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Volumn 464, Issue 2, 2014, Pages 169-177

[NiFe]-hydrogenase maturation in vitro: Analysis of the roles of the HybG and HypD accessory proteins

Author keywords

Biosynthesis; Carbon monoxide; Cyanide; Hydrogenase activity; Metalloprotein; Nickel

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARBAMOYL PHOSPHATE; COBALT; COPPER; ESCHERICHIA COLI PROTEIN; HYBG ACCESSORY PROTEIN; HYPD ACCESSORY PROTEIN; NICKEL; NICKEL IRON HYDROGENASE; UNCLASSIFIED DRUG; ZINC; CARBON MONOXIDE; CHAPERONE; COENZYME; CYANIDE; HYBG PROTEIN, E COLI; HYDROGENASE; HYDROGENASE MATURATING ENDOPEPTIDASE HYBD; HYPC PROTEIN, E COLI; IRON; LIGAND; MULTIPROTEIN COMPLEX; NICKEL-IRON HYDROGENASE; PROTEINASE;

EID: 84911894921     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140485     Document Type: Article
Times cited : (22)

References (55)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • CrossRef PubMed
    • Vignais, P. M. and Billoud, B. (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem. Rev. 107, 4206-4272 CrossRef PubMed
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 3
    • 0035197070 scopus 로고    scopus 로고
    • Hydrogen production: Green algae as a source of energy
    • CrossRef PubMed
    • Melis, A. and Happe, T. (2001) Hydrogen production: green algae as a source of energy. Plant Physiol. 127, 740-748 CrossRef PubMed
    • (2001) Plant Physiol. , vol.127 , pp. 740-748
    • Melis, A.1    Happe, T.2
  • 7
    • 0026814596 scopus 로고
    • Structure function relationships among nickel-containing hydrogenases
    • CrossRef PubMed
    • Przybyla, A. E., Robbins, J., Menon, N. and Peck, H. D. (1992) Structure function relationships among nickel-containing hydrogenases. FEMS Microbiol. Rev. 8, 109-136 CrossRef PubMed
    • (1992) FEMS Microbiol. Rev. , vol.8 , pp. 109-136
    • Przybyla, A.E.1    Robbins, J.2    Menon, N.3    Peck, H.D.4
  • 9
    • 0033524910 scopus 로고    scopus 로고
    • Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe]-hydrogenases
    • CrossRef PubMed
    • Pierik, A. J., Roseboom, W., Happe, R. P., Bagley, K. A. and Albracht, S. P. J. (1999) Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe]-hydrogenases. J. Biol. Chem. 274, 3331-3337 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 3331-3337
    • Pierik, A.J.1    Roseboom, W.2    Happe, R.P.3    Bagley, K.A.4    Albracht, S.P.J.5
  • 11
    • 34248681266 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli
    • CrossRef PubMed
    • Forzi, L. and Sawers, R. G. (2007) Maturation of [NiFe]-hydrogenases in Escherichia coli. Biometals 20, 565-578 CrossRef PubMed
    • (2007) Biometals , vol.20 , pp. 565-578
    • Forzi, L.1    Sawers, R.G.2
  • 12
    • 0037147254 scopus 로고    scopus 로고
    • HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation
    • CrossRef PubMed
    • Paschos, A., Bauer, A., Zimmermann, A., Zehelein, E. and Böck, A. (2002) HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation. J. Biol. Chem. 277, 49945-49951 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 49945-49951
    • Paschos, A.1    Bauer, A.2    Zimmermann, A.3    Zehelein, E.4    Böck, A.5
  • 13
    • 0346890205 scopus 로고    scopus 로고
    • Taming of a poison: Biosynthesis of the NiFe-hydrogenase cyanide ligands
    • CrossRef PubMed
    • Reissmann, S., Hochleitner, E., Wang, H., Paschos, A., Lottspeich, F., Glass, R. S. and Böck, A. (2003) Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands. Science 299, 1067-1070 CrossRef PubMed
    • (2003) Science , vol.299 , pp. 1067-1070
    • Reissmann, S.1    Hochleitner, E.2    Wang, H.3    Paschos, A.4    Lottspeich, F.5    Glass, R.S.6    Böck, A.7
  • 14
    • 84865239562 scopus 로고    scopus 로고
    • Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases
    • CrossRef
