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Volumn 179, Issue 7, 1997, Pages 2259-2266

In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: Molecular and physiological characterization of cooCTJ

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE DEHYDROGENASE; NICKEL;

EID: 0030944159     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.7.2259-2266.1997     Document Type: Article
Times cited : (106)

References (61)
  • 1
    • 0027505027 scopus 로고
    • Dinitrogenase reductase and MgATP-dependent maturation of apodinitrogenase from Azotobacter vinelandii
    • Allen, R. M., M. J. Homer, R. Chatterjee, P. W. Ludden, G. P. Roberts, and V. K. Shah. 1993. Dinitrogenase reductase and MgATP-dependent maturation of apodinitrogenase from Azotobacter vinelandii. J. Biol. Chem. 268:23670-23674.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23670-23674
    • Allen, R.M.1    Homer, M.J.2    Chatterjee, R.3    Ludden, P.W.4    Roberts, G.P.5    Shah, V.K.6
  • 3
    • 0024347769 scopus 로고
    • Regulation of carbon monoxide dehydrogenase and hydrogenase in Rhodospiritlum rubrum: Effects of CO and oxygen on synthesis and activity
    • Bonam, D., L. Lehman, G. P. Roberts, and P. W. Ludden. 1989. Regulation of carbon monoxide dehydrogenase and hydrogenase in Rhodospiritlum rubrum: effects of CO and oxygen on synthesis and activity. J. Bacteriol. 171:3102-3107.
    • (1989) J. Bacteriol. , vol.171 , pp. 3102-3107
    • Bonam, D.1    Lehman, L.2    Roberts, G.P.3    Ludden, P.W.4
  • 4
    • 0023644648 scopus 로고
    • Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum
    • Bonam, D., and P. W. Ludden. 1987. Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum. J. Biol. Chem. 262:2980-2987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2980-2987
    • Bonam, D.1    Ludden, P.W.2
  • 5
    • 0023703931 scopus 로고
    • Nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: In vivo and in vitro activation by exogenous nickel
    • Bonam, D., M. C. McKenna, P. J. Stephens, and P. W. Ludden. 1988. Nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: in vivo and in vitro activation by exogenous nickel. Proc. Natl. Acad. Sci. USA 85:31-35.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 31-35
    • Bonam, D.1    McKenna, M.C.2    Stephens, P.J.3    Ludden, P.W.4
  • 6
    • 0029812727 scopus 로고    scopus 로고
    • Purification, characterization, and functional analysis of a truncated Klebsiella aerogenes UreE urease accessory protein lacking the histidine-rich carboxyl terminus
    • Brayman, T. G., and R. P. Hausinger. 1996. Purification, characterization, and functional analysis of a truncated Klebsiella aerogenes UreE urease accessory protein lacking the histidine-rich carboxyl terminus. J. Bacteriol. 178:5410-5416.
    • (1996) J. Bacteriol. , vol.178 , pp. 5410-5416
    • Brayman, T.G.1    Hausinger, R.P.2
  • 7
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult, C. J., et al. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 8
    • 0029050025 scopus 로고
    • Analysis of a gene region required for dihydrogen oxidation in Azotobacter vinelandii
    • Chen, J. C., L. E. Mortenson, and L. C. Seefeldt. 1995. Analysis of a gene region required for dihydrogen oxidation in Azotobacter vinelandii. Curr. Microbiol. 30:351-355.
    • (1995) Curr. Microbiol. , vol.30 , pp. 351-355
    • Chen, J.C.1    Mortenson, L.E.2    Seefeldt, L.C.3
  • 9
    • 15444357950 scopus 로고
    • M.S. thesis. University of Wisconsin, Madison
    • MURBURMmEB9. Coppoc, L. J. 1991. M.S. thesis. University of Wisconsin, Madison.
