메뉴 건너뛰기




Volumn 188, Issue 6, 2006, Pages 2163-2172

Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; HYDROGENASE; IRON SULFUR PROTEIN; PROTEIN HYDA1; PROTEIN HYDE; PROTEIN HYDF; PROTEIN HYDG; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

EID: 33644850541     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.6.2163-2172.2006     Document Type: Article
Times cited : (275)

References (52)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams, M. W. 1990. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020:115-145.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.1
  • 2
    • 0001030519 scopus 로고
    • Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum
    • Adams, M. W. W., E. Eccleston, and J. B. Howard. 1989. Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum. Proc. Natl. Acad. Sci. USA 86:4932-4936.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4932-4936
    • Adams, M.W.W.1    Eccleston, E.2    Howard, J.B.3
  • 3
    • 0021194792 scopus 로고
    • The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I
    • Adams, M. W. W., and L. E. Mortenson. 1984. The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I. J. Biol. Chem. 259:7045-7055.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7045-7055
    • Adams, M.W.W.1    Mortenson, L.E.2
  • 4
    • 0033967946 scopus 로고    scopus 로고
    • Heterologous expression of clostridial hydrogenase in the cyanobacterium Synechococcus PCC7942
    • Asada, Y., Y. Koike, J. Schnackenberg, M. Miyake, I. Uemura, and J. Miyake. 2000. Heterologous expression of clostridial hydrogenase in the cyanobacterium Synechococcus PCC7942. Biochim. Biophys. Acta 1490:269-278.
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 269-278
    • Asada, Y.1    Koike, Y.2    Schnackenberg, J.3    Miyake, M.4    Uemura, I.5    Miyake, J.6
  • 7
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch, F., Y. Nicolet, J. T. Wan, J. T. Jarrett, and C. L. Drennan. 2004. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303:76-79.
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 8
    • 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
    • Blokesch, M., S. P. Alhracht, B. F. Matzanke, N. M. Drapal, A. Jacobi, and A. Bock. 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.
    • (2004) J. Mol. Biol. , vol.344 , pp. 155-167
    • Blokesch, M.1    Alhracht, S.P.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Bock, A.6
  • 9
    • 4344582395 scopus 로고    scopus 로고
    • Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE
    • Blokesch, M., A. Paschos, A. Bauer, S. Reissmann, N. Drapal, and A. Bock. 2004. Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur. J. Biochem. 271:3428-3436.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3428-3436
    • Blokesch, M.1    Paschos, A.2    Bauer, A.3    Reissmann, S.4    Drapal, N.5    Bock, A.6
  • 12
    • 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. Bock. 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    Bock, A.2
  • 13
    • 0034822720 scopus 로고    scopus 로고
    • A capable bridging ligand for Fe-only hydrogenase: Density functional calculations of a low-energy route for heterolytic cleavage and formation of dihydrogen
    • Fan, H.-J., and M. B. Hall. 2001. A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a low-energy route for heterolytic cleavage and formation of dihydrogen. J. Am. Chem. Soc. 123:3828-3829.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3828-3829
    • Fan, H.-J.1    Hall, M.B.2
  • 14
    • 0035794131 scopus 로고    scopus 로고
    • A novel type of iron hydrogenase in the green alga Scenedesmus obliquus is linked to the photosynthetic electron transport chain
    • Florin, L., A. Tsokoglou, and T. Happe. 2001. A novel type of iron hydrogenase in the green alga Scenedesmus obliquus is linked to the photosynthetic electron transport chain. J. Biol. Chem. 276:6125-6132.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6125-6132
    • Florin, L.1    Tsokoglou, A.2    Happe, T.3
  • 16
    • 0038575234 scopus 로고    scopus 로고
    • S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin?
    • Frey, P. A., and O. T. Magnusson. 2003. S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chem. Rev. 103:2129-2148.
    • (2003) Chem. Rev. , vol.103 , pp. 2129-2148
    • Frey, P.A.1    Magnusson, O.T.2
  • 17
    • 18444393412 scopus 로고    scopus 로고
    • Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities
    • Girbal, L., G. von Abendroth, M. Winkler, P. M. Benton, I. Meynial-Salles, C. Croux, J. W. Peters, T. Happe, and P. Soucaille. 2005. Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities. Appl. Environ. Microbiol. 71:2777-2781.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2777-2781
    • Girbal, L.1    Von Abendroth, G.2    Winkler, M.3    Benton, P.M.4    Meynial-Salles, I.5    Croux, C.6    Peters, J.W.7    Happe, T.8    Soucaille, P.9
  • 18
    • 0029863961 scopus 로고    scopus 로고
    • Molecular characterization and transcriptional analysis of the putative hydrogenase gene of Clostridium acetobutylicum ATCC 824
    • Gorwa, M. F., C. Croux, and P. Soucaille. 1996. Molecular characterization and transcriptional analysis of the putative hydrogenase gene of Clostridium acetobutylicum ATCC 824. J. Bacteriol. 178:2668-2675.