    • Shomura, Y. and Higuchi, Y. (2012) Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases. J. Biol. Chem. 287, 28409-28419 CrossRef
    • (2012) J. Biol. Chem. , vol.287 , pp. 28409-28419
    • Shomura, Y.1    Higuchi, Y.2
  • 15
    • 7044222771 scopus 로고    scopus 로고
    • The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases
    • CrossRef PubMed
    • Blokesch, M., Albracht, S. P. J., Matzanke, B. F., Drapal, N. M., Jacobi, A. and Böck, A. (2004) The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J. Mol. Biol. 344, 155-167 CrossRef PubMed
    • (2004) J. Mol. Biol. , vol.344 , pp. 155-167
    • Blokesch, M.1    Albracht, S.P.J.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Böck, A.6
  • 16
    • 38949209555 scopus 로고    scopus 로고
    • Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coliand its interaction with HypF
    • CrossRef PubMed
    • Rangarajan, E. S., Asinas, A., Proteau, A., Munger, C., Baardsnes, J., Iannuzzi, P., Matte, A. and Cygler, M. (2008) Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coliand its interaction with HypF. J. Bacteriol. 190, 1447-1458 CrossRef PubMed
    • (2008) J. Bacteriol. , vol.190 , pp. 1447-1458
    • Rangarajan, E.S.1    Asinas, A.2    Proteau, A.3    Munger, C.4    Baardsnes, J.5    Iannuzzi, P.6    Matte, A.7    Cygler, M.8
  • 17
    • 34250851695 scopus 로고    scopus 로고
    • -, but not of the intrinsic CO in the active site of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha
    • CrossRef
    • -, but not of the intrinsic CO in the active site of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha. FEBS Lett. 17, 3322-3326 CrossRef
    • (2007) FEBS Lett. , vol.17 , pp. 3322-3326
    • Lenz, O.1    Zebger, I.2    Hamann, J.3    Hildebrandt, P.4    Friedrich, B.5
  • 19
    • 84868150470 scopus 로고    scopus 로고
    • [NiFe]-hydrogenase maturation: Isolation of a HypC-HypD complex carrying diatomic CO and CN-ligands
    • CrossRef PubMed
    • Soboh, B., Stripp, S. T., Muhr, E., Granich, C., Braussemann, M., Herzberg, M., Heberle, J. and Sawers, R. G. (2012) [NiFe]-hydrogenase maturation: isolation of a HypC-HypD complex carrying diatomic CO and CN-ligands. FEBS Lett. 586, 3882-3887 CrossRef PubMed
    • (2012) FEBS Lett. , vol.586 , pp. 3882-3887
    • Soboh, B.1    Stripp, S.T.2    Muhr, E.3    Granich, C.4    Braussemann, M.5    Herzberg, M.6    Heberle, J.7    Sawers, R.G.8
  • 21
    • 11844252075 scopus 로고    scopus 로고
    • The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different
    • CrossRef PubMed
    • Roseboom, W., Blokesch, M., Böck, A. and Albracht, S. P. J. (2005) The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett. 579, 469-472 CrossRef PubMed
    • (2005) FEBS Lett. , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Böck, A.3    Albracht, S.P.J.4
  • 22
    • 0345647107 scopus 로고    scopus 로고
    • Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia colihydrogenase 3 during enzyme maturation
    • CrossRef PubMed
    • Drapal, N. and Böck, A. (1998) Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia colihydrogenase 3 during enzyme maturation. Biochemistry 37, 2941-2948 CrossRef PubMed
    • (1998) Biochemistry , vol.37 , pp. 2941-2948
    • Drapal, N.1    Böck, A.2
  • 23
    • 15744391209 scopus 로고    scopus 로고
    • A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway
    • CrossRef PubMed
    • Zhang, J. W., Butland, G., Greenblatt, J. F., Emili, A. and Zamble, D. B. (2005) A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway. J. Biol. Chem. 280, 4360-4366 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 4360-4366
    • Zhang, J.W.1    Butland, G.2    Greenblatt, J.F.3    Emili, A.4    Zamble, D.B.5
  • 24
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • CrossRef PubMed
