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Volumn 179, Issue 19, 1997, Pages 6053-6060

Purification and molecular characterization of the H2 uptake membrane- bound NiFe-hydrogenase from the carboxidotrophic bacterium Oligotropha carboxidovorans

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HYDROGENASE; IRON; METHYLENE BLUE; NICKEL; PYRIDINE NUCLEOTIDE;

EID: 0030929424     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.19.6053-6060.1997     Document Type: Article
Times cited : (19)

References (46)
  • 4
    • 84942490613 scopus 로고
    • Diphosphofructose-Aldolase, Phosphoglycerinaldehyd-Dehydrogenase, Milchsäure-Dehydrogenase, Glycerophosphat-Dehydrogenase und Pyruvat-Kinase aus Kaninchenmuskel in einem Arbeitsgang
    • Beisenherz, G., H. G. Bolze, T. Bücher, R. Czok, K. H. Garbade, E. Meyer-Arendt, and G. Pfleiderer. 1953. Diphosphofructose-Aldolase, Phosphoglycerinaldehyd-Dehydrogenase, Milchsäure-Dehydrogenase, Glycerophosphat-Dehydrogenase und Pyruvat-Kinase aus Kaninchenmuskel in einem Arbeitsgang. Z. Naturforsch. 8B:555-557.
    • (1953) Z. Naturforsch. , vol.8 B , pp. 555-557
    • Beisenherz, G.1    Bolze, H.G.2    Bücher, T.3    Czok, R.4    Garbade, K.H.5    Meyer-Arendt, E.6    Pfleiderer, G.7
  • 5
    • 0028007441 scopus 로고
    • Sequences and characterization of hupU and hupV genes of Bradyrhizobium japonicum encoding a possible nickel-sensing complex involved in hydrogenase expression
    • Black, L. K., C. Fu, and R. J. Maier. 1994. Sequences and characterization of hupU and hupV genes of Bradyrhizobium japonicum encoding a possible nickel-sensing complex involved in hydrogenase expression. J. Bacteriol. 176:7102-7106.
    • (1994) J. Bacteriol. , vol.176 , pp. 7102-7106
    • Black, L.K.1    Fu, C.2    Maier, R.J.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0026050629 scopus 로고
    • The hydrogenase structural operon in Rhodobacter capsulatus contains a third gene, hupM, necessary for the formation of a physiologically competent hydrogenase
    • Cauvin, B., A. Colbeau, and P. M. Vignais. 1991. The hydrogenase structural operon in Rhodobacter capsulatus contains a third gene, hupM, necessary for the formation of a physiologically competent hydrogenase. Mol. Microbiol. 5:2519-2527.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2519-2527
    • Cauvin, B.1    Colbeau, A.2    Vignais, P.M.3
  • 8
    • 0019191594 scopus 로고
    • Physiological characteristics of various species of strain of carboxydobacteria
    • Cypionka, H., O. Meyer, and H. G. Schlegel. 1980. Physiological characteristics of various species of strain of carboxydobacteria. Arch. Microbiol. 127:301-307.
    • (1980) Arch. Microbiol. , vol.127 , pp. 301-307
    • Cypionka, H.1    Meyer, O.2    Schlegel, H.G.3
  • 10
    • 0029812909 scopus 로고    scopus 로고
    • The hupTUV operon is involved in negative control of hydrogenase synthesis in Rhodobacter capsulatus
    • Elsen, S., A. Colbeau, J. Chabert, and P. M. Vignais. 1996. The hupTUV operon is involved in negative control of hydrogenase synthesis in Rhodobacter capsulatus. J. Bacteriol. 178:5174-5181.
    • (1996) J. Bacteriol. , vol.178 , pp. 5174-5181
    • Elsen, S.1    Colbeau, A.2    Chabert, J.3    Vignais, P.M.4
  • 11
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 12
    • 33947457186 scopus 로고
    • Spectrophotometric determination of hydrogen sulfide
    • Fogo, J. K., and M. Popowsky. 1949. Spectrophotometric determination of hydrogen sulfide. Anal. Chem. 21:732-734.
