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Volumn 181, Issue 16, 1999, Pages 4919-4928

A megaplasmid-borne anaerobic ribonucleotide reductase in Alcaligenes eutrophus H16

Author keywords

[No Author keywords available]

Indexed keywords

NITRATE; RIBONUCLEOTIDE REDUCTASE;

EID: 0032817064     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.16.4919-4928.1999     Document Type: Article
Times cited : (12)

References (63)
  • 2
    • 0028172124 scopus 로고
    • Coenzyme B12-dependent ribonucleotide reductase: Evidence for the participation of five cystein residues in ribonucleotide reduction
    • Booker, S., S. Licht, J. Broderick, and J. Stubbe. 1994. Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cystein residues in ribonucleotide reduction. Biochemistry 33:12676-12685.
    • (1994) Biochemistry , vol.33 , pp. 12676-12685
    • Booker, S.1    Licht, S.2    Broderick, J.3    Stubbe, J.4
  • 4
    • 0026236530 scopus 로고
    • Expression of nrdA and nrdB genes of Escherichia coli is decreased under anaerobiosis
    • Casado, C., M. Llagostera, and J. Barbé. 1991. Expression of nrdA and nrdB genes of Escherichia coli is decreased under anaerobiosis. FEMS Microbiol. Lett. 67:153-157.
    • (1991) FEMS Microbiol. Lett. , vol.67 , pp. 153-157
    • Casado, C.1    Llagostera, M.2    Barbé, J.3
  • 5
    • 0030714062 scopus 로고    scopus 로고
    • Two isofunctional nitric oxide reductases in Alcaligenes eutrophus H16
    • Cramm, R., R. A. Siddiqui, and B. Friedrich. 1997. Two isofunctional nitric oxide reductases in Alcaligenes eutrophus H16. J. Bacteriol. 179:6769-6777.
    • (1997) J. Bacteriol. , vol.179 , pp. 6769-6777
    • Cramm, R.1    Siddiqui, R.A.2    Friedrich, B.3
  • 6
    • 0023261241 scopus 로고
    • A set of cassettes and improved vectors for genetic and biochemical characterization of Pseudomonas genes
    • Deretic, V., S. Chandrasekharappa, J. F. Gill, D. K. Chatterjee, and A. M. Chachrabarty. 1987. A set of cassettes and improved vectors for genetic and biochemical characterization of Pseudomonas genes. Gene 57:61-72.
    • (1987) Gene , vol.57 , pp. 61-72
    • Deretic, V.1    Chandrasekharappa, S.2    Gill, J.F.3    Chatterjee, D.K.4    Chachrabarty, A.M.5
  • 7
    • 0015501033 scopus 로고
    • Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase
    • Ehrenberg, A., and P. Reichard. 1972. Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase. J. Biol. Chem. 247: 3485-3488.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3485-3488
    • Ehrenberg, A.1    Reichard, P.2
  • 9
    • 0029093215 scopus 로고
    • The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy
    • Eliasson, R., P. Reichard, E. Mulliez, S. Ollagnier, M. Fontecave, E. Liepinsh, and G. Otting. 1995. The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy. Biochem. Biophys. Res. Commun. 214:28-35.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 28-35
    • Eliasson, R.1    Reichard, P.2    Mulliez, E.3    Ollagnier, S.4    Fontecave, M.5    Liepinsh, E.6    Otting, G.7
  • 11
    • 0000087813 scopus 로고
    • Oxygen-sensitive ribonucleoside triphosphate reductase is present in anaerobic Escherichia coli
    • Fontecave, M., R. Eliasson, and P. Reichard. 1989. Oxygen-sensitive ribonucleoside triphosphate reductase is present in anaerobic Escherichia coli. Proc. Natl. Acad. Sci. USA 86:2147-2151.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2147-2151
    • Fontecave, M.1    Eliasson, R.2    Reichard, P.3
  • 13
    • 0027382485 scopus 로고
    • Molecular biology of hydrogen utilization in aerobic chemolithotrophs
    • Friedrich, B., and E. Schwartz. 1993. Molecular biology of hydrogen utilization in aerobic chemolithotrophs. Annu. Rev. Microbiol. 47:351-383.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 351-383
    • Friedrich, B.1    Schwartz, E.2
  • 15
    • 0027491211 scopus 로고
    • Ribonucleotide reductases and their occurrence in microorganisms: A link to RNA/DNA transition