    • Olson, J. W., Mehta, N. S. and Maier, R. J. (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 CrossRef PubMed
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 25
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coliK-12: Evidence for a third isoenzyme
    • PubMed
    • Sawers, R. G., Ballantine, S. P. and Boxer, D. H. (1985) Differential expression of hydrogenase isoenzymes in Escherichia coliK-12: evidence for a third isoenzyme. J. Bacteriol. 164, 1324-1331 PubMed
    • (1985) J. Bacteriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 26
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia colioperon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • CrossRef PubMed
    • Andrews, S. C., Berks, B. C., McClay, J., Ambler, A., Quail, M. A., Golby, P. and Guest, J. R. (1997) A 12-cistron Escherichia colioperon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143, 3633-3647 CrossRef PubMed
    • (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
  • 27
    • 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
    • CrossRef PubMed
    • Blokesch, M., Magalon, A. and Böck, A. (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 CrossRef PubMed
    • (2001) J. Bacteriol. , vol.183 , pp. 2817-2822
    • Blokesch, M.1    Magalon, A.2    Böck, A.3
  • 28
    • 0036304751 scopus 로고    scopus 로고
    • Network of hydrogenase maturation in Escherichia coli: Role of accessory proteins HypA and HybF
    • CrossRef PubMed
    • Hube, M., Blokesch, M. and Böck, A. (2002) Network of hydrogenase maturation in Escherichia coli: role of accessory proteins HypA and HybF. J. Bacteriol. 184, 3879-3885 CrossRef PubMed
    • (2002) J. Bacteriol. , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Böck, A.3
  • 29
    • 0025975104 scopus 로고
    • Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli
    • CrossRef PubMed
    • Lutz, S., Jacobi, A., Schlensog, V., Böhm, R., Sawers, R. G. and Böck, A. (1991) Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5, 123-135 CrossRef PubMed
    • (1991) Mol. Microbiol. , vol.5 , pp. 123-135
    • Lutz, S.1    Jacobi, A.2    Schlensog, V.3    Böhm, R.4    Sawers, R.G.5    Böck, A.6
  • 31
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia colibiosynthetic system
    • CrossRef PubMed
    • King, P. W., Posewitz, M. C., Ghirardi, M. L. and Seibert, M. (2006) Functional studies of [FeFe] hydrogenase maturation in an Escherichia colibiosynthetic system. J. Bacteriol. 188, 2163-2172 CrossRef PubMed
    • (2006) J. Bacteriol. , vol.188 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 32
    • 36749042644 scopus 로고    scopus 로고
    • In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins
    • CrossRef PubMed
    • Curatti, L., Hernandez, J. A., Igarashi, R. Y., Soboh, B., Zhao, D. and Rubio, L. M. (2007) In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins. Proc. Natl. Acad. Sci. U.S.A. 104, 17626-17631 CrossRef PubMed
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17626-17631
    • Curatti, L.1    Hernandez, J.A.2    Igarashi, R.Y.3    Soboh, B.4    Zhao, D.5    Rubio, L.M.6
  • 35
    • 84877717602 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum cofactor of nitrogenise
    • CrossRef PubMed
    • Hu, Y. and Ribbe, M. W. (2013) Biosynthesis of the iron-molybdenum cofactor of nitrogenise. J. Biol. Chem. 288, 13173-13177 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 13173-13177
    • Hu, Y.1    Ribbe, M.W.2
  • 36
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coliusing bacteriophage lambda and Mu
    • CrossRef PubMed
    • Casadaban, M. J. (1976) Transposition and fusion of the lac genes to selected promoters in Escherichia coliusing bacteriophage lambda and Mu. J. Mol. Biol. 104, 541-555 CrossRef PubMed
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 37