    • (1949) Anal. Chem. , vol.21 , pp. 732-734
    • Fogo, J.K.1    Popowsky, M.2
  • 13
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
    • Fox, J. C., R. L. Kerby, G. P. Roberts, and P. W. Ludden. 1996. Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178:1515-1524.
    • (1996) J. Bacteriol. , vol.178 , pp. 1515-1524
    • Fox, J.C.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 14
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox, J. D., Y. He, D. Shelver, G. P. Roberts, and P. W. Ludden. 1996. Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178:6200-6208.
    • (1996) J. Bacteriol. , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 15
    • 0025180835 scopus 로고
    • Searching for and predicting the activity sites for DNA binding proteins: Compilation and analysis of the binding sites for Escherichia coli integration host factor (IHF)
    • Goodrich, J. A., M. L. Schwartz, and W. R. McClure. 1990. Searching for and predicting the activity sites for DNA binding proteins: compilation and analysis of the binding sites for Escherichia coli integration host factor (IHF). Nucleic Acids Res. 18:4993-5000.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4993-5000
    • Goodrich, J.A.1    Schwartz, M.L.2    McClure, W.R.3
  • 16
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff, S. 1984. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28:351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 17
    • 0025475251 scopus 로고
    • Nucleotide sequence of the hydrogenase structural genes from Rhizobium leguminosarum
    • Hidalgo, E., A. Leyva, and T. Ruiz-Argüeso. 1990. Nucleotide sequence of the hydrogenase structural genes from Rhizobium leguminosarum. Plant Mol. Biol. 15:367-370.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 367-370
    • Hidalgo, E.1    Leyva, A.2    Ruiz-Argüeso, T.3
  • 18
    • 0026628893 scopus 로고
    • Nucleotide sequence and characterization of four additional genes of the hydrogenase structural operon from Rhizobium leguminosarum bv. viciae
    • Hidalgo, E., J. M. Palacios, J. Murillo, and T. Ruiz-Argüeso. 1992. Nucleotide sequence and characterization of four additional genes of the hydrogenase structural operon from Rhizobium leguminosarum bv. viciae. J. Bacteriol. 174:4130-4139.
    • (1992) J. Bacteriol. , vol.174 , pp. 4130-4139
    • Hidalgo, E.1    Palacios, J.M.2    Murillo, J.3    Ruiz-Argüeso, T.4
  • 19
    • 0026043149 scopus 로고
    • Genes encoding ribulosebisphosphate carboxylase and phosphoribulokinase are duplicated in Pseudomonas carboxydovorans and conserved in carboxidotrophic bacteria
    • Hugendieck, I., and O. Meyer. 1991. Genes encoding ribulosebisphosphate carboxylase and phosphoribulokinase are duplicated in Pseudomonas carboxydovorans and conserved in carboxidotrophic bacteria. Arch. Microbiol. 157:92-96.
    • (1991) Arch. Microbiol. , vol.157 , pp. 92-96
    • Hugendieck, I.1    Meyer, O.2
  • 21
    • 0002768724 scopus 로고
    • 6 transformants/μg
    • 6 transformants/μg. Focus 8:9-10.
    • (1988) Focus , vol.8 , pp. 9-10
    • Jessee, J.1
  • 22
    • 0006392352 scopus 로고
    • Genes of lithoautotrophic metabolism are clustered on the megaplasmid pHG1 in Alcaligenes eutrophus
    • Kortlücke, C. H., C. Hogrefe, G. Eberz, A. Pühler, and B. Friedrich. 1987. Genes of lithoautotrophic metabolism are clustered on the megaplasmid pHG1 in Alcaligenes eutrophus. Mol. Gen. Genet. 210:122-128.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 122-128
    • Kortlücke, C.H.1    Hogrefe, C.2    Eberz, G.3    Pühler, A.4    Friedrich, B.5
  • 24
    • 0007715843 scopus 로고
    • Plasmids in carboxydotrophic bacteria: Physical and restriction analysis
    • Kraut, M., and O. Meyer. 1988. Plasmids in carboxydotrophic bacteria: physical and restriction analysis. Arch. Microbiol. 149:540-546.