    • (1996) J. Bacteriol. , vol.178 , pp. 2668-2675
    • Gorwa, M.F.1    Croux, C.2    Soucaille, P.3
  • 20
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • Hanzelmann, P., and H. Schindelin. 2004. Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc. Natl. Acad. Sci. USA 101:12870-12875.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12870-12875
    • Hanzelmann, P.1    Schindelin, H.2
  • 21
    • 0036186921 scopus 로고    scopus 로고
    • Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii
    • Happe, T., and A. Kaminski. 2002. Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 269:1022-1032.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1022-1032
    • Happe, T.1    Kaminski, A.2
  • 22
    • 0028285551 scopus 로고
    • Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii
    • Happe, T., B. Mosler, and D. J. Naber. 1994. Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 222:769-774.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 769-774
    • Happe, T.1    Mosler, B.2    Naber, D.J.3
  • 23
    • 0027153213 scopus 로고
    • Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
    • Happe, T., and D. J. Naber. 1993. Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 214:475-481.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 475-481
    • Happe, T.1    Naber, D.J.2
  • 24
    • 0027965030 scopus 로고
    • Regulated expression in vitro of genes coding for formate hydrogenlyase components of Escherichia coli
    • Hopper, S., M. Babst, V. Schlensog, H. M. Fischer, H. Hennecke, and A. Bock. 1994. Regulated expression in vitro of genes coding for formate hydrogenlyase components of Escherichia coli. J. Biol. Chem. 269:19597-19604.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19597-19604
    • Hopper, S.1    Babst, M.2    Schlensog, V.3    Fischer, H.M.4    Hennecke, H.5    Bock, A.6
  • 25
    • 14744279761 scopus 로고    scopus 로고
    • Identification of a nitrogenase FeMo cofactor precursor on NifEN complex
    • Hu, Y., A. W. Fay, and M. W. Ribbe. 2005. Identification of a nitrogenase FeMo cofactor precursor on NifEN complex. Proc. Natl. Acad. Sci. USA 102:3236-3241.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3236-3241
    • Hu, Y.1    Fay, A.W.2    Ribbe, M.W.3
  • 26
    • 0035914323 scopus 로고    scopus 로고
    • Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide dehydrogenase from Rhodospirillum rubrum
    • Jeon, W. B., J. Cheng, and P. W. Ludden. 2001. Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide dehydrogenase from Rhodospirillum rubrum. J. Biol. Chem. 276:38602-38609.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38602-38609
    • Jeon, W.B.1    Cheng, J.2    Ludden, P.W.3
  • 27
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D. D., Y. I. Wolf, E. V. Koonin, and L. Aravind. 2002. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317:41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 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. Bohm, G. Sawers, and A. Bock. 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    Bohm, R.4    Sawers, G.5    Bock, A.6
  • 30
    • 0029901484 scopus 로고    scopus 로고
    • Analysis of the hydA locus of Escherichia coli: Two genes (hydN and hypF) involved in formate and hydrogen metabolism
    • Maier, T., U. Binder, and A. Bock. 1996. Analysis of the hydA locus of Escherichia coli: two genes (hydN and hypF) involved in formate and hydrogen metabolism. Arch. Microbiol. 165:333-341.
    • (1996) Arch. Microbiol. , vol.165 , pp. 333-341
    • Maier, T.1    Binder, U.2    Bock, A.3
  • 31
    • 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
  • 32
    • 0026040877 scopus 로고
    • Primary structure of hydrogenase I from Clostridium pasteurianum
    • Meyer, J., and J. Gagnon. 1991. Primary structure of hydrogenase I from Clostridium pasteurianum. Biochemistry 40:9697-9704.
    • (1991) Biochemistry , vol.40 , pp. 9697-9704
    • Meyer, J.1    Gagnon, J.2
  • 33
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster
    • Nakamura, M., K. Saeki, and Y. Takahashi. 1999. Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster. J. Biochem. 126:10-18.