    • (1991)
    • Coppoc, L.J.1
  • 10
    • 0026723973 scopus 로고
    • Expression of Helicobacter pylori urease genes in Escherichia coli grown under nitrogen-limiting conditions
    • Cussac, V., R. L. Ferrero, and A. Labigne. 1992. Expression of Helicobacter pylori urease genes in Escherichia coli grown under nitrogen-limiting conditions. J. Bacteriol. 174:2466-2473.
    • (1992) J. Bacteriol. , vol.174 , pp. 2466-2473
    • Cussac, V.1    Ferrero, R.L.2    Labigne, A.3
  • 11
    • 0029671234 scopus 로고    scopus 로고
    • Hyp gene products in Alcaligenes eutrophus are part of a hydrogenase-maturation system
    • Dernedde, J., T. Eitinger, N. Patenge, and B. Friedrich. 1996. hyp gene products in Alcaligenes eutrophus are part of a hydrogenase-maturation system. Eur. J. Biochem. 235:351-358.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 351-358
    • Dernedde, J.1    Eitinger, T.2    Patenge, N.3    Friedrich, B.4
  • 12
    • 0028127867 scopus 로고
    • The hupB gene of the Azotobacter chroococcum hydrogenase gene cluster is involved in nickel metabolism
    • Du, L., and K. H. Tibelius. 1994. The hupB gene of the Azotobacter chroococcum hydrogenase gene cluster is involved in nickel metabolism. Curr. Microiol. 28:21-24.
    • (1994) Curr. Microiol. , vol.28 , pp. 21-24
    • Du, L.1    Tibelius, K.H.2
  • 13
    • 0025255324 scopus 로고
    • Activation of the nickel-deficient carbon monoxide dehydrogenas from Rhodospirillum rubrum: Kinetic characterization and reductant requirement
    • Ensign, S. A., M. J. Campbell, and P. W. Ludden. 1990. Activation of the nickel-deficient carbon monoxide dehydrogenas from Rhodospirillum rubrum: kinetic characterization and reductant requirement. Biochemistry 29:2162-2168.
    • (1990) Biochemistry , vol.29 , pp. 2162-2168
    • Ensign, S.A.1    Campbell, M.J.2    Ludden, P.W.3
  • 14
    • 0025954526 scopus 로고
    • 2 evolution system of Rhodospirillum rubrum: Role of a 22-kDa ironsulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase
    • 2 evolution system of Rhodospirillum rubrum: role of a 22-kDa ironsulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase. J. Biol. Chem. 266:18395-18403.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18395-18403
    • Ensign, S.A.1    Ludden, P.W.2
  • 16
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillu 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 Rhodospirillu 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
  • 17
    • 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. D., 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.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 18
    • 0028911174 scopus 로고
    • HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer
    • Fu, C., J. W. Olson, and R. J. Maier. 1995. HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer. Proc. Natl. Acad. Sci. USA 92:2333-2337.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2333-2337
    • Fu, C.1    Olson, J.W.2    Maier, R.J.3
  • 20
    • 0029070195 scopus 로고
    • Protein Hpn: Cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae
    • Gilbert, J. V., J. Ramakrishna, F. W. Sunderman, Jr., A. Wright, and A. G. Plaut. 1995. Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae. Infect. Immun. 63:2682-2688.
    • (1995) Infect. Immun. , vol.63 , pp. 2682-2688
    • Gilbert, J.V.1    Ramakrishna, J.2    Sunderman Jr., F.W.3    Wright, A.4    Plaut, A.G.5
  • 21
    • 0026335588 scopus 로고
    • Linker insertion mutagenesis as probe of structure-function relationships
    • Goff, S. P., and V. R. Prasad. 1991. Linker insertion mutagenesis as probe of structure-function relationships. Methods Enzymol. 208:586-603.
