메뉴 건너뛰기




Volumn 38, Issue 5, 1999, Pages 264-267

Distribution of the rubredoxin gene among the Clostridium butyricum species

Author keywords

[No Author keywords available]

Indexed keywords

RUBREDOXIN;

EID: 0345621641     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006799     Document Type: Article
Times cited : (4)

References (30)
  • 2
    • 0014408664 scopus 로고
    • Non-heme iron proteins. V. The amino acid sequence of rubredoxin from Peptostreptococcus Elsdenii
    • Bachmayer H, Peel JL, Yasunobu KT, Mayhew SG (1968b) Non-heme iron proteins. V. The amino acid sequence of rubredoxin from Peptostreptococcus elsdenii. J Biol Chem 243:1024-1032.
    • (1968) J Biol Chem , vol.243 , pp. 1024-1032
    • Bachmayer, H.1    Peel, J.L.2    Yasunobu, K.T.3    Mayhew, S.G.4
  • 3
    • 0000058583 scopus 로고
    • Isolation of members of the family Rhodospirillaceae
    • Berlin, Heidelberg, New York: Springer
    • Biebl H, Pfenning N (1981) Isolation of members of the family Rhodospirillaceae. In: The prokaryotes. Berlin, Heidelberg, New York: Springer, pp 267-273
    • (1981) The Prokaryotes , pp. 267-273
    • Biebl, H.1    Pfenning, N.2
  • 4
    • 0026347331 scopus 로고
    • Determinants of protein hyperthermostability: Purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR
    • Blake PR, Park JB, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard JB, Summers MF, Adams MWW (1991) Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR. Biochemistry 30:10885-10895
    • (1991) Biochemistry , vol.30 , pp. 10885-10895
    • Blake, P.R.1    Park, J.B.2    Bryant, F.O.3    Aono, S.4    Magnuson, J.K.5    Eccleston, E.6    Howard, J.B.7    Summers, M.F.8    Adams, M.W.W.9
  • 5
    • 0017081290 scopus 로고
    • The amino acid sequence of rubredoxin from Desulfovibrio vulgaris
    • Bruschi M (1976a) The amino acid sequence of rubredoxin from Desulfovibrio vulgaris. Biochim Biophys Acta 434:4-17
    • (1976) Biochim Biophys Acta , vol.434 , pp. 4-17
    • Bruschi, M.1
  • 6
    • 0017185356 scopus 로고
    • The amino acid sequence of rubredoxin from the sulfate reducing bacterium, Desulfovibrio gigas
    • Bruschi M (1976b) The amino acid sequence of rubredoxin from the sulfate reducing bacterium, Desulfovibrio gigas. Biochem Biophys Res Commun 70:615-621
    • (1976) Biochem Biophys Res Commun , vol.70 , pp. 615-621
    • Bruschi, M.1
  • 7
    • 0344834199 scopus 로고
    • Iron-sulfur clusters in enzymes: Themes and variations
    • Cammack R (1992) Iron-sulfur clusters in enzymes: themes and variations. Adv Inorg Chem Iron-sulfur proteins 38:281-322
    • (1992) Adv Inorg Chem Iron-sulfur Proteins , vol.38 , pp. 281-322
    • Cammack, R.1
  • 8
    • 0027197351 scopus 로고
    • Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas
    • Chen L, Liu MY, LeGall J, Fareleira P, Santos H, Xavier AV (1993a) Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas. Eur J Biochem 216:443-448
    • (1993) Eur J Biochem , vol.216 , pp. 443-448
    • Chen, L.1    Liu, M.Y.2    LeGall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 9
    • 0027263895 scopus 로고
    • Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the strict anaerobe Desulfovibrio gigas
    • Chen L, Liu MY, LeGall J, Fareleira P, Santos H, Xavier AV (1993b) Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the strict anaerobe Desulfovibrio gigas. Biochem Biophys Res Commun 193:100-105
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 100-105
    • Chen, L.1    Liu, M.Y.2    LeGall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 10
    • 0030954667 scopus 로고    scopus 로고
    • Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin
    • Gomes CM, Silva G, Oliveira S, LeGall J, Liu MY, Xavier AV, Rodrigues-Pousadas C, Teixeira M (1997) Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin. J Biol Chem 272: 22502-22508
