메뉴 건너뛰기




Volumn 11, Issue 2, 2007, Pages 159-165

Metallocenter assembly of the hydrogenase enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; ENZYME PRECURSOR; FERROUS SULFATE; HYDROGENASE; IRON; LIGAND; METAL; NICKEL; NONMETAL; PROTEIN;

EID: 34047134687     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2007.01.011     Document Type: Review
Times cited : (83)

References (54)
  • 1
    • 0035986679 scopus 로고    scopus 로고
    • Metallochaperones: bind and deliver
    • Rosenzweig A.C. Metallochaperones: bind and deliver. Chem Biol 9 (2002) 673-677
    • (2002) Chem Biol , vol.9 , pp. 673-677
    • Rosenzweig, A.C.1
  • 2
    • 1542304722 scopus 로고    scopus 로고
    • Biosynthesis of metal sites
    • Kuchar J., and Hausinger R.P. Biosynthesis of metal sites. Chem Rev 104 (2004) 509-525
    • (2004) Chem Rev , vol.104 , pp. 509-525
    • Kuchar, J.1    Hausinger, R.P.2
  • 3
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais P.M., Billoud B., and Meyer J. Classification and phylogeny of hydrogenases. FEMS Microbiol Rev 25 (2001) 455-501
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 5
    • 0242695597 scopus 로고    scopus 로고
    • The active site and catalytic mechanism of NiFe hydrogenases
    • Volbeda A., and Fontecilla-Camps J.C. The active site and catalytic mechanism of NiFe hydrogenases. Dalton Trans (2003) 4030-4038
    • (2003) Dalton Trans , pp. 4030-4038
    • Volbeda, A.1    Fontecilla-Camps, J.C.2
  • 6
    • 33750086029 scopus 로고    scopus 로고
    • The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif
    • X-ray absorption spectroscopy and mutagenesis was used to demonstrate that the Fe-S-cluster-free hydrogenase contains a mononuclear iron site with two CO ligands, one or two N or O ligands, and one sulfur ligand supplied by a cysteine residue on the protein or an exogenous ligand in the free cofactor. Previous spectroscopic and structural studies are referenced.
    • Korbas M., Vogt S., Meyer-Klaucke W., Bill E., Lyon E.J., Thauer R.K., and Shima S. The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif. J Biol Chem 281 (2006) 30804-30813. X-ray absorption spectroscopy and mutagenesis was used to demonstrate that the Fe-S-cluster-free hydrogenase contains a mononuclear iron site with two CO ligands, one or two N or O ligands, and one sulfur ligand supplied by a cysteine residue on the protein or an exogenous ligand in the free cofactor. Previous spectroscopic and structural studies are referenced.
    • (2006) J Biol Chem , vol.281 , pp. 30804-30813
    • Korbas, M.1    Vogt, S.2    Meyer-Klaucke, W.3    Bill, E.4    Lyon, E.J.5    Thauer, R.K.6    Shima, S.7
  • 9
    • 23644455994 scopus 로고    scopus 로고
    • A model system for [NiFe] hydrogenase maturation studies: purification of an active site-containing hydrogenase large subunit without small subunit
    • 2-sensing [NiFe] hydrogenase from R. eutropha was purified in two forms, one as a homodimer and the other in a complex with HypC and HypB. Both forms contained iron but only sub-stoichiometric amounts of nickel, providing evidence that iron insertion precedes nickel insertion.
    • 2-sensing [NiFe] hydrogenase from R. eutropha was purified in two forms, one as a homodimer and the other in a complex with HypC and HypB. Both forms contained iron but only sub-stoichiometric amounts of nickel, providing evidence that iron insertion precedes nickel insertion.
    • (2005) FEBS Lett , vol.579 , pp. 4292-4296
    • Winter, G.1    Buhrke, T.2    Lenz, O.3    Jones, A.K.4    Forgber, M.5    Friedrich, B.6
  • 10
    • 23644447227 scopus 로고    scopus 로고
    • The structure of the Ni-Fe site in the isolated HoxC subunit of the hydrogen-sensing hydrogenase from Ralstonia eutropha
    • X-ray absorption spectroscopy provides evidence for a completed iron center in a purified intermediate lacking nickel.
    • Löscher S., Zebger I., Andersen L.K., Hildebrandt P., Meyer-Klaucke W., and Haumann M. The structure of the Ni-Fe site in the isolated HoxC subunit of the hydrogen-sensing hydrogenase from Ralstonia eutropha. FEBS Lett 579 (2005) 4287-4291. X-ray absorption spectroscopy provides evidence for a completed iron center in a purified intermediate lacking nickel.
