메뉴 건너뛰기




Volumn 393, Issue 10, 2012, Pages 1089-1100

Structural basis of [NiFe] hydrogenase maturation by Hyp proteins

Author keywords

Assembly of the metal center; Hydrogenase; Hyp protein

Indexed keywords

GUANOSINE TRIPHOSPHATASE; HYDROGENASE; METALLOCHAPERONE; MONOMER; PROTEIN HYP; UNCLASSIFIED DRUG;

EID: 84869456872     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0197     Document Type: Review
Times cited : (32)

References (64)
  • 1
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallo graphy
    • Anand, R., Hoskins, A.A., Stubbe, J., and Ealick, S.E. (2004). Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallo graphy. Biochemistry 43, 10328-10342.
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 2
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: A snapshot of the evolution of sequence, structure and function
    • Arcus, V. (2002). OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr. Opin. Struct. Biol. 12, 794-801.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 794-801
    • Arcus, V.1
  • 3
    • 0036440688 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli : The HypC cycle
    • Blokesch, M. and Böck, A. (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
  • 4
    • 33745867578 scopus 로고    scopus 로고
    • Properties of the [NiFe]- hydrogenase maturation protein HypD
    • Blokesch, M. and Böck, A. (2006). Properties of the [NiFe]- hydrogenase maturation protein HypD. FEBS Lett. 580, 4065-4068.
    • (2006) Febs Lett. , vol.580 , pp. 4065-4068
    • Blokesch, M.1    Bock, A.2
  • 5
    • 7044222771 scopus 로고    scopus 로고
    • The complex between hydrogenasematuration proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]- hydrogenases
    • Blokesch, M., Albracht, S.P., Matzanke, B.F., Drapal, N.M., Jacobi, A., and Böck, A. (2004a). The complex between hydrogenasematuration 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    Albracht, S.P.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Bock, A.6
  • 6
    • 1942539935 scopus 로고    scopus 로고
    • HybF, a zinc-containing protein involved in NiFe hydrogenase maturation
    • Blokesch, M., Rohrmoser, M., Rode, S., and Böck, A. (2004b). HybF, a zinc-containing protein involved in NiFe hydrogenase maturation. J. Bacteriol. 186, 2603-2611.
    • (2004) J. Bacteriol. , vol.186 , pp. 2603-2611
    • Blokesch, M.1    Rohrmoser, M.2    Rode, S.3    Bock, A.4
  • 8
    • 84455192785 scopus 로고    scopus 로고
    • Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase
    • Bürstel, I., Hummel, P., Siebert, E., Wisitruangsakul, N., Zebger, I., Friedrich, B., and Lenz, O. (2011). Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase. J. Biol. Chem. 286, 44937-44944.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44937-44944
    • Bürstel, I.1    Hummel, P.2    Siebert, E.3    Wisitruangsakul, N.4    Zebger, I.5    Friedrich, B.6    Lenz, O.7
  • 9
    • 80051546547 scopus 로고    scopus 로고
    • Relationship between the GTPase, metal-binding, and dimerization activities of e
    • Cai, F., Ngu, T.T., Kaluarachchi, H., and Zamble, D.B. (2011). Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB. J. Biol. Inorg. Chem. 16, 857-868.
    • (2011) Coli HypB. J. Biol. Inorg. Chem. , vol.16 , pp. 857-868
    • Cai, F.1    Ngu, T.T.2    Kaluarachchi, H.3    Zamble, D.B.4
  • 10
    • 15444373859 scopus 로고    scopus 로고
    • Investigating the effects of mutations on protein aggregation in the cell
    • Calloni, G., Zoffoli, S., Stefani, M., Dobson, C.M., and Chiti, F. (2005). Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem. 280, 10607-10613.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10607-10613
    • Calloni, G.1    Zoffoli, S.2    Stefani, M.3    Dobson, C.M.4    Chiti, F.5
  • 12
    • 84863287540 scopus 로고    scopus 로고
    • Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation
    • Chan, K.H., Lee, K.M., and Wong, K.B. (2012a). Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation. PLoS One 7, e32592.
    • (2012) PLoS One , vol.7
    • Chan, K.H.1    Lee, K.M.2    Wong, K.B.3
  • 13
    • 84856063603 scopus 로고    scopus 로고
    • Structural basis for GTP-dependent dimerization of hydrogenase maturation factor HypB
    • Chan, K.H., Li, T., Wong, C.O., and Wong, K.B. (2012b). Structural basis for GTP-dependent dimerization of hydrogenase maturation factor HypB. PLoS One 7, e30547.
    • (2012) PLoS One , vol.7
    • Chan, K.H.1    Li, T.2    Wong, C.O.3    Wong, K.B.4
  • 14
    • 83355169703 scopus 로고    scopus 로고
    • Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase
