메뉴 건너뛰기




Volumn 186, Issue 9, 2004, Pages 2603-2611

HybF, a Zinc-Containing Protein Involved in NiFe Hydrogenase Maturation

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; NICKEL; PROTEIN; PROTEIN HYPF; UNCLASSIFIED DRUG;

EID: 1942539935     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.9.2603-2611.2004     Document Type: Article
Times cited : (60)

References (60)
  • 1
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogen lyase system
    • Andrews, S. C., B. C. Berks, J. McClay, A. Ambler, M. A. Quail, P. Golby, and J. R. Guest. 1997. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogen lyase system. Microbiology 143:3633-3647.
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 2
    • 0029066353 scopus 로고
    • Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum
    • Bagley, K. A., E. C. Duin, W. Roseboom, S. P. J. Albracht, and W. H. Woodruff. 1995. Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum. Biochemistry 34:5527-5535.
    • (1995) Biochemistry , vol.34 , pp. 5527-5535
    • Bagley, K.A.1    Duin, E.C.2    Roseboom, W.3    Albracht, S.P.J.4    Woodruff, W.H.5
  • 4
    • 0035218392 scopus 로고    scopus 로고
    • Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli
    • Bagramyan, K., A. Vassilian, N. Mnatsakanyan, and A. Trehounian. 2001. Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli. Membr. Cell Biol. 14:749-763.
    • (2001) Membr. Cell Biol. , vol.14 , pp. 749-763
    • Bagramyan, K.1    Vassilian, A.2    Mnatsakanyan, N.3    Trehounian, A.4
  • 5
    • 0023049446 scopus 로고
    • Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli
    • Ballantine, S. P., and D. H. Boxer. 1986. Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli. Eur. J. Biochem. 156:277-284.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 277-284
    • Ballantine, S.P.1    Boxer, D.H.2
  • 6
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12
    • Ballantine, S. P., and D. H. Boxer. 1985. Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. J. Bacteriol. 163:454-459.
    • (1985) J. Bacteriol. , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 7
    • 0017389525 scopus 로고
    • The identification of mutants of Escherichia coli deficient in formate dehydrogenase and nitrate reductase activities using dye indicator plates
    • Begg, Y. A., J. N. Whyte, and B. A. Haddock. 1977. The identification of mutants of Escherichia coli deficient in formate dehydrogenase and nitrate reductase activities using dye indicator plates. FEMS Microbiol. Lett. 2:47-50.
    • (1977) FEMS Microbiol. Lett. , vol.2 , pp. 47-50
    • Begg, Y.A.1    Whyte, J.N.2    Haddock, B.A.3
  • 8
    • 0025255158 scopus 로고
    • Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules
    • Berg, J. M. 1990. Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules. J. Biol. Chem. 265:6513-6516.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6513-6516
    • Berg, J.M.1
  • 9
    • 0036440688 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli: The HypC cycle
    • Blokesch, M., and A. Böck. 2002. Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle. J. Mol. Biol. 324:287-296.
    • (2002) J. Mol. Biol. , vol.324 , pp. 287-296
    • Blokesch, M.1    Böck, A.2
  • 10
    • 0035048481 scopus 로고    scopus 로고
    • Interplay between the specific chaperone-like proteins HybG and HypC in maturation of hydrogenases 1, 2, and 3 from Escherichia coli
    • Blokesch, M., A. Magalon, and A. Böck. 2001. Interplay between the specific chaperone-like proteins HybG and HypC in maturation of hydrogenases 1, 2, and 3 from Escherichia coli. J. Bacteriol. 183:2817-2822.