    • (2005) FEBS Lett , vol.579 , pp. 4287-4291
    • Löscher, S.1    Zebger, I.2    Andersen, L.K.3    Hildebrandt, P.4    Meyer-Klaucke, W.5    Haumann, M.6
  • 12
    • 4344582395 scopus 로고    scopus 로고
    • Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE
    • Blokesch M., Paschos A., Bauer A., Reissmann S., Drapal N., and Böck A. Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur J Biochem 271 (2004) 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    Böck, A.6
  • 13
    • 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
    • This study demonstrates that HypD contains a [4Fe-4S] cluster. A HypD-HypC complex interacts with HypE and receives the CN ligand produced by HypF and HypE. These results suggest a defined pathway for the transfer of the CN ligands to the Fe of [NiFe] hydrogenases.
    • Blokesch M., Albracht S.P.J., Matzanke B.F., Drapal N.M., Jacobi A., and Böck A. 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 (2004) 155-167. This study demonstrates that HypD contains a [4Fe-4S] cluster. A HypD-HypC complex interacts with HypE and receives the CN ligand produced by HypF and HypE. These results suggest a defined pathway for the transfer of the CN ligands to the Fe of [NiFe] hydrogenases.
    • (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
  • 14
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A.-L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., and Szweda L.I. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305 (2004) 242-245
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.-L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 15
    • 33745867578 scopus 로고    scopus 로고
    • Properties of the [NiFe]-hydrogenase maturation protein HypD
    • Blokesch M., and Böck A. Properties of the [NiFe]-hydrogenase maturation protein HypD. FEBS Lett 580 (2006) 4065-4068
    • (2006) FEBS Lett , vol.580 , pp. 4065-4068
    • Blokesch, M.1    Böck, A.2
  • 16
    • 0035846848 scopus 로고    scopus 로고
    • Carbamoylphosphate requirement for synthesis of the active center of [NiFe]-hydrogenases
    • Paschos A., Glass R.S., and Böck A. Carbamoylphosphate requirement for synthesis of the active center of [NiFe]-hydrogenases. FEBS Lett 488 (2001) 9-12
    • (2001) FEBS Lett , vol.488 , pp. 9-12
    • Paschos, A.1    Glass, R.S.2    Böck, A.3
  • 17
    • 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.J. The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett 579 (2005) 469-472
    • (2005) FEBS Lett , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Böck, A.3    Albracht, S.P.J.4
  • 18
    • 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. Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase. J Bacteriol 185 (2003) 726-734
    • (2003) J Bacteriol , vol.185 , pp. 726-734
    • Mehta, N.1    Olson, J.W.2    Maier, R.J.3
  • 19
    • 21844469960 scopus 로고    scopus 로고
    • Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel
    • Atanassova A., and Zamble D.B. Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel. J Bacteriol 187 (2005) 4689-4697
    • (2005) J Bacteriol , vol.187 , pp. 4689-4697
    • Atanassova, A.1    Zamble, D.B.2
  • 20
    • 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. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol Microbiol 39 (2001) 176-182
    • (2001) Mol Microbiol , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 21
    • 14644401765 scopus 로고    scopus 로고
    • [NiFe]-hydrogenase maturation endopeptidase: structure and function
    • Theodoratou E., Huber R., and Böck A. [NiFe]-hydrogenase maturation endopeptidase: structure and function. Biochem Soc Trans 33 (2005) 108-111
    • (2005) Biochem Soc Trans , vol.33 , pp. 108-111
    • Theodoratou, E.1    Huber, R.2    Böck, A.3
  • 22
    • 1942539935 scopus 로고    scopus 로고
    • HybF, a zinc-containing protein involved in NiFe hydrogenase maturation
    • Blokesch M., Rohrmoser M., Rode S., and Böck A. HybF, a zinc-containing protein involved in NiFe hydrogenase maturation. J Bacteriol 186 (2004) 2603-2611
    • (2004) J Bacteriol , vol.186 , pp. 2603-2611
    • Blokesch, M.1    Rohrmoser, M.2    Rode, S.3    Böck, A.4
  • 23
    • 24644474525 scopus 로고    scopus 로고
    • Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB
    • Metal-binding studies of fully reduced HypB from E. coli demonstrate that it possesses a high-affinity Ni(II)-binding site localized to an N-terminal CxxCGC motif, and a weaker metal site involving conserved cysteine and histidine residues located near the catalytically important G3 motif. These results demonstrate that a HypB homolog without a histidine-rich motif binds nickel and supports a metallochaperone role.