    • (1997) J Biol Chem , vol.272 , pp. 22502-22508
    • Gomes, C.M.1    Silva, G.2    Oliveira, S.3    LeGall, J.4    Liu, M.Y.5    Xavier, A.V.6    Rodrigues-Pousadas, C.7    Teixeira, M.8
  • 11
    • 0021866257 scopus 로고
    • Cloning and nucleotide sequence determination of the Clostridium pasteurianum ferredoxin gene
    • Graves MC, Mullenbach GT, Rabinowitz JC (1985) Cloning and nucleotide sequence determination of the Clostridium pasteurianum ferredoxin gene. Proc Natl Acad Sci USA, 82:1653-1657
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1653-1657
    • Graves, M.C.1    Mullenbach, G.T.2    Rabinowitz, J.C.3
  • 13
    • 0028956795 scopus 로고
    • Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, Heliobacillus mobilis
    • Lee WY, Brune DC, LoBrutto R, Blankenship RE (1995) Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, Heliobacillus mobilis. Arch Biochem Biophys 318:80-88
    • (1995) Arch Biochem Biophys , vol.318 , pp. 80-88
    • Lee, W.Y.1    Brune, D.C.2    LoBrutto, R.3    Blankenship, R.E.4
  • 14
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteurianum
    • Lovenberg W, Sobel BE (1965) Rubredoxin: a new electron transfer protein from Clostridium pasteurianum. Proc Natl Acad Sci USA 54:193-199
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.E.2
  • 15
    • 0026681502 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum
    • Mathieu I, Meyer J, Moulis JM (1992) Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum. Biochem J 285:255-262
    • (1992) Biochem J , vol.285 , pp. 255-262
    • Mathieu, I.1    Meyer, J.2    Moulis, J.M.3
  • 16
    • 0015220756 scopus 로고
    • Properties of two clostridial flavodoxins
    • Mayhew SG (1971) Properties of two clostridial flavodoxins. Biochim Biophys Acta 235:276-288
    • (1971) Biochim Biophys Acta , vol.235 , pp. 276-288
    • Mayhew, S.G.1
  • 17
    • 0025162725 scopus 로고
    • Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data
    • Meyer J, Gagnon J, Sieker LC, Van Dorsselaer A, Moulis JM (1990) Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data. Biochem J 271:839-841
    • (1990) Biochem J , vol.271 , pp. 839-841
    • Meyer, J.1    Gagnon, J.2    Sieker, L.C.3    Van Dorsselaer, A.4    Moulis, J.M.5
  • 18
    • 0018622764 scopus 로고
    • Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum
    • Petitdemange H, Marczak R, Blusson H, Gay R (1979) Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum. Biochem Biophys Res Commun 91:1258-1265
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 1258-1265
    • Petitdemange, H.1    Marczak, R.2    Blusson, H.3    Gay, R.4
  • 19
    • 0029569167 scopus 로고
    • Fermentation of raw glycerol to 1,3 propanediol by new strains of Clostridium butyricum
    • Petitdemange E, Durr C, Abbad Andaloussi S, Raval G (1995) Fermentation of raw glycerol to 1,3 propanediol by new strains of Clostridium butyricum. J Ind Microbiol 15:498-502
    • (1995) J Ind Microbiol , vol.15 , pp. 498-502
    • Petitdemange, E.1    Durr, C.2    Abbad Andaloussi, S.3    Raval, G.4
  • 20
    • 0021079728 scopus 로고
    • Isolation of carbon monoxide dehydrogenase from Acetobacterium woodi and comparison of its properties with those of the Clostridium thermoaceticum enzyme
    • Ragsdale SW, Ljungdahl LG, DerVartanian DV (1983) Isolation of carbon monoxide dehydrogenase from Acetobacterium woodi and comparison of its properties with those of the Clostridium thermoaceticum enzyme. J Bacteriol 155:1224-1237
    • (1983) J Bacteriol , vol.155 , pp. 1224-1237
    • Ragsdale, S.W.1    Ljungdahl, L.G.2    DerVartanian, D.V.3
  • 21
    • 0024725593 scopus 로고
    • Purification and properties of ferredoxin and rubredoxin from Butyribacterium methylotrophicum