    • (1988) Arch. Microbiol. , vol.149 , pp. 540-546
    • Kraut, M.1    Meyer, O.2
  • 25
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 26
    • 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 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucJcic acid from microorganisms
    • Marmur, J. 1961. A procedure for the isolation of deoxyribonucJcic acid from microorganisms. J. Mol. Biol. 3:208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 28
    • 0026703940 scopus 로고
    • Nucleotide sequences and genetic analysis of hydrogen oxidation (hox) genes in Azotobacter vinelandii
    • Menon, A. L., L. E. Mortenson, and R. L. Robson. 1992. Nucleotide sequences and genetic analysis of hydrogen oxidation (hox) genes in Azotobacter vinelandii. J. Bacteriol. 174:4549-4557.
    • (1992) J. Bacteriol. , vol.174 , pp. 4549-4557
    • Menon, A.L.1    Mortenson, L.E.2    Robson, R.L.3
  • 29
    • 0025614729 scopus 로고
    • Cloning, sequencing and characterization of the [NiFe] hydrogenase-encoding structural genes of Azotobacter vinelandii
    • Menon, A. L., L. W. Stults, R. L. Robson, and L. E. Mortenson. 1990. Cloning, sequencing and characterization of the [NiFe] hydrogenase-encoding structural genes of Azotobacter vinelandii. Gene 96:67-74.
    • (1990) Gene , vol.96 , pp. 67-74
    • Menon, A.L.1    Stults, L.W.2    Robson, R.L.3    Mortenson, L.E.4
  • 31
    • 0002798821 scopus 로고
    • Biochemistry of aerobic utilization of carbon monoxide
    • J. C. Murrel and D. P. Kelly (ed.), Intercept, Ltd., Andover, Mass.
    • 1 compounds. Intercept, Ltd., Andover, Mass.
    • (1993) 1 Compounds , pp. 433-459
    • Meyer, O.1    Frunzke, K.2    Mörsdort, G.3
  • 32
    • 0017806087 scopus 로고
    • Reisolation of the carbon monoxide utilizing hydrogen bacterium Pseudomonas carboxydovorans (Kistner) comb. nov
    • Meyer, O., and H. G. Schlegel. 1978. Reisolation of the carbon monoxide utilizing hydrogen bacterium Pseudomonas carboxydovorans (Kistner) comb. nov. Arch. Microbiol. 118:35-43.
    • (1978) Arch. Microbiol. , vol.118 , pp. 35-43
    • Meyer, O.1    Schlegel, H.G.2
  • 33
    • 0018343530 scopus 로고
    • Oxidation of CO in cell extracts of Pseudomonas carboxydovorans
    • Meyer, O., and H. G. Schlegel. 1979. Oxidation of CO in cell extracts of Pseudomonas carboxydovorans. J. Bacteriol. 137:811-817.
    • (1979) J. Bacteriol. , vol.137 , pp. 811-817
    • Meyer, O.1    Schlegel, H.G.2
  • 34
    • 0020653833 scopus 로고
    • Biology of aerobic carbon monoxide oxidizing bacteria
    • Meyer, O., and H. G. Sthlegel. 1983. Biology of aerobic carbon monoxide oxidizing bacteria. Annu. Rev. Microbiol. 37:277-310.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 277-310
    • Meyer, O.1    Sthlegel, H.G.2
  • 35
    • 0027142846 scopus 로고
    • T to Corbophilus, gen. nov., as Carbophilus carboxidus, comb. nov., transfer of "[Pseudomonas] compransoris"
    • T to Zarvazinia, gen. nov., as Zarvazinia compransoris, comb. nov., and amended descriptions of the new genera
    • T to Zarvazinia, gen. nov., as Zarvazinia compransoris, comb. nov., and amended descriptions of the new genera. Syst. Appl. Microbiol. 16:390-395.