    • (2001) J. Bacteriol. , vol.183 , pp. 2817-2822
    • Blokesch, M.1    Magalon, A.2    Böck, A.3
  • 11
    • 0000190996 scopus 로고    scopus 로고
    • Fermentation
    • F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Böck, A., and G. Sawers. 1996. Fermentation, p. 262-282. In F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, vol. 1. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 262-282
    • Böck, A.1    Sawers, G.2
  • 12
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm, R., M. Sauter, and A. Böck. 1990. Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4:231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 13
    • 0017584161 scopus 로고
    • Construction and characterization of new cloning vehicles. II. A multipurpose cloning system
    • Bolivar, F., R. L. Rodriguez, P. J. Greene, M. C. Betlach, H. L. Heyneker, and H. W. Boyer. 1977. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene 2:95-113.
    • (1977) Gene , vol.2 , pp. 95-113
    • Bolivar, F.1    Rodriguez, R.L.2    Greene, P.J.3    Betlach, M.C.4    Heyneker, H.L.5    Boyer, H.W.6
  • 14
    • 0000366608 scopus 로고
    • Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences
    • Casadaban, M. J., and S. N. Cohen. 1979. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc. Natl. Acad. Sci. 76:4530-4533.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 4530-4533
    • Casadaban, M.J.1    Cohen, S.N.2
  • 15
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C., and S. N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134:1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.1    Cohen, S.N.2
  • 16
    • 0027526586 scopus 로고
    • Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants
    • Colbeau, A., P. Richaud, B. Toussaint, F. J. Caballero, C. Elster, C. Delphin, R. L. Smith, J. Chabert, and P. M. Vignais. 1993. Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants. Mol. Microbiol. 8:15-29.
    • (1993) Mol. Microbiol. , vol.8 , pp. 15-29
    • Colbeau, A.1    Richaud, P.2    Toussaint, B.3    Caballero, F.J.4    Elster, C.5    Delphin, C.6    Smith, R.L.7    Chabert, J.8    Vignais, P.M.9
  • 17
    • 0345647107 scopus 로고    scopus 로고
    • Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation
    • Drapal, N., and A. Böck. 1998. Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation. Biochemistry 37:2941-2948.
    • (1998) Biochemistry , vol.37 , pp. 2941-2948
    • Drapal, N.1    Böck, A.2
  • 18
    • 0028127867 scopus 로고
    • The hupB gene of Azotobacter chroococcum hydrogenase gene cluster is involved in nickel metabolism
    • Du, L., and K. H. Tibelius. 1994. The hupB gene of Azotobacter chroococcum hydrogenase gene cluster is involved in nickel metabolism. Curr. Microbiol. 28:21-24.
    • (1994) Curr. Microbiol. , vol.28 , pp. 21-24
    • Du, L.1    Tibelius, K.H.2
  • 20
    • 0001067991 scopus 로고    scopus 로고
    • Nickel-iron hydrogenases
    • A. Messerschmidt, R. Huber, T. Poulos, and K. Wieghardt (ed.), John Wiley & Sons, Ltd., Chichester, United Kingdom
    • Frey, M., J. C. Fontecilla-Camps, and A. Volbeda. 2001. Nickel-iron hydrogenases, p. 880-896. In A. Messerschmidt, R. Huber, T. Poulos, and K. Wieghardt (ed.), Handbook of metalloproteins, vol. 2. John Wiley & Sons, Ltd., Chichester, United Kingdom.
    • (2001) Handbook of Metalloproteins , vol.2 , pp. 880-896
    • Frey, M.1    Fontecilla-Camps, J.C.2    Volbeda, A.3
  • 21
    • 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. 92:2333-2337.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 2333-2337
    • Fu, C.1    Olson, J.W.2    Maier, R.J.3
  • 22
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C. M., M. Aldea, B. K. Washburn, P. Babitzke, and S. R. Kushner. 1989. New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171:4617-4622.
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 24
    • 0036304751 scopus 로고    scopus 로고
    • Network of hydrogenase maturation in Escherichia coli: Role of accessory proteins HypA and HybF
    • Hube, M., M. Blokesch, and A. Böck. 2002. Network of hydrogenase maturation in Escherichia coli: role of accessory proteins HypA and HybF. J. Bacteriol. 184:3879-3885.