    • (1991) Methods Enzymol. , vol.208 , pp. 586-603
    • Goff, S.P.1    Prasad, V.R.2
  • 22
    • 0028938830 scopus 로고
    • Post-translational regulation of nitrogenasc in Rhodospirillum rubrum strains overexpressing the regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase activating glycohydrolase
    • Grunwald, S. K., D. P. Lies, G. P. Roberts, and P. W. Ludden. 1995. Post-translational regulation of nitrogenasc in Rhodospirillum rubrum strains overexpressing the regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase activating glycohydrolase. J. Bacteriol. 177:628-635.
    • (1995) J. Bacteriol. , vol.177 , pp. 628-635
    • Grunwald, S.K.1    Lies, D.P.2    Roberts, G.P.3    Ludden, P.W.4
  • 23
    • 0003721012 scopus 로고    scopus 로고
    • General principles and mechanisms of metallocenter assembly
    • R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli, (ed.). VCH Publishers, Inc., New York, N.Y.
    • Hausinger, R. P. 1996. General principles and mechanisms of metallocenter assembly, p. 1-18. In R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli, (ed.), Mechanisms of metallocenter assembly. VCH Publishers, Inc., New York, N.Y.
    • (1996) Mechanisms of Metallocenter Assembly , pp. 1-18
    • Hausinger, R.P.1
  • 24
    • 0030051489 scopus 로고    scopus 로고
    • Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum
    • He, Y., D. Shelver, R. L. Kerby, and G. P. Roberts. 1996. Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum. J. Biol.Chem. 271:120-123.
    • (1996) J. Biol.Chem. , vol.271 , pp. 120-123
    • He, Y.1    Shelver, D.2    Kerby, R.L.3    Roberts, G.P.4
  • 27
    • 0025904248 scopus 로고
    • Metal speciation and microbial growth-the hard (and soft) facts
    • Hughes, M. N., and R. K.Poole, 1991. Metal speciation and microbial growth-the hard (and soft) facts. J. Gen. Microbiol. 137:725-734.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 725-734
    • Hughes, M.N.1    Poole, R.K.2
  • 28
    • 0029564163 scopus 로고
    • Proteus mirabilis urease: Operon fusion and linker insertion analysis of ure gene organization, regulation, and function
    • Island, M. D., and H. L. T. Mobley. 1995. Proteus mirabilis urease: operon fusion and linker insertion analysis of ure gene organization, regulation, and function. J. Bacteriol. 177:5653-5660.
    • (1995) J. Bacteriol. , vol.177 , pp. 5653-5660
    • Island, M.D.1    Mobley, H.L.T.2
  • 29
    • 0026446645 scopus 로고
    • The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli
    • Jacobi, A., R. Rossmann, and A. Bock. 1992. The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli. Arch. Microbiol. 158:444-451.
    • (1992) Arch. Microbiol. , vol.158 , pp. 444-451
    • Jacobi, A.1    Rossmann, R.2    Bock, A.3
  • 30
    • 0026649571 scopus 로고
    • Genetic and physiological characterization of the Rhodospirillum carbon monoxide dehydrogenase system
    • Kerby, R. L., S. S. Hong, S. A. Ensign, L. J. Coppoc, P. W. Ludden, and G. P. Roberts. 1992. Genetic and physiological characterization of the Rhodospirillum carbon monoxide dehydrogenase system. J. Bacteriol. 174:5284-5294.
    • (1992) J. Bacteriol. , vol.174 , pp. 5284-5294
    • Kerby, R.L.1    Hong, S.S.2    Ensign, S.A.3    Coppoc, L.J.4    Ludden, P.W.5    Roberts, G.P.6
  • 31
    • 0028925554 scopus 로고
    • Carbon monoxidedependent growth of Rhodospirillum rubrum
    • Kerby, R. L., P. W. Ludden, and G. P. Roberts. 1995. Carbon monoxidedependent growth of Rhodospirillum rubrum. J. Bacteriol. 177:2241-2244.