    • (1993) Syst. Appl. Microbiol. , vol.16 , pp. 390-395
    • Meyer, O.1    Stackebrandt, E.2    Auling, G.3
  • 37
    • 0026646678 scopus 로고
    • Site directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a β-lactamase fusion protein
    • Nivière, V., S. L. Wong, and G. Voordouw. 1992. Site directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a β-lactamase fusion protein. J. Gen. Microbiol. 138:2173-2183.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2173-2183
    • Nivière, V.1    Wong, S.L.2    Voordouw, G.3
  • 38
    • 0028603529 scopus 로고
    • DNA sequence of the cut A, B, and C genes, encoding the molybdenum containing hydroxylase carbon monoxide dehydrogenase, from Pseudomonas thermocarboxydovorans strain C2
    • Pearson, D., C. O'Reilly, J. Colby, and G. W. Black. 1994. DNA sequence of the cut A, B, and C genes, encoding the molybdenum containing hydroxylase carbon monoxide dehydrogenase, from Pseudomonas thermocarboxydovorans strain C2. Biochim. Biophys. Acta 1188:432-438.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 432-438
    • Pearson, D.1    O'Reilly, C.2    Colby, J.3    Black, G.W.4
  • 39
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of Escherichia colt hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
    • Rossmann, R., M. Sauter, F. Lottspeich, and A. Böck. 1994. Maturation of the large subunit (HYCE) of Escherichia colt hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537. Eur. J. Biochem. 220:377-384.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Böck, A.4
  • 41
    • 0028968003 scopus 로고
    • Molecular characterization of the gene cluster coxMSL encoding the molybdenum containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans
    • Schübel, U., M. Kraut, G. Mörsdorf, and O. Meyer. 1995. Molecular characterization of the gene cluster coxMSL encoding the molybdenum containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans. J. Bacteriol. 177:2197-2203.
    • (1995) J. Bacteriol. , vol.177 , pp. 2197-2203
    • Schübel, U.1    Kraut, M.2    Mörsdorf, G.3    Meyer, O.4
  • 44
    • 0000003202 scopus 로고
    • Evolution of hydrogenase genes
    • Voordouw, G. 1992. Evolution of hydrogenase genes. Adv. Inorg. Chem. 38:397-422.
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 397-422
    • Voordouw, G.1
  • 45
    • 0027167618 scopus 로고
    • Microbial hydrogenases: Primary structure, classification, signatures and phylogeny
    • Wu, L. F., and W. A. Mandrand. 1993. Microbial hydrogenases: primary structure, classification, signatures and phylogeny. FEMS Microbiol. Rev. 104:243-270.
    • (1993) FEMS Microbiol. Rev. , vol.104 , pp. 243-270
    • Wu, L.F.1    Mandrand, W.A.2
  • 46
    • 0028850433 scopus 로고
    • Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen. nov.: Proposal of Ralstonia picketii (Ralston, Palleroni and Doudoroff 1973) comb, nov., Ralstonia solanacearum (Smith 1896) comb. nov. and Ralstonia eutropha (Davis 1969) com. nov
    • Yabucchi, E., Y. Kosako, I. Yano, H. Hotta, and Y. Nishiuchi. 1995. Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen. nov.: proposal of Ralstonia picketii (Ralston, Palleroni and Doudoroff 1973) comb, nov., Ralstonia solanacearum (Smith 1896) comb. nov. and Ralstonia eutropha (Davis 1969) com. nov. Microbiol. Immunol. 39:897-904.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 897-904
    • Yabucchi, E.1    Kosako, Y.2    Yano, I.3    Hotta, H.4    Nishiuchi, Y.5


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