    • (1999) J. Biochem. , vol.126 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 34
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • Nicolet, Y., A. L. de Lacey, X. Vernede, V. M. Fernandez, C. E. Hactikian, and J. C. Fontecilla-Camps. 2001. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J. Am. Chem. Soc. 123:1596-1601.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1596-1601
    • Nicolet, Y.1    De Lacey, A.L.2    Vernede, X.3    Fernandez, V.M.4    Hactikian, C.E.5    Fontecilla-Camps, J.C.6
  • 35
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet, Y., C. Prias, P. Legrand, C. E. Hatchikian, and J. C. Fontecilla-Camps. 1999. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure 7:13-23.
    • (1999) Structure , vol.7 , pp. 13-23
    • Nicolet, Y.1    Prias, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 37
    • 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
  • 38
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters, J. W., W. N. Lanzilotta, B. J. Lemon, and L. C. Seefeldt. 1998. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 282:1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 39
    • 0032403791 scopus 로고    scopus 로고
    • A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases
    • Pierik, A. J., M. Hulstein, W. R. Hagen, and S. P. J. Albracht. 1998. A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases. Eur. J. Biochem. 258:572-578.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 572-578
    • Pierik, A.J.1    Hulstein, M.2    Hagen, W.R.3    Albracht, S.P.J.4
  • 40
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • Posewitz, M. C., P. W. King, S. L. Smolinski, L. Zhang, M. Seibert, and M. L. Ghirardi. 2004. Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J. Biol. Chem. 279:25711-25720.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25711-25720
    • Posewitz, M.C.1    King, P.W.2    Smolinski, S.L.3    Zhang, L.4    Seibert, M.5    Ghirardi, M.L.6
  • 41
    • 0033538446 scopus 로고    scopus 로고
    • In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH
    • Rangaraj, P., M. J. Ryle, W. N. Lanzilotta, P. W. Ludden, and V. K. Shah. 1999. In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH. J. Biol. Chem. 274:19778-19784.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19778-19784
    • Rangaraj, P.1    Ryle, M.J.2    Lanzilotta, W.N.3    Ludden, P.W.4    Shah, V.K.5
  • 43
    • 0020033948 scopus 로고
    • Anionic modulation of the catalytic activity of hydrogenase from Chlamydomonas reinhardtii
    • Roessler, P., and S. Lien. 1982. Anionic modulation of the catalytic activity of hydrogenase from Chlamydomonas reinhardtii. Arch. Biochem. Biophys. 213:37-44.
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 37-44
    • Roessler, P.1    Lien, S.2
  • 44
    • 0000030603 scopus 로고
    • Activation and de novo synthesis of hydrogenase in Chlamydomonas
    • Roessler, P. G., and S. Lien. 1984. Activation and de novo synthesis of hydrogenase in Chlamydomonas. Plant Physiol. 75:705-709.
    • (1984) Plant Physiol. , vol.75 , pp. 705-709
    • Roessler, P.G.1    Lien, S.2
  • 45
    • 11844252075 scopus 로고    scopus 로고
    • The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different
    • Roseboom, W., M. Blokesch, A. Bock, and S. P. Albracht. 2005. The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett. 579:469-472.
    • (2005) FEBS Lett. , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Bock, A.3    Albracht, S.P.4
  • 46
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • Rubach, J. K., X. Brazolotto, J. Gaillard, and M. Fontecave. 2005. Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima. FEBS Lett. 579:5055-5060.
    • (2005) FEBS Lett. , vol.579 , pp. 5055-5060
    • Rubach, J.K.1    Brazolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 47
    • 0028821460 scopus 로고
    • Characterization and expression of the hydrogenase-encoding gene from Clostridium acetobutylicum P262
    • Santangelo, J. D., P. Durre, and D. R. Woods. 1995. Characterization and expression of the hydrogenase-encoding gene from Clostridium acetobutylicum P262. Microbiology 141:171-180.
    • (1995) Microbiology , vol.141 , pp. 171-180
    • Santangelo, J.D.1    Durre, P.2    Woods, D.R.3
  • 50
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phytogeny of hydrogenases
    • Vignais, P. M., B. Billoud, and J. Meyer. 2001. Classification and phytogeny 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
  • 52
    • 0023091332 scopus 로고
    • Purification and characterization of Desulfovibrio vulgaris (Hildenborough) hydrogenase expressed in Escherichia coli
    • Voordouw, G., W. R. Hagen, K. M. Kruse-Wolters, A. van Berkel-Arts, and C. Veeger. 1987. Purification and characterization of Desulfovibrio vulgaris (Hildenborough) hydrogenase expressed in Escherichia coli. Eur. J. Biochem. 162:31-36.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 31-36
    • Voordouw, G.1    Hagen, W.R.2    Kruse-Wolters, K.M.3    Van Berkel-Arts, A.4    Veeger, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.