    • Leach M.R., Sandal S., Sun H., and Zamble D.B. Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB. Biochemistry 44 (2005) 12229-12238. Metal-binding studies of fully reduced HypB from E. coli demonstrate that it possesses a high-affinity Ni(II)-binding site localized to an N-terminal CxxCGC motif, and a weaker metal site involving conserved cysteine and histidine residues located near the catalytically important G3 motif. These results demonstrate that a HypB homolog without a histidine-rich motif binds nickel and supports a metallochaperone role.
    • (2005) Biochemistry , vol.44 , pp. 12229-12238
    • Leach, M.R.1    Sandal, S.2    Sun, H.3    Zamble, D.B.4
  • 24
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • This X-ray crystal structure of HypB from M. jannaschii shows a HypB dimer with an extensive dimeric interface at the GTPase active site and a dizinc metal site bound to residues corresponding to those identified in E. coli HypB. One of the cysteine ligands is connected to the GTPase switch II region, potentially linking metal binding to the hydrolysis of nucleotide.
    • Gasper R., Scrima A., and Wittinghofer A. Structural insights into HypB, a GTP-binding protein that regulates metal binding. J Biol Chem 281 (2006) 27492-27502. This X-ray crystal structure of HypB from M. jannaschii shows a HypB dimer with an extensive dimeric interface at the GTPase active site and a dizinc metal site bound to residues corresponding to those identified in E. coli HypB. One of the cysteine ligands is connected to the GTPase switch II region, potentially linking metal binding to the hydrolysis of nucleotide.
    • (2006) J Biol Chem , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 25
    • 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. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317 (2002) 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
  • 27
    • 1542304548 scopus 로고    scopus 로고
    • Formation and insertion of the nitrogenase iron-molybdenum cofactor
    • Dos Santos P.C., Dean D.R., Hu Y., and Ribbe M.W. Formation and insertion of the nitrogenase iron-molybdenum cofactor. Chem Rev 104 (2004) 1159-1173
    • (2004) Chem Rev , vol.104 , pp. 1159-1173
    • Dos Santos, P.C.1    Dean, D.R.2    Hu, Y.3    Ribbe, M.W.4
  • 28
    • 14744279761 scopus 로고    scopus 로고
    • Identification of a nitrogenase FeMo cofactor precursor on NifEN complex
    • Hu Y., Fay A.W., and Ribbe M.W. Identification of a nitrogenase FeMo cofactor precursor on NifEN complex. Proc Natl Acad Sci USA 102 (2005) 3236-3241
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3236-3241
    • Hu, Y.1    Fay, A.W.2    Ribbe, M.W.3
  • 29
    • 15744391209 scopus 로고    scopus 로고
    • A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway
    • Tagged HypB was used as bait to pull out the PPIase SlyD, and complex formation was confirmed by using chemical cross-linking. SlyD possesses a metal-binding C-terminal tail and, with the use of knockout cells, was shown to be a novel player in the nickel insertion step of [NiFe]-hydrogenase maturation.
    • Zhang J.W., Butland G., Greenblatt J.F., Emili A., and Zamble D.B. A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway. J Biol Chem 280 (2005) 4360-4366. Tagged HypB was used as bait to pull out the PPIase SlyD, and complex formation was confirmed by using chemical cross-linking. SlyD possesses a metal-binding C-terminal tail and, with the use of knockout cells, was shown to be a novel player in the nickel insertion step of [NiFe]-hydrogenase maturation.
    • (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
  • 30
    • 0030916764 scopus 로고    scopus 로고
    • Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase
    • Hottenrott S., Schumann T., Plückthun A., Fischer G., and Rahfeld J.-U. Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase. J Biol Chem 272 (1997) 15697-15701
    • (1997) J Biol Chem , vol.272 , pp. 15697-15701
    • Hottenrott, S.1    Schumann, T.2    Plückthun, A.3    Fischer, G.4    Rahfeld, J.-U.5
  • 31
    • 30144446085 scopus 로고    scopus 로고
    • SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities
    • Scholz C., Eckert B., Hagn P., Schaarschmidt P., Balbach J., and Schmid F.X. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities. Biochemistry 45 (2006) 20-33
    • (2006) Biochemistry , vol.45 , pp. 20-33
    • Scholz, C.1    Eckert, B.2    Hagn, P.3    Schaarschmidt, P.4    Balbach, J.5    Schmid, F.X.6
  • 32
    • 0029848538 scopus 로고    scopus 로고
    • Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA)
    • Kansau I., Guillain F., Thiberge J.-M., and Labigne A. Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA). Mol Microbiol 22 (1996) 1013-1023
    • (1996) Mol Microbiol , vol.22 , pp. 1013-1023
    • Kansau, I.1    Guillain, F.2    Thiberge, J.-M.3    Labigne, A.4
  • 33
    • 0029070195 scopus 로고
    • Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae
    • Gilbert J.V., Ramakrishna J., Sunderman F.W., Wright A., and Plaut A.G. Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae. Infect Immun 63 (1995) 2682-2688
    • (1995) Infect Immun , vol.63 , pp. 2682-2688
    • Gilbert, J.V.1    Ramakrishna, J.2    Sunderman, F.W.3    Wright, A.4    Plaut, A.G.5
  • 34
    • 3943058946 scopus 로고    scopus 로고
    • The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
    • +-reducing [NiFe]-hydrogenase from R. eutropha with IR spectroscopy indicates that the metallocenter has four CN ligands, one of which is on the nickel atom, and one CO ligand. Selective removal of the nickel-bound cyanide produces an oxygen-sensitive enzyme.