    • (2002) J. Bacteriol. , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Böck, A.3
  • 25
    • 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. Böck. 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    Böck, A.3
  • 26
    • 0030944159 scopus 로고    scopus 로고
    • In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: Molecular and physiological characterization of cooCTJ
    • Kerby, R. L., P. W. Ludden, and G. P. Roberts. 1997. In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: molecular and physiological characterization of cooCTJ. J. Bacteriol. 179:2259-2266.
    • (1997) J. Bacteriol. , vol.179 , pp. 2259-2266
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 27
    • 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
  • 28
    • 0025975104 scopus 로고
    • Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli
    • Lutz, S., A. Jacobi, V. Schlensog, R. Böhm, G. Sawers, and A. Böck. 1991. Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5:123-135.
    • (1991) Mol. Microbiol. , vol.5 , pp. 123-135
    • Lutz, S.1    Jacobi, A.2    Schlensog, V.3    Böhm, R.4    Sawers, G.5    Böck, A.6
  • 29
    • 0040355752 scopus 로고    scopus 로고
    • Analysis of the HypC-HycE complex, a key intermediate in the assembly of the metal center of the Escherichia coli hydrogenase 3
    • Magalon, A., and A. Böck. 2000. Analysis of the HypC-HycE complex, a key intermediate in the assembly of the metal center of the Escherichia coli hydrogenase 3. J. Biol. Chem. 275:21114-21220.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21114-21220
    • Magalon, A.1    Böck, A.2
  • 30
    • 0029757989 scopus 로고    scopus 로고
    • Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form
    • Maier, T., and A. Böck. 1996. Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form. Biochemistry 35:10089-10093.
    • (1996) Biochemistry , vol.35 , pp. 10089-10093
    • Maier, T.1    Böck, A.2
  • 31
    • 0027450599 scopus 로고
    • The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein
    • Maier, T., A. Jacobi, M. Sauter, and A. Böck. 1993. The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein. J. Bacteriol. 175:630-635.
    • (1993) J. Bacteriol. , vol.175 , pp. 630-635
    • Maier, T.1    Jacobi, A.2    Sauter, M.3    Böck, A.4
  • 32
    • 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
  • 33
    • 0037307747 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase
    • Mehta, N., J. W. Olson, and R. J. Maier. 2003. Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase. J. Bacteriol. 185:726-734.
    • (2003) J. Bacteriol. , vol.185 , pp. 726-734
    • Mehta, N.1    Olson, J.W.2    Maier, R.J.3
  • 34
    • 0028157325 scopus 로고
    • In vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase in Azotobacter vinelandii
    • Menon, A. L., and R. L. Robson. 1994. In vivo and in vitro nickel-dependent processing of the [NiFe] hydrogenase in Azotobacter vinelandii. J. Bacteriol. 176:291-295.
    • (1994) J. Bacteriol. , vol.176 , pp. 291-295
    • Menon, A.L.1    Robson, R.L.2
  • 36
    • 0025366313 scopus 로고
    • Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames
    • Menon, N. K., J. Robbins, H. D. Peck, Jr., C. Y. Chatelus, E. S. Choi, and A. E. Przybyla. 1990. Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames. J. Bacteriol. 172:1969-1977.
    • (1990) J. Bacteriol. , vol.172 , pp. 1969-1977
    • Menon, N.K.1    Robbins, J.2    Peck Jr., H.D.3    Chatelus, C.Y.4    Choi, E.S.5    Przybyla, A.E.6
  • 38
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., A. S. Gerber, and D. L. Hartl. 1988. Genetic applications of an inverse polymerase chain reaction. Genetics 120:621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 39
    • 0034053033 scopus 로고    scopus 로고
    • Dual roles of Bradyrhizobium japonicum nickelin protein in nickel storage and GTP-dependent Ni mobilization
    • Olson, J. W., and R. J. Maier. 2000. Dual roles of Bradyrhizobium japonicum nickelin protein in nickel storage and GTP-dependent Ni mobilization. J. Bacteriol. 182:1702-1705.