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • CrossRef PubMed
    • Sauter, M., Böhm, R. and Böck, A. (1992) Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol. Microbiol. 6, 1523-1532 CrossRef PubMed
    • (1992) Mol. Microbiol. , vol.6 , pp. 1523-1532
    • Sauter, M.1    Böhm, R.2    Böck, A.3
  • 38
    • 36749100610 scopus 로고    scopus 로고
    • Dissecting the roles of Escherichia colihydrogenases in biohydrogen production
    • CrossRef PubMed
    • Redwood, M. D., Mikheenko, I. P., Sargent, F. and Macaskie, L. E. (2008) Dissecting the roles of Escherichia colihydrogenases in biohydrogen production. FEMS Microbiol. Lett. 278, 48-55 CrossRef PubMed
    • (2008) FEMS Microbiol. Lett. , vol.278 , pp. 48-55
    • Redwood, M.D.1    Mikheenko, I.P.2    Sargent, F.3    Macaskie, L.E.4
  • 39
    • 0026446645 scopus 로고
    • The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli
    • CrossRef PubMed
    • Jacobi, A., Rossmann, R. and Böck, A. (1992) The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli. Arch. Microbiol. 158, 444-451 CrossRef PubMed
    • (1992) Arch. Microbiol. , vol.158 , pp. 444-451
    • Jacobi, A.1    Rossmann, R.2    Böck, A.3
  • 40
    • 77956933857 scopus 로고    scopus 로고
    • Development of a cell-free system reveals an oxygen-labile step in the maturation of [NiFe]-hydrogenase 2 of Escherichia coli
    • CrossRef PubMed
    • Soboh, B., Krüger, S., Kuhns, M., Pinske, C., Lehmann, A. and Sawers, R. G. (2010) Development of a cell-free system reveals an oxygen-labile step in the maturation of [NiFe]-hydrogenase 2 of Escherichia coli. FEBS Lett. 584, 4109-4114 CrossRef PubMed
    • (2010) FEBS Lett. , vol.584 , pp. 4109-4114
    • Soboh, B.1    Krüger, S.2    Kuhns, M.3    Pinske, C.4    Lehmann, A.5    Sawers, R.G.6
  • 41
    • 84864093074 scopus 로고    scopus 로고
    • Evidence for an oxygen-sensitive iron-sulfur cluster in an immature large subunit species of Escherichia coli[NiFe]-hydrogenase 2
    • CrossRef PubMed
    • Soboh, B., Kuhns, M., Braussemann, M., Waclawek, M., Muhr, E., Pierik, A. J. and Sawers, R. G. (2012) Evidence for an oxygen-sensitive iron-sulfur cluster in an immature large subunit species of Escherichia coli[NiFe]-hydrogenase 2. Biochem. Biophys. Res. Commun. 424, 158-163 CrossRef PubMed
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 158-163
    • Soboh, B.1    Kuhns, M.2    Braussemann, M.3    Waclawek, M.4    Muhr, E.5    Pierik, A.J.6    Sawers, R.G.7
  • 42
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coliK-12
    • PubMed
    • Ballantine, S. P. and Boxer, D. H. (1985) Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coliK-12. J. Bacteriol. 163, 454-459 PubMed
    • (1985) J. Bacteriol. , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 43
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • PubMed
    • Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275 PubMed
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 45
    • 34250886905 scopus 로고    scopus 로고
    • - ligands to the active site Fe in [NiFe]-hydrogenase of Escherichia coli have different metabolic origins
    • CrossRef PubMed
    • - ligands to the active site Fe in [NiFe]-hydrogenase of Escherichia coli have different metabolic origins. FEBS Lett. 581, 3317-3321 CrossRef PubMed
    • (2007) FEBS Lett. , vol.581 , pp. 3317-3321
    • Forzi, L.1    Hellwig, P.2    Thauer, R.K.3    Sawers, R.G.4
  • 46
    • 79960870552 scopus 로고    scopus 로고
    • The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia colihave hydrogen:benzyl viologen oxidoreductase activity
    • CrossRef PubMed
    • Soboh, B., Pinske, C., Kuhns, M., Waclawek, M., Ihling, C., Trchounian, K., Trchounian, A., Sinz, A. and Sawers, R. G. (2011) The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia colihave hydrogen:benzyl viologen oxidoreductase activity. BMC Microbiol. 11, 173 CrossRef PubMed