    • Harder, J. 1993. Ribonucleotide reductases and their occurrence in microorganisms: a link to RNA/DNA transition. FEMS Microbiol. Rev. 12:273-292.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 273-292
    • Harder, J.1
  • 16
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 17
    • 0345239949 scopus 로고
    • Ribonucleotide reductase in cell extracts of Methanobacterium thermoautotrophicum
    • Hogenkamp, H. P. C., H. Follmann, and R. K. Thauer. 1987. Ribonucleotide reductase in cell extracts of Methanobacterium thermoautotrophicum. FEBS Lett. 219:197-201.
    • (1987) FEBS Lett. , vol.219 , pp. 197-201
    • Hogenkamp, H.P.C.1    Follmann, H.2    Thauer, R.K.3
  • 18
    • 0025727991 scopus 로고
    • Expression of regulatory nif genes in Rhodobacter capsulatus
    • Hübner, P., J. C. Willison, P. M. Vignais, and T. Blickle. 1991. Expression of regulatory nif genes in Rhodobacter capsulatus. J. Bacteriol. 173:2993-2999.
    • (1991) J. Bacteriol. , vol.173 , pp. 2993-2999
    • Hübner, P.1    Willison, J.C.2    Vignais, P.M.3    Blickle, T.4
  • 23
    • 0025063286 scopus 로고
    • A radical-chemical route to acetyl-CoA: The anaerobically induced pyruvate formate-lyase system of Escherichia coli
    • Knappe, J., and G. Sawers. 1990. A radical-chemical route to acetyl-CoA: the anaerobically induced pyruvate formate-lyase system of Escherichia coli. FEMS Microbiol. Rev. 75:383-398.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 383-398
    • Knappe, J.1    Sawers, G.2
  • 24
    • 0026738084 scopus 로고
    • Maturation of membrane-bound hydrogenase of Alcaligenes eutrophus H16
    • Kortlüke, C., and B. Friedrich. 1992. Maturation of membrane-bound hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol. 174:6290-6293.
    • (1992) J. Bacteriol. , vol.174 , pp. 6290-6293
    • Kortlüke, C.1    Friedrich, B.2
  • 25
    • 0026700702 scopus 로고
    • A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16
    • Kortlüke, C., K. Horstmann, E. Schwartz, M. Rhode, R. Binsack, and B. Friedrich. 1992. A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol. 174:6277-6289.
    • (1992) J. Bacteriol. , vol.174 , pp. 6277-6289
    • Kortlüke, C.1    Horstmann, K.2    Schwartz, E.3    Rhode, M.4    Binsack, R.5    Friedrich, B.6
  • 26
    • 0028228427 scopus 로고
    • The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation
    • Lenz, O., E. Schwartz, J. Dernedde, M. Eitinger, and B. Friedrich. 1994. The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation. J. Bacteriol. 176:4385-4393.
    • (1994) J. Bacteriol. , vol.176 , pp. 4385-4393
    • Lenz, O.1    Schwartz, E.2    Dernedde, J.3    Eitinger, M.4    Friedrich, B.5
  • 27
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • Licht, S., G. J. Gerfen, and J. Stubbe. 1996. Thiyl radicals in ribonucleotide reductases. Science 271:477-481.
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 28
    • 0028168338 scopus 로고
    • Dioxygen is the source of the μ-oxo brige in iron ribonucleotide reductase
    • Ling, J. S., M. Sahlin, B.-M. Sjöberg, T. M. Loehr, and J. Sanders-Loehr. 1994. Dioxygen is the source of the μ-oxo brige in iron ribonucleotide reductase. J. Biol. Chem. 269:5595-5601.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5595-5601
    • Ling, J.S.1    Sahlin, M.2    Sjöberg, B.-M.3    Loehr, T.M.4    Sanders-Loehr, J.5
  • 29
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • Logan, D. T., J. Andersson, B.-M. Sjöberg, and P. Nordlund. 1999. A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. Science 283:1499-1504.
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.T.1    Andersson, J.2    Sjöberg, B.-M.3    Nordlund, P.4
  • 31
    • 0026801085 scopus 로고
    • A model for the role of multiple cysteine residues involved in ribonucleotide reduction-amazing and still confusing
    • Mao, S. S., T. P. Holler, G. X. Yu, J. M. Bollinger, S. Booker, M. I. Johnston, and J. Stubbe. 1992. A model for the role of multiple cysteine residues involved in ribonucleotide reduction-amazing and still confusing. Biochemistry 31:9733-9743.