    • Chan Chung, K.C. and Zamble, D.B. (2011). Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase. J. Biol. Chem. 286, 43081-43090.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43081-43090
    • Chan Chung, K.C.1    Zamble, D.B.2
  • 16
    • 34447120818 scopus 로고    scopus 로고
    • Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase
    • Dai, S., Friemann, R., Glauser, D.A., Bourquin, F., Manieri, W., Schürmann, P., and Eklund, H. (2007). Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Nature 448, 92-96.
    • (2007) Nature , vol.448 , pp. 92-96
    • Dai, S.1    Friemann, R.2    Glauser, D.A.3    Bourquin, F.4    Manieri, W.5    Schürmann, P.6    Eklund, H.7
  • 17
    • 56249119177 scopus 로고    scopus 로고
    • Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB
    • Dias, A.V., Mulvihill, C.M., Leach, M.R., Pickering, I.J., George, G.N., and Zamble, D.B. (2008). Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB. Biochemistry 47, 11981-11991.
    • (2008) Biochemistry , vol.47 , pp. 11981-11991
    • Dias, A.V.1    Mulvihill, C.M.2    Leach, M.R.3    Pickering, I.J.4    George, G.N.5    Zamble, D.B.6
  • 18
    • 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 Böck, A. (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
  • 21
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]- hydrogenases
    • Fontecilla-Camps, J.C., Volbeda, A., Cavazza, C., and Nicolet, Y. (2007). Structure/function relationships of [NiFe]- and [FeFe]- hydrogenases. Chem. Rev. 107, 4273-4303.
    • (2007) Chem. Rev. , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 22
    • 68949181269 scopus 로고    scopus 로고
    • Structure-function relationships of anaerobic gas-processing metalloenzymes
    • Fontecilla-Camps, J.C., Amara, P., Cavazza, C., Nicolet, Y., and Volbeda, A. (2009). Structure-function relationships of anaerobic gas-processing metalloenzymes. Nature 460, 814-822.
    • (2009) Nature , vol.460 , pp. 814-822
    • Fontecilla-Camps, J.C.1    Amara, P.2    Cavazza, C.3    Nicolet, Y.4    Volbeda, A.5
  • 23
    • 0028911174 scopus 로고
    • HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer
    • Fu, C., Olson, J.W., and Maier, R.J. (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
  • 24
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • Gasper, R., Scrima, A., and Wittinghofer, A. (2006). Structural insights into HypB, a GTP-binding protein that regulates metal binding. J. Biol. Chem. 281, 27492-27502.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 26
    • 0036304751 scopus 로고    scopus 로고
    • Network of hydrogenase maturation in Escherichia coli : Role of accessory proteins HypA and HybF
    • 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.
    • (2002) J. Bacteriol. , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Bock, A.3
  • 28
    • 83455221556 scopus 로고    scopus 로고
    • Escherichia coli SlyD, more than a Ni(II) reservoir
    • Kaluarachchi, H., Zhang, J.W., and Zamble, D.B. (2011). Escherichia coli SlyD, more than a Ni(II) reservoir. Biochemistry 50, 10761-10763.
    • (2011) Biochemistry , vol.50 , pp. 10761-10763
    • Kaluarachchi, H.1    Zhang, J.W.2    Zamble, D.B.3
  • 29
    • 24644474525 scopus 로고    scopus 로고
    • Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB
    • Leach, M.R., Sandal, S., Sun, H., and Zamble, D.B. (2005). Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB. Biochemistry 44, 12229-12238.
    • (2005) Biochemistry , vol.44 , pp. 12229-12238
    • Leach, M.R.1    Sandal, S.2    Sun, H.3    Zamble, D.B.4
  • 30
    • 34447518542 scopus 로고    scopus 로고
    • The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD
    • Leach, M.R., Zhang, J.W., and Zamble, D.B. (2007). The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD. J. Biol. Chem. 282, 16177-16186.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16177-16186
    • Leach, M.R.1    Zhang, J.W.2    Zamble, D.B.3
  • 31
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D.D., Wolf, Y.I., Koonin, E.V., and Aravind, L. (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
  • 32
    • 0001007592 scopus 로고    scopus 로고
    • X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution
    • Li, C., Kappock, T.J., Stubbe, J., Weaver, T.M., and Ealick, S.E. (1999). X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution. Structure 7, 1155-1166.
    • (1999) Structure , vol.7 , pp. 1155-1166
    • Li, C.1    Kappock, T.J.2    Stubbe, J.3    Weaver, T.M.4    Ealick, S.E.5
  • 34
    • 0029054222 scopus 로고
    • GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli
    • Maier, T., Lottspeich, F., and Böck, A. (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    Böck, A.3
  • 35
    • 77950298239 scopus 로고    scopus 로고
    • Specificity and selectivity of HypC chaperonins and endopeptidases in the molecular assembly machinery of [NiFe] hydrogenases of Thiocapsa roseopersicina
    • Maróti, G., Rakhely, G., Maroti, J., Doroghazi, E., Klement, E., Medzihradszky, K.F., and Kovacs, K.L. (2010). Specificity and selectivity of HypC chaperonins and endopeptidases in the molecular assembly machinery of [NiFe] hydrogenases of Thiocapsa roseopersicina. Int. J. Hydrogen Energ. 35, 3358- 3370.
    • (2010) Int. J. Hydrogen Energ. , vol.35 , pp. 3358-3370
    • Maróti, G.1    Rakhely, G.2    Maroti, J.3    Doroghazi, E.4    Klement, E.5    Medzihradszky, K.F.6    Kovacs, K.L.7
  • 36
    • 0141681866 scopus 로고    scopus 로고
    • Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization
    • Mehta, N., Benoit, S., and Maier, R.J. (2003a). Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization. Microb. Pathog. 35, 229-234.
    • (2003) Microb. Pathog. , vol.35 , pp. 229-234
    • Mehta, N.1    Benoit, S.2    Maier, R.J.3
  • 37
    • 0037307747 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase
    • Mehta, N., Olson, J.W., and Maier, R.J. (2003b). 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
  • 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 Maier, R.J. (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., 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.
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 41
    • 0035846848 scopus 로고    scopus 로고
    • Carbamoylphosphate requirement for synthesis of the active center of [NiFe]- hydrogenases
    • Paschos, A., Glass, R.S., and Böck, A. (2001). Carbamoylphosphate requirement for synthesis of the active center of [NiFe]- hydrogenases. FEBS Lett. 488, 9-12.
    • (2001) Febs Lett. , vol.488 , pp. 9-12
    • Paschos, A.1    Glass, R.S.2    Bock, A.3
  • 43
    • 38949209555 scopus 로고    scopus 로고
    • Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF
    • 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 coli and its interaction with HypF. J. Bacteriol. 190, 1447-1458.
    • (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
  • 46
    • 0028102344 scopus 로고
    • Purification of Rhizobium leguminosarum HypB, a nickelbinding protein required for hydrogenase synthesis
    • Rey, L., Imperial, J., Palacios, J.M., and Ruiz-Argueso, T. (1994). Purification of Rhizobium leguminosarum HypB, a nickelbinding 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
  • 47
    • 0029745210 scopus 로고    scopus 로고
    • Involvement of the GroE chaperonins in the nickel-dependent anaerobic biosynthesis of NiFe-hydrogenases of Escherichia coli
    • Rodrigue, A., Batia, N., Muller, M., Fayet, O., Bohm, R., Mandrand- Berthelot, M.A., and Wu, L.F. (1996). Involvement of the GroE chaperonins in the nickel-dependent anaerobic biosynthesis of NiFe-hydrogenases of Escherichia coli . J. Bacteriol. 178, 4453-4460.
    • (1996) J. Bacteriol. , vol.178 , pp. 4453-4460
    • Rodrigue, A.1    Batia, N.2    Muller, M.3    Fayet, O.4    Bohm, R.5    Mandrand-Berthelot, M.A.6    Wu, L.F.7
  • 48
    • 0036382641 scopus 로고    scopus 로고
    • Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain
    • Rosano, C., Zuccotti, S., Bucciantini, M., Stefani, M., Ramponi, G., and Bolognesi, M. (2002). Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain. J. Mol. Biol. 321, 785-796.
    • (2002) J. Mol. Biol. , vol.321 , pp. 785-796
    • Rosano, C.1    Zuccotti, S.2    Bucciantini, M.3    Stefani, M.4    Ramponi, G.5    Bolognesi, M.6
  • 49
    • 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., 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.
    • (2005) Febs Lett. , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Bock, A.3    Albracht, S.P.4
  • 50
    • 84855793147 scopus 로고    scopus 로고
    • Characterization and in vitro interaction study of a [NiFe] hydrogenase large subunit from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1
    • Sasaki, D., Watanabe, S., Kanai, T., Atomi, H., Imanaka, T., and Miki, K. (2011). Characterization and in vitro interaction study of a [NiFe] hydrogenase large subunit from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1. Biochem. Biophys. Res. Commun. 417, 192-196.
    • (2011) Biochem. Biophys. Res. Commun. , vol.417 , pp. 192-196
    • Sasaki, D.1    Watanabe, S.2    Kanai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 51
    • 84865239562 scopus 로고    scopus 로고
