fromDesulfovibrio fructosovorans
    • Rousset M., Dermoun Z., Hatchikian E. C., Belaïch J-P. Cloning and sequencing of the locus encoding the large and small subunits genes of the periplasmic [NiFe] hydrogenase fromDesulfovibrio fructosovorans. Gene. 94:1990;95-101.
    • (1990) Gene , vol.94 , pp. 95-101
    • Rousset, M.1    Dermoun, Z.2    Hatchikian, E.C.3    Belaïch, J-P.4
  • 17
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase inDesulfovibrio fructosovorans
    • Malki S., Saimmaime I., De Luca G., Rousset M., Dermoun Z., Belaïch J-P. Characterization of an operon encoding an NADP-reducing hydrogenase inDesulfovibrio fructosovorans. J Bacteriol. 177:1995;2628-2636.
    • (1995) J Bacteriol , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaïch, J-P.6
  • 18
    • 0031039226 scopus 로고    scopus 로고
    • Physiological characteristics and growth behaviour of single and double hydrogenase mutants ofDesulfovibrio fructosovorans
    • Malki S., De Luca G., Fardeau M-L., Rousset M., Belaïch J-P., Dermoun Z. Physiological characteristics and growth behaviour of single and double hydrogenase mutants ofDesulfovibrio fructosovorans. Arch Microbiol. 167:1997;38-45.
    • (1997) Arch Microbiol , vol.167 , pp. 38-45
    • Malki, S.1    De Luca, G.2    Fardeau, M-L.3    Rousset, M.4    Belaïch, J-P.5    Dermoun, Z.6
  • 19
    • 0025769946 scopus 로고
    • Marker exchange mutagenesis of thehydNDesulfovibrio fructosovorans
    • Rousset M., Dermoun Z., Chippaux M., Belaich J-P. Marker exchange mutagenesis of thehydNDesulfovibrio fructosovorans. Mol Microbiol. 5:1991;1735-1740.
    • (1991) Mol Microbiol , vol.5 , pp. 1735-1740
    • Rousset, M.1    Dermoun, Z.2    Chippaux, M.3    Belaich, J-P.4
  • 21
    • 0022370609 scopus 로고
    • Properties and reactivation of two different deactivated forms ofDesulfovibrio gigas
    • Fernandez V. M., Hatchikian E. C., Cammack R. Properties and reactivation of two different deactivated forms ofDesulfovibrio gigas. Biochim Biophys Acta. 832:1985;69-79.
    • (1985) Biochim Biophys Acta , vol.832 , pp. 69-79
    • Fernandez, V.M.1    Hatchikian, E.C.2    Cammack, R.3
  • 23
    • 0013954237 scopus 로고
    • Multiple forms of bacterial hydrogenases
    • Ackrell B. A.C., Asato R. N., Mower H. F. Multiple forms of bacterial hydrogenases. J Bacteriol. 92:1966;828-838.
    • (1966) J Bacteriol , vol.92 , pp. 828-838
    • Ackrell, B.A.C.1    Asato, R.N.2    Mower, H.F.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymathylated proteins
    • Crestfield A. M., Moore S., Stein W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymathylated proteins. J Biol Chem. 238:1963;622-627.
    • (1963) J Biol Chem , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.H.3
  • 28
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur J. A procedure for the isolation of deoxyribonucleic acid from microorganisms. J Mol Biol. 3:1961;208-218.
    • (1961) J Mol Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 29
    • 0001305277 scopus 로고
    • Amplification of flanking sequences by inverse PCR
    • M.A. Innis, D.H. Gelfand, J.J. Sninsky, & T.J. White. San Diego: Academic Press
    • Ochman H., Medhora M. M., Garza D., Hartl D. L. Amplification of flanking sequences by inverse PCR. Innis M. A., Gelfand D. H., Sninsky J. J., White T. J. PCR Protocols. 1990;Academic Press, San Diego.
    • (1990) PCR Protocols
    • Ochman, H.1    Medhora, M.M.2    Garza, D.3    Hartl, D.L.4
  • 30
    • 0017812528 scopus 로고
    • Separation of hydrogenase from intact cells ofDesulfovibrio vulgaris
    • Van der Westen H., Mayhew S. G., Veeger C. Separation of hydrogenase from intact cells ofDesulfovibrio vulgaris. FEBS Lett. 86:1978;122-126.