    • (1992) Biochemistry , vol.31 , pp. 9733-9743
    • Mao, S.S.1    Holler, T.P.2    Yu, G.X.3    Bollinger, J.M.4    Booker, S.5    Johnston, M.I.6    Stubbe, J.7
  • 32
    • 0028982741 scopus 로고
    • A pAO1-encoded molybdopterin cofactor gene (moa4) of Arthrobacter nicotinovorans: Characterisation and site-directed mutagenesis of the encoded protein
    • Menéndez, C., G. Iglio, H. Henninger, and R. Brandsch. 1995. A pAO1-encoded molybdopterin cofactor gene (moa4) of Arthrobacter nicotinovorans: characterisation and site-directed mutagenesis of the encoded protein. Arch. Microbiol. 164:142-151.
    • (1995) Arch. Microbiol. , vol.164 , pp. 142-151
    • Menéndez, C.1    Iglio, G.2    Henninger, H.3    Brandsch, R.4
  • 33
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics, p. 352-355. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 36
    • 0032894598 scopus 로고    scopus 로고
    • InBase, the New England Biolabs Intein Database
    • Perier, F. B. 1999. InBase, the New England Biolabs Intein Database. Nucleic Acids Res. 27:346-347.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 346-347
    • Perier, F.B.1
  • 39
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard, P. 1993. From RNA to DNA, why so many ribonucleotide reductases? Science 260:1773-1777.
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 40
    • 0031106730 scopus 로고    scopus 로고
    • The evolution of ribonucleotide reduction
    • Reichard, P. 1997. The evolution of ribonucleotide reduction. Trends Biochem. Sci. 22:81-85.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 81-85
    • Reichard, P.1
  • 41
    • 0021806598 scopus 로고
    • Dentrification by Alcaligenes eutrophus is plasmid dependent
    • Römermann, D., and B. Friedrich. 1985. Dentrification by Alcaligenes eutrophus is plasmid dependent. J. Bacteriol. 162:852-854.
    • (1985) J. Bacteriol. , vol.162 , pp. 852-854
    • Römermann, D.1    Friedrich, B.2
  • 43
    • 0025373543 scopus 로고
    • Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli
    • Sauter, M., and R. G. Sawers. 1990. Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli. Mol. Microbiol. 4:355-363.
    • (1990) Mol. Microbiol. , vol.4 , pp. 355-363
    • Sauter, M.1    Sawers, R.G.2
  • 44
    • 34250969714 scopus 로고
    • Ein Submersverfahren zur kultur wasserstoffoxidierender bakterien: Wachstumsphysiologische untersuchungen
    • Schlegel, H. G., H. Kaltwasser, and G. Gottschalk. 1961. Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: wachstumsphysiologische Untersuchungen. Arch. Microbiol. 38:209-222.
    • (1961) Arch. Microbiol. , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 45
    • 0342966964 scopus 로고
    • Transfer and expression of lithoautotrophy and denitrification in a host lacking these metabolic activities
    • Schneider, B., A. Nies, and B. Friedrich. 1988. Transfer and expression of lithoautotrophy and denitrification in a host lacking these metabolic activities. Appl. Env. Microbiol. 54:3173-3176.
    • (1988) Appl. Env. Microbiol. , vol.54 , pp. 3173-3176
    • Schneider, B.1    Nies, A.2    Friedrich, B.3
  • 46
    • 0031747821 scopus 로고    scopus 로고
    • Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes
    • Schwartz, E., U. Gerischer, and B. Friedrich. 1998. Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes. J. Bacteriol. 180:3197-3204.
    • (1998) J. Bacteriol. , vol.180 , pp. 3197-3204
    • Schwartz, E.1    Gerischer, U.2    Friedrich, B.3
  • 48
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 49
    • 0002243030 scopus 로고
    • Structure of ribonucleotide reductase from Escherichia coli
    • F. Eckstein and D. M. F. Lilley (ed.), Springer-Verlag, Heidelberg, Germany
    • Sjöberg, B.-M. 1995. Structure of ribonucleotide reductase from Escherichia coli, p. 192-221. In F. Eckstein and D. M. F. Lilley (ed.), Nucleic acids and molecular biology. Springer-Verlag, Heidelberg, Germany.