    • Structural basis for the reaction mechanism of S -carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases
    • in press
    • 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. (in press).
    • (2012) J. Biol. Chem.
    • Shomura, Y.1    Higuchi, Y.2
  • 52
    • 34548408733 scopus 로고    scopus 로고
    • Crystal structures of hydrogenase maturation protein HypE in the Apo and ATP-bound forms
    • Shomura, Y., Komori, H., Miyabe, N., Tomiyama, M., Shibata, N., and Higuchi, Y. (2007). Crystal structures of hydrogenase maturation protein HypE in the Apo and ATP-bound forms. J. Mol. Biol. 372, 1045-1054.
    • (2007) J. Mol. Biol. , vol.372 , pp. 1045-1054
    • Shomura, Y.1    Komori, H.2    Miyabe, N.3    Tomiyama, M.4    Shibata, N.5    Higuchi, Y.6
  • 53
    • 79952385857 scopus 로고    scopus 로고
    • Effects of metal on the biochemical properties of Helicobacter pylori HypB, a maturation factor of [NiFe]-hydrogenase and urease
    • Sydor, A.M., Liu, J., and Zamble, D.B. (2011). Effects of metal on the biochemical properties of Helicobacter pylori HypB, a maturation factor of [NiFe]-hydrogenase and urease. J. Bacteriol. 193, 1359-1368.
    • (2011) J. Bacteriol. , vol.193 , pp. 1359-1368
    • Sydor, A.M.1    Liu, J.2    Zamble, D.B.3
  • 55
    • 14644401765 scopus 로고    scopus 로고
    • [NiFe]-Hydrogenase maturation endopeptidase: Structure and function
    • Theodoratou, E., Huber, R., and Bock, A. (2005). [NiFe]-Hydrogenase maturation endopeptidase: structure and function. Biochem. Soc. Trans. 33, 108-111.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 108-111
    • Theodoratou, E.1    Huber, R.2    Bock, A.3
  • 56
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais, P.M. and Billoud, B. (2007). Occurrence, classification, and biological function of hydrogenases: an overview. Chem. Rev. 107, 4206-4272.
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 57
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P.M., Billoud, B., and Meyer, J. (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
  • 58
    • 0242695597 scopus 로고    scopus 로고
    • The active site and catalytic mechanism of NiFe hydrogenases
    • Volbeda, A. and Fontecilla-Camps, J.C. (2003). The active site and catalytic mechanism of NiFe hydrogenases. Dalton Trans. 4030-4038.
    • (2003) Dalton Trans , pp. 4030-4038
    • Volbeda, A.1    Fontecilla-Camps, J.C.2
  • 59
    • 34547785583 scopus 로고    scopus 로고
    • Solution structure of Escherichia coli HypC
    • Wang, L., Xia, B., and Jin, C. (2007). Solution structure of Escherichia coli HypC. Biochem. Biophys. Res. Commun. 361, 665-669.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 665-669
    • Wang, L.1    Xia, B.2    Jin, C.3
  • 60
    • 34250874525 scopus 로고    scopus 로고
    • Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: Insights into cyanation reaction by thiol redox signaling
    • Watanabe, S., Matsumi, R., Arai, T., Atomi, H., Imanaka, T., and Miki, K. (2007). Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling. Mol. Cell 27, 29-40.
    • (2007) Mol. Cell , vol.27 , pp. 29-40
    • Watanabe, S.1    Matsumi, R.2    Arai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 61
    • 70350728386 scopus 로고    scopus 로고
    • Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation
    • Watanabe, S., Arai, T., Matsumi, R., Atomi, H., Imanaka, T., and Miki, K. (2009). Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation. J. Mol. Biol. 394, 448-459.
    • (2009) J. Mol. Biol. , vol.394 , pp. 448-459
    • Watanabe, S.1    Arai, T.2    Matsumi, R.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 62
    • 67651221840 scopus 로고    scopus 로고
    • Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites
    • Xia, W., Li, H., Sze, K.H., and Sun, H. (2009). Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites. J. Am. Chem. Soc. 131, 10031-10040.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10031-10040
    • Xia, W.1    Li, H.2    Sze, K.H.3    Sun, H.4
  • 63
    • 84863149329 scopus 로고    scopus 로고
    • Metallo- GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA
    • Xia, W., Li, H., Yang, X., Wong, K.B., and Sun, H. (2012). Metallo- GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA. J. Biol. Chem. 287, 6753-6763.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6753-6763
    • Xia, W.1    Li, H.2    Yang, X.3    Wong, K.B.4    Sun, H.5
  • 64
    • 15744391209 scopus 로고    scopus 로고
    • A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway
    • 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.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.