    • (1995) J. Bacteriol. , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 32
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodziej, P. A., and R. A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 33
    • 0028886155 scopus 로고
    • A methylnickel intermediate in a bimetallic mechanism of acetyl-cocnzyme A synthesis by anaerobic bacteria
    • Kumar, M., D. Qiu, T. G. Spiro, and S. W. Ragsdale. 1995. A methylnickel intermediate in a bimetallic mechanism of acetyl-cocnzyme A synthesis by anaerobic bacteria. Science 270:628-630.
    • (1995) Science , vol.270 , pp. 628-630
    • Kumar, M.1    Qiu, D.2    Spiro, T.G.3    Ragsdale, S.W.4
  • 34
    • 0026704632 scopus 로고
    • Klebsiella aerogenes urease gene cluster: Sequence of ureD and demonstration that four accessory genes (ureD, ureE, ureF, and ureG) are involved in nickel melallocenter biosynthesis
    • Lee, M. H., S. B. Mulrooney, M. J. Renner, Y. Markowicz, and R. P. Hausinger. 1992. Klebsiella aerogenes urease gene cluster: sequence of ureD and demonstration that four accessory genes (ureD, ureE, ureF, and ureG) are involved in nickel melallocenter biosynthesis. J. Bacteriol. 174:4324-4330.
    • (1992) J. Bacteriol. , vol.174 , pp. 4324-4330
    • Lee, M.H.1    Mulrooney, S.B.2    Renner, M.J.3    Markowicz, Y.4    Hausinger, R.P.5
  • 35
    • 0027164052 scopus 로고
    • Purification and characterization of Klebsiella aerogenes UreE protein: A nickel-binding protein that functions in urease metallocenter assembly
    • Lee, M. H., H. S. Pankratz, S. Wang, R. A. Scott, M. G. Finnegan, M. K. Johnson, J. A. Ippolito, D. W. Christianson, and R. P. Hausinger. 1993. Purification and characterization of Klebsiella aerogenes UreE protein: a nickel-binding protein that functions in urease metallocenter assembly. Protein Sci. 2:1042-1052.
    • (1993) Protein Sci. , vol.2 , pp. 1042-1052
    • Lee, M.H.1    Pankratz, H.S.2    Wang, S.3    Scott, R.A.4    Finnegan, M.G.5    Johnson, M.K.6    Ippolito, J.A.7    Christianson, D.W.8    Hausinger, R.P.9
  • 37
    • 0002886141 scopus 로고
    • The biochemistry and genetics of nitrogen fixation by photosynthetic bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.). Kluwer Academic Publishers, Dordrecht. The Netherlands
    • Ludden, P. W., and G. P. Roberts. 1995. The biochemistry and genetics of nitrogen fixation by photosynthetic bacteria, p. 929-947. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photusynthetic bacteria. Kluwer Academic Publishers, Dordrecht. The Netherlands.
    • (1995) Anoxygenic Photusynthetic Bacteria , pp. 929-947
    • Ludden, P.W.1    Roberts, G.P.2
  • 38
    • 0028031878 scopus 로고
    • Cloning, sequencing, and expression of thermophilic Bacillus sp. strain TB-90 urease gene complex in Escherichia coli
    • Maeda, M., M. Hidaka, A. Nakamura, H. Masaki, and T. Uozumi. 1994. Cloning, sequencing, and expression of thermophilic Bacillus sp. strain TB-90 urease gene complex in Escherichia coli. J. Bacteriol. 176:432-442.
    • (1994) J. Bacteriol. , vol.176 , pp. 432-442
    • Maeda, M.1    Hidaka, M.2    Nakamura, A.3    Masaki, H.4    Uozumi, T.5
  • 39
    • 0001789455 scopus 로고    scopus 로고
    • Nickel incorporation into hydrogenases
    • R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli, (ed.). VCH Publishers, Inc., New York, N.Y.
    • Maier, T., and A. Bock. 1996. Nickel incorporation into hydrogenases, p. 173-192. In R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli, (ed.), Mechanisms of metallocenter assembly. VCH Publishers, Inc., New York, N.Y.