    • (1995) Nucleic Acids and Molecular Biology , pp. 192-221
    • Sjöberg, B.-M.1
  • 51
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spiro, S., and J. Guest. 1990. FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev. 75:399-428.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 399-428
    • Spiro, S.1    Guest, J.2
  • 52
    • 0028837286 scopus 로고
    • Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme
    • Sun, X., R. Eliasson, E. Pontis, J. Andersson, G. Buist, B.-M. Sjöberg, and P. Reichard. 1995. Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme. J. Biol. Chem. 270:2443-2446.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2443-2446
    • Sun, X.1    Eliasson, R.2    Pontis, E.3    Andersson, J.4    Buist, G.5    Sjöberg, B.-M.6    Reichard, P.7
  • 53
    • 0027388888 scopus 로고
    • A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: Nucleotide sequence of the cloned nrdD gene
    • Sun, X., J. Harder, M. Krock, H. Jörnvall, B.-M. Sjöberg, and P. Reichard. 1993. A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene. Proc. Natl. Acad. Sci. USA 90:577-581.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 577-581
    • Sun, X.1    Harder, J.2    Krock, M.3    Jörnvall, H.4    Sjöberg, B.-M.5    Reichard, P.6
  • 55
    • 0015911796 scopus 로고
    • Direct spectrophotometric observation of an intermediate formed from deoxyadenosylcobalamin in ribonucleotide reduction
    • Tamao, Y., and R. L. Blakley. 1973. Direct spectrophotometric observation of an intermediate formed from deoxyadenosylcobalamin in ribonucleotide reduction. Biochemistry 12:24-34.
    • (1973) Biochemistry , vol.12 , pp. 24-34
    • Tamao, Y.1    Blakley, R.L.2
  • 56
    • 0023663372 scopus 로고
    • Nucleotide sequence and primary structures of gene products coded for by the T4 genome between map positions 48.266 kb and 39.166 kb
    • Tomaschewski, J., and W. Roger. 1987. Nucleotide sequence and primary structures of gene products coded for by the T4 genome between map positions 48.266 kb and 39.166 kb. Nucleic Acids Res. 15:3632-3633.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3632-3633
    • Tomaschewski, J.1    Roger, W.2
  • 57
    • 0031049495 scopus 로고    scopus 로고
    • Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate
    • Toyama, H., L. Chistoserdova, and M. E. Lidstrom. 1997. Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate. Microbiology 143:595-602.
    • (1997) Microbiology , vol.143 , pp. 595-602
    • Toyama, H.1    Chistoserdova, L.2    Lidstrom, M.E.3
  • 58
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U., and H. Eklund. 1994. Structure of ribonucleotide reductase protein R1. Nature 370:533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 59
    • 0027450107 scopus 로고
    • Three nitrate reductase activities in Alcaligenes eutrophus
    • Warnecke-Eberz, U., and B. Friedrich. 1992. Three nitrate reductase activities in Alcaligenes eutrophus. Arch. Microbiol. 159:405-409.
    • (1992) Arch. Microbiol. , vol.159 , pp. 405-409
    • Warnecke-Eberz, U.1    Friedrich, B.2
  • 60
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 61
    • 0028104402 scopus 로고
    • Bacteriophage T4 gene 55.9 encodes an activity required for anaerobic ribonucleotide reduction
    • Young, P., M. Öhmann, and B.-M. Sjöberg. 1994. Bacteriophage T4 gene 55.9 encodes an activity required for anaerobic ribonucleotide reduction. J. Biol. Chem. 269:27815-27818.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27815-27818
    • Young, P.1    Öhmann, M.2    Sjöberg, B.-M.3
  • 62
    • 0028050514 scopus 로고
    • Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase
    • Young, P., M. Öhmann, M. Q. Xu, D. A. Shub, and B.-M. Sjöberg. 1994. Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase. J. Biol. Chem. 269:20229-20232.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20229-20232
    • Young, P.1    Öhmann, M.2    Xu, M.Q.3    Shub, D.A.4    Sjöberg, B.-M.5


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