    • (2011) BMC Microbiol. , vol.11 , pp. 173
    • Soboh, B.1    Pinske, C.2    Kuhns, M.3    Waclawek, M.4    Ihling, C.5    Trchounian, K.6    Trchounian, A.7    Sinz, A.8    Sawers, R.G.9
  • 47
    • 84874101282 scopus 로고    scopus 로고
    • Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen-the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases
    • CrossRef PubMed
    • Evans, R. M., Parkin, A., Roessler, M. M., Murphy, B. J., Adamson, H., Lukey, M. J., Sargent, F., Volbeda, A., Fontecilla-Camps, J. C. and Armstrong, F. A. (2013) Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen-the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases. J. Am. Chem. Soc. 135, 2694-2707 CrossRef PubMed
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2694-2707
    • Evans, R.M.1    Parkin, A.2    Roessler, M.M.3    Murphy, B.J.4    Adamson, H.5    Lukey, M.J.6    Sargent, F.7    Volbeda, A.8    Fontecilla-Camps, J.C.9    Armstrong, F.A.10
  • 48
    • 11844252075 scopus 로고    scopus 로고
    • The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different
    • CrossRef PubMed
    • Roseboom, W., Blokesch, M., Böck, A. and Albracht, S. P. (2005) The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett. 579, 469-472 CrossRef PubMed
    • (2005) FEBS Lett. , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Böck, A.3    Albracht, S.P.4
  • 49
    • 1942539935 scopus 로고    scopus 로고
    • HybF, a zinc containing protein involved in NiFe hydrogenase maturation
    • CrossRef PubMed
    • Blokesch, M., Rohrmoser, M., Rode, S. and Böck, A. (2004) HybF, a zinc containing protein involved in NiFe hydrogenase maturation. J. Bacteriol. 186, 2603-2611 CrossRef PubMed
    • (2004) J. Bacteriol. , vol.186 , pp. 2603-2611
    • Blokesch, M.1    Rohrmoser, M.2    Rode, S.3    Böck, A.4
  • 50
    • 0022632813 scopus 로고
    • Pleiotropic hydrogenase mutants of Escherichia coli K12: Growth in the presence of nickel can restore hydrogenase activity
    • CrossRef PubMed
    • Waugh, R. and Boxer, D. H. (1986) Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity. Biochimie 68, 157-166 CrossRef PubMed
    • (1986) Biochimie , vol.68 , pp. 157-166
    • Waugh, R.1    Boxer, D.H.2
  • 51
    • 0036440688 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli: The HypC cycle
    • CrossRef PubMed
    • Blokesch, M. and Böck, A. (2002) Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle. J. Mol. Biol. 324, 287-296 CrossRef PubMed
    • (2002) J. Mol. Biol. , vol.324 , pp. 287-296
    • Blokesch, M.1    Böck, A.2
  • 52
    • 2342435513 scopus 로고    scopus 로고
    • Thiamine biosynthesis in Escherichia coli: In vitro reconstitution of the thiazole synthase activity
    • CrossRef PubMed
    • Leonardi, R. and Roach, P. L. (2004) Thiamine biosynthesis in Escherichia coli: in vitro reconstitution of the thiazole synthase activity. J. Biol. Chem. 279, 17054-17062 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 17054-17062
    • Leonardi, R.1    Roach, P.L.2
  • 54
    • 50149115452 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • CrossRef PubMed
    • Rubio, L. M. and Ludden, P. W. (2008) Biosynthesis of the iron-molybdenum cofactor of nitrogenase. Annu. Rev. Microbiol. 62, 93-111 CrossRef PubMed
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 93-111
    • Rubio, L.M.1    Ludden, P.W.2
  • 55
    • 84896548907 scopus 로고    scopus 로고
    • Metalloprotein mimics: Old tools in a new light
    • CrossRef PubMed
    • Happe, T. and Hemschemeier, A. (2014) Metalloprotein mimics: old tools in a new light. Trends Biotechnol. 32, 170-176 CrossRef PubMed
    • (2014) Trends Biotechnol. , vol.32 , pp. 170-176
    • Happe, T.1    Hemschemeier, A.2


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