    • (1996) Mechanisms of Metallocenter Assembly , pp. 173-192
    • Maier, T.1    Bock, A.2
  • 40
    • 0029054222 scopus 로고
    • GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli
    • Maier, T., F. Lottspeich, and A. Bock. 1995. GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli. Eur. J. Biochem. 230:133-138.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 133-138
    • Maier, T.1    Lottspeich, F.2    Bock, A.3
  • 41
    • 0029832099 scopus 로고    scopus 로고
    • Analysis of the CO dehydrogenase/acetyl-coenzyme A synthase operon of Methanosarcina themiophila
    • Maupin-Furlow, J. A., and J. G. Ferry. 1996. Analysis of the CO dehydrogenase/acetyl-coenzyme A synthase operon of Methanosarcina themiophila. J. Bacteriol. 178:6849-6856.
    • (1996) J. Bacteriol. , vol.178 , pp. 6849-6856
    • Maupin-Furlow, J.A.1    Ferry, J.G.2
  • 42
    • 0028930318 scopus 로고
    • Helicobacter pylori nickel-transport gene nixA: Synthesis of catalytically active urease in Escherichia coli independent of growth conditions
    • Mobley, H. L. T., R. M. Garner, and P. Bauerfeind. 1995. Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditions. Mol. Microbiol. 16:97-109.
    • (1995) Mol. Microbiol. , vol.16 , pp. 97-109
    • Mobley, H.L.T.1    Garner, R.M.2    Bauerfeind, P.3
  • 44
    • 0002303675 scopus 로고    scopus 로고
    • Nickel incorporation into urease
    • R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli, (ed.). VCH Publishers, Inc., New York, N.Y.
    • Moncrief, M. B. C., and R. P. Hausinger. 1996. Nickel incorporation into urease, p. 151-171. In R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli, (ed.), Mechanisms of metallocenter assembly. VCH Publishers, Inc., New York, N.Y.
    • (1996) Mechanisms of Metallocenter Assembly , pp. 151-171
    • Moncrief, M.B.C.1    Hausinger, R.P.2
  • 45
    • 0027482679 scopus 로고
    • The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel
    • Navarro, C., L.-F. Wu, and M.-A. Mandrand-Berthelot. 1993. The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel. Mol. Microbiol. 9:1181-1191.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1181-1191
    • Navarro, C.1    Wu, L.-F.2    Mandrand-Berthelot, M.-A.3
  • 46
    • 0023473632 scopus 로고
    • The use of random-sequence oligonucleotides for determining consensus sequences
    • Oliphant, A. R., and K. Struhl. 1987. The use of random-sequence oligonucleotides for determining consensus sequences. Methods Enzymol. 155:568-582.
    • (1987) Methods Enzymol. , vol.155 , pp. 568-582
    • Oliphant, A.R.1    Struhl, K.2
  • 47
    • 0017362759 scopus 로고
    • Mapping of closed circular DNAs by cleavage with restriction endonucleases and calibration by agarose gel electrophoresis
    • Parker, R. C., R. M. Watson, and J. Vinograd. 1977. Mapping of closed circular DNAs by cleavage with restriction endonucleases and calibration by agarose gel electrophoresis. Proc. Natl. Acad. Sci. USA 74:851-855.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 851-855
    • Parker, R.C.1    Watson, R.M.2    Vinograd, J.3
  • 48
    • 0028791920 scopus 로고
    • Nitrogenase structure and function: A biochemical-genetic perspective
    • Peters, J. W., K. Fisher, and D. R. Dean. 1995. Nitrogenase structure and function: a biochemical-genetic perspective. Annu. Rev. Microbiol. 49:335-366.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 335-366
    • Peters, J.W.1    Fisher, K.2    Dean, D.R.3
  • 49
    • 0021592032 scopus 로고
    • In vitro inserlional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. M. Krisch. 1984. In vitro inserlional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 50
    • 0028102344 scopus 로고
    • Purification of Rhizobiurn leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis
    • Rey, L., J. Imperial, J.-M. Palacios, and T. Ruiz-Argueso. 1994. Purification of Rhizobiurn leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis. J. Bacteriol. 176:6066-6073.