    • (2000) J. Bacteriol. , vol.182 , pp. 1702-1705
    • Olson, J.W.1    Maier, R.J.2
  • 40
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • Olson, J. W., N. S. Mehta, and R. J. Maier. 2001. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol. Microbiol. 39:176-182.
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 41
    • 0037147254 scopus 로고    scopus 로고
    • HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation
    • Paschos, A., A. Bauer, A. Zimmermann, E. Zehelein, and A. Bock. 2002. HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation. J. Biol. Chem. 277:49945-49951.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49945-49951
    • Paschos, A.1    Bauer, A.2    Zimmermann, A.3    Zehelein, E.4    Bock, A.5
  • 42
    • 0001380812 scopus 로고
    • Formic dehydrogenase and the hydrogenlyase enzyme complex in coli-aerogenes bacteria
    • Peck, H. D., and H. Gest. 1957. Formic dehydrogenase and the hydrogenlyase enzyme complex in coli-aerogenes bacteria. J. Bacteriol. 73:706-721.
    • (1957) J. Bacteriol. , vol.73 , pp. 706-721
    • Peck, H.D.1    Gest, H.2
  • 44
    • 0035966111 scopus 로고    scopus 로고
    • 2+ transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii
    • 2+ transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii. J. Biol. Chem. 276:49365-49370.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49365-49370
    • Remaut, H.1    Safarov, N.2    Ciurli, S.3    Van Beeumen, J.4
  • 45
    • 0028102344 scopus 로고
    • Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis
    • Rey, L, J. Imperial, J. M. Palacios, and T. Ruiz-Argueso. 1994. Purification of Rhizobium 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
  • 46
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • Sawers, G. 1994. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Leeuwenhoek 66:57-88.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 57-88
    • Sawers, G.1
  • 47
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: Evidence for a third isoenzyme
    • Sawers, R. G., S. P. Ballantine, and D. H. Boxer. 1985. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J. Bacteriol. 164:1324-1331.
    • (1985) J. Bacteriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 48
    • 0023049475 scopus 로고
    • Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K-12
    • Sawers, R. G., and D. H. Boxer. 1986. Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K-12. Eur. J. Biochem. 156:265-275.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 265-275
    • Sawers, R.G.1    Boxer, D.H.2
  • 50
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 51
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 52
    • 0027032362 scopus 로고
    • Active zinc binding sites of zinc metalloenzymes
    • Vallee, B. L., and D. S. Auld. 1992. Active zinc binding sites of zinc metalloenzymes. Matrix Suppl. 1:5-19.
    • (1992) Matrix Suppl. , vol.1 , pp. 5-19
    • Vallee, B.L.1    Auld, D.S.2
  • 53
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P. M., B. Billoud, and J. Meyer. 2001. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25:455-501.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 56
    • 0024563905 scopus 로고
    • Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli
    • Walleczek, J., T. Martin, B. Redl, M. Stoffier-Meilicke, and G. Stoffler. 1989. Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli. Biochemistry 28:4099-4105.
    • (1989) Biochemistry , vol.28 , pp. 4099-4105
    • Walleczek, J.1    Martin, T.2    Redl, B.3    Stoffier-Meilicke, M.4    Stoffler, G.5
  • 57
    • 0017717820 scopus 로고
    • Polyspermine-ribonuclease prepared by cross-linkage with dimethyl suberimidate
    • Wang, D., and S. Moore. 1977. Polyspermine-ribonuclease prepared by cross-linkage with dimethyl suberimidate. Biochemistry 16:2937-2942.
    • (1977) Biochemistry , vol.16 , pp. 2937-2942
    • Wang, D.1    Moore, S.2
  • 58
    • 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
    • 0022639247 scopus 로고
    • Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity
    • Wu, L. F., and M. A. Mandrand-Berthelot. 1986. Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity. Biochimie 68:167-179.
    • (1986) Biochimie , vol.68 , pp. 167-179
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.