    • (1978) FEBS Lett , vol.86 , pp. 122-126
    • Van Der Westen, H.1    Mayhew, S.G.2    Veeger, C.3
  • 31
    • 0026761176 scopus 로고
    • Further characterization of the [Fe] hydrogenase fromDesulfovibrio desulfuricans
    • Hatchikian E. C., Forget N., Fernandez V. M., Williams R., Cammack R. Further characterization of the [Fe] hydrogenase fromDesulfovibrio desulfuricans. Eur J Biochem. 209:1992;357-365.
    • (1992) Eur J Biochem , vol.209 , pp. 357-365
    • Hatchikian, E.C.1    Forget, N.2    Fernandez, V.M.3    Williams, R.4    Cammack, R.5
  • 32
    • 0027221472 scopus 로고
    • Analysis of the periplasmic [NiFe] hydrogenase transcription unit fromDesulfovibrio fructosovorans
    • Rousset M., Dermoun Z., Wall J. D., Belaïch J-P. Analysis of the periplasmic [NiFe] hydrogenase transcription unit fromDesulfovibrio fructosovorans. J Bacteriol. 175:1993;3388-3393.
    • (1993) J Bacteriol , vol.175 , pp. 3388-3393
    • Rousset, M.1    Dermoun, Z.2    Wall, J.D.3    Belaïch, J-P.4
  • 34
    • 0026040877 scopus 로고
    • Primary structure of hydrogenase I fromClostridium pasteurianum
    • Meyer J., Gagnon J. Primary structure of hydrogenase I fromClostridium pasteurianum. Biochemistry. 30:1991;9697-9704.
    • (1991) Biochemistry , vol.30 , pp. 9697-9704
    • Meyer, J.1    Gagnon, J.2
  • 35
    • 0029863961 scopus 로고    scopus 로고
    • Molecular characterization and transcriptional analysis of the putative hydrogenase gene ofClostridium acetobutylicum
    • Gorwa M-F., Croux C., Soucaille P. Molecular characterization and transcriptional analysis of the putative hydrogenase gene ofClostridium acetobutylicum. J Bacteriol. 178:1996;2668-2675.
    • (1996) J Bacteriol , vol.178 , pp. 2668-2675
    • Gorwa, M-F.1    Croux, C.2    Soucaille, P.3
  • 36
    • 0028821460 scopus 로고
    • Characterization and expression of the hydrogenase-encoding gene fromClostridium acetobutylicum
    • Santangelo J. D., Dürre P., Woods D. R. Characterization and expression of the hydrogenase-encoding gene fromClostridium acetobutylicum. Microbiology. 141:1995;171-180.
    • (1995) Microbiology , vol.141 , pp. 171-180
    • Santangelo, J.D.1    Dürre, P.2    Woods, D.R.3
  • 38
    • 0029881944 scopus 로고    scopus 로고
    • Identification and characterization of [Fe] hydrogenase in the hydrogenosome ofTrichomonas vaginalis
    • Bui E. T.N., Johnson P. J. Identification and characterization of [Fe] hydrogenase in the hydrogenosome ofTrichomonas vaginalis. Mol Biochem Parasitol. 76:1996;305-310.
    • (1996) Mol Biochem Parasitol , vol.76 , pp. 305-310
    • Bui, E.T.N.1    Johnson, P.J.2
  • 39
    • 0023985949 scopus 로고
    • Structure, function and evolution of bacterial ferredoxin
    • Bruschi M., Guerlesquin F. Structure, function and evolution of bacterial ferredoxin. FEMS Microbio Rev. 54:1988;155-176.
    • (1988) FEMS Microbio Rev , vol.54 , pp. 155-176
    • Bruschi, M.1    Guerlesquin, F.2
  • 40
    • 0026646678 scopus 로고
    • Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a β-lactamase fusion protein
    • Nivière V., Wong S-L., Voordouw G. Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a β-lactamase fusion protein. J Gen Microbiol. 138:1992;2173-2183.
    • (1992) J Gen Microbiol , vol.138 , pp. 2173-2183
    • Nivière, V.1    Wong, S-L.2    Voordouw, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.