    • (1994) J. Bacteriol. , vol.176 , pp. 6066-6073
    • Rey, L.1    Imperial, J.2    Palacios, J.-M.3    Ruiz-Argueso, T.4
  • 52
    • 0027134384 scopus 로고
    • Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis
    • Schweizer, H. P. 1993. Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis. BioTechniqucs 15:831-834.
    • (1993) BioTechniqucs , vol.15 , pp. 831-834
    • Schweizer, H.P.1
  • 53
    • 0028963922 scopus 로고
    • Carbon monoxideinduced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators
    • Shelver, D., R. L. Kerby, Y. He, and G. P. Roberts. 1995. Carbon monoxideinduced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators. J. Bacteriol. 177:2157-2163.
    • (1995) J. Bacteriol. , vol.177 , pp. 2157-2163
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 54
    • 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
  • 55
    • 0028117720 scopus 로고
    • Single-step purification of Proteus mirabilis urease accessory protein UreE, a protein with a naturally occurring histidine tail, by nickel chelate affinity chromatography
    • Sriwanthana, B., M. D. Island, D. Maneval, and H. L. T. Mobley. 1994. Single-step purification of Proteus mirabilis urease accessory protein UreE, a protein with a naturally occurring histidine tail, by nickel chelate affinity chromatography. J. Bacteriol. 176:6836-6841.
    • (1994) J. Bacteriol. , vol.176 , pp. 6836-6841
    • Sriwanthana, B.1    Island, M.D.2    Maneval, D.3    Mobley, H.L.T.4
  • 56
    • 0027477526 scopus 로고
    • Structural analysis based on state-space modeling
    • Stultz, C. M., J. V. White, and T. F. Smith. 1993. Structural analysis based on state-space modeling. Protein Sci. 2:305-314.
    • (1993) Protein Sci. , vol.2 , pp. 305-314
    • Stultz, C.M.1    White, J.V.2    Smith, T.F.3
  • 57
    • 0028726343 scopus 로고
    • 430, a nickel porphinoid involved in methanogenesis
    • 430, a nickel porphinoid involved in methanogenesis. CIBA Found. Symp. 180:210-227.
    • (1994) CIBA Found. Symp. , vol.180 , pp. 210-227
    • Thauer, R.K.1    Bonacker, L.G.2
  • 59
    • 0022632813 scopus 로고
    • Pleiotropic hydrogenase mutants of Escherichia coli K12: Growth in the presence of nickel can restore hydrogenase activity
    • Waugh, R., and D. H. Boxer. 1986. Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity. Biochimie 68:157-166.
    • (1986) Biochimie , vol.68 , pp. 157-166
    • Waugh, R.1    Boxer, D.H.2
  • 60
    • 0028181528 scopus 로고
    • Protein classification by stochastic modeling and optimal filtering of amino-acid sequences
    • White, J. V., C. M. Stultz, and T. F. Smith. 1994. Protein classification by stochastic modeling and optimal filtering of amino-acid sequences. Math. Biosci. 119:35-75.
    • (1994) Math. Biosci. , vol.119 , pp. 35-75
    • White, J.V.1    Stultz, C.M.2    Smith, T.F.3
  • 61
    • 0025800967 scopus 로고
    • Clustering of genes necessary for hydrogen oxidation in Rhodobacter capsulatus
    • Xu, H.-W., and J. D. Wall. 1991. Clustering of genes necessary for hydrogen oxidation in Rhodobacter capsulatus. J. Bacteriol. 173:2401-2405.
    • (1991) J. Bacteriol. , vol.173 , pp. 2401-2405
    • Xu, H.-W.1    Wall, J.D.2


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