    • Saeki K, Jain MK, Shen GJ, Prince RC, Zeikus JG (1989a) Purification and properties of ferredoxin and rubredoxin from Butyribacterium methylotrophicum. J Bacteriol 171:4736-4741
    • (1989) J Bacteriol , vol.171 , pp. 4736-4741
    • Saeki, K.1    Jain, M.K.2    Shen, G.J.3    Prince, R.C.4    Zeikus, J.G.5
  • 22
    • 0024746545 scopus 로고
    • Ferredoxin and rubredoxin from Butyribacterium methylotrophicum: Complete primary structures and construction of phylogenetic trees
    • Saeki K, Yao Y, Wakabayashi S, Shen GJ, Zeikus JG, Matsubara H (1989b) Ferredoxin and rubredoxin from Butyribacterium methylotrophicum: complete primary structures and construction of phylogenetic trees. J Biochem 106:656-662
    • (1989) J Biochem , vol.106 , pp. 656-662
    • Saeki, K.1    Yao, Y.2    Wakabayashi, S.3    Shen, G.J.4    Zeikus, J.G.5    Matsubara, H.6
  • 23
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito H, Miura KI (1963) Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72:619-629
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.I.2
  • 25
    • 0023933393 scopus 로고
    • Rubredoxin as an intermediary electron carrier for nitrate reduction by NAD(P)H in Clostridium perfringens
    • Seki S, Ikeda A, Ishimoto M (1988) Rubredoxin as an intermediary electron carrier for nitrate reduction by NAD(P)H in Clostridium perfringens. J Biochem 103:583-584
    • (1988) J Biochem , vol.103 , pp. 583-584
    • Seki, S.1    Ikeda, A.2    Ishimoto, M.3
  • 26
    • 0024373795 scopus 로고
    • Rubredoxin from Clostridium perfringens: Complete amino acid sequence and participation in nitrate reduction
    • Seki Y, Seki S, Satoh M, Ikeda A, Ishimoto M (1989) Rubredoxin from Clostridium perfringens: complete amino acid sequence and participation in nitrate reduction. J Biochem 106:336-341
    • (1989) J Biochem , vol.106 , pp. 336-341
    • Seki, Y.1    Seki, S.2    Satoh, M.3    Ikeda, A.4    Ishimoto, M.5
  • 27
    • 0024817640 scopus 로고
    • Amino acid sequence and function of rubredoxin from Desulfovibrio vulgaris Miyazaki
    • Shimizu F, Ogata M, Yagi T, Wakabayashi S, Matsubara H (1989) Amino acid sequence and function of rubredoxin from Desulfovibrio vulgaris Miyazaki. Biochimie 71:1171-1177
    • (1989) Biochimie , vol.71 , pp. 1171-1177
    • Shimizu, F.1    Ogata, M.2    Yagi, T.3    Wakabayashi, S.4    Matsubara, H.5
  • 28
    • 0023802453 scopus 로고
    • Cloning of genes encoding redox proteins of known amino acid sequence from a library of the Desulfovibrio vulgaris (Hildenborough) genome
    • Voordouw G (1988) Cloning of genes encoding redox proteins of known amino acid sequence from a library of the Desulfovibrio vulgaris (Hildenborough) genome. Gene 69:75-83
    • (1988) Gene , vol.69 , pp. 75-83
    • Voordouw, G.1
  • 29
    • 0023143072 scopus 로고
    • The complete amino acid sequence of rubredoxin from the green phototrophic bacterium Chlorobium thiosulfatophilum strain PM
    • Woodley KJ, Meyer TE (1987) The complete amino acid sequence of rubredoxin from the green phototrophic bacterium Chlorobium thiosulfatophilum strain PM. Eur J Biochem 163:161-166
    • (1987) Eur J Biochem , vol.163 , pp. 161-166
    • Woodley, K.J.1    Meyer, T.E.2
  • 30
    • 0002603862 scopus 로고
    • The types, distribution in nature, structure, and evolution data of the iron-sulfur proteins
    • Lovenberg W (eds) New York: Academic Press
    • Yasunobu KT, Tanaka M (1973) The types, distribution in nature, structure, and evolution data of the iron-sulfur proteins. In: Lovenberg W (eds) Iron sulfur proteins, vol. 2. New York: Academic Press, pp 27-130
    • (1973) Iron Sulfur Proteins , vol.2 , pp. 27-130
    • Yasunobu, K.T.1    Tanaka, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.