    • +-reducing [NiFe]-hydrogenase from R. eutropha with IR spectroscopy indicates that the metallocenter has four CN ligands, one of which is on the nickel atom, and one CO ligand. Selective removal of the nickel-bound cyanide produces an oxygen-sensitive enzyme.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 616-626
    • Van der Linden, E.1    Burgdorf, T.2    Bernhard, M.3    Bleijlevens, B.4    Friedrich, B.5    Albracht, S.P.J.6
  • 35
    • 8744311816 scopus 로고    scopus 로고
    • The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel
    • +-reducing [NiFe]-hydrogenase and the production of an oxygen-tolerant enzyme.
    • +-reducing [NiFe]-hydrogenase and the production of an oxygen-tolerant enzyme.
    • (2004) J Biol Chem , vol.279 , pp. 46686-46691
    • Bleijlevens, B.1    Buhrke, T.2    van der Linden, E.3    Friedrich, B.4    Albracht, S.P.J.5
  • 36
    • 6344223356 scopus 로고    scopus 로고
    • NiFe hydrogenase active site biosynthesis: identification of Hyp protein complexes in Ralstonia eutropha
    • Jones A.K., Lenz O., Strack A., Buhrke T., and Friedrich B. NiFe hydrogenase active site biosynthesis: identification of Hyp protein complexes in Ralstonia eutropha. Biochemistry 43 (2004) 13467-13477
    • (2004) Biochemistry , vol.43 , pp. 13467-13477
    • Jones, A.K.1    Lenz, O.2    Strack, A.3    Buhrke, T.4    Friedrich, B.5
  • 38
    • 33645784842 scopus 로고    scopus 로고
    • NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase
    • Curatti L., Ludden P.W., and Rubio L.M. NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Proc Natl Acad Sci USA 103 (2006) 5297-5301
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5297-5301
    • Curatti, L.1    Ludden, P.W.2    Rubio, L.M.3
  • 39
    • 0032524072 scopus 로고    scopus 로고
    • Strep-tag II affinity purification: an approach to study intermediates of metalloenzyme biosynthesis
    • Maier T., Drapal N., Thanbichler M., and Böck A. Strep-tag II affinity purification: an approach to study intermediates of metalloenzyme biosynthesis. Anal Biochem 259 (1998) 68-73
    • (1998) Anal Biochem , vol.259 , pp. 68-73
    • Maier, T.1    Drapal, N.2    Thanbichler, M.3    Böck, A.4
  • 41
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • Initial identification of the Hyd accessory proteins for [FeFe] hydrogenase biosynthesis. Heterologous expression of hydEFG genes with the enzyme gene demonstrate that they are sufficient for [FeFe] hydrogenase production in a prokaryotic host.
    • Posewitz M.C., King P.W., Smolinski S.L., Zhang L., Seibert M., and Ghirardi M.L. Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J Biol Chem 279 (2004) 25711-25720. Initial identification of the Hyd accessory proteins for [FeFe] hydrogenase biosynthesis. Heterologous expression of hydEFG genes with the enzyme gene demonstrate that they are sufficient for [FeFe] hydrogenase production in a prokaryotic host.
    • (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
  • 42
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • Rubach J.K., Brazzolotto X., Gaillard J., and Fontecave M. Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima. FEBS Lett 579 (2005) 5055-5060
    • (2005) FEBS Lett , vol.579 , pp. 5055-5060
    • Rubach, J.K.1    Brazzolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 43
    • 33644852344 scopus 로고    scopus 로고
    • The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster
    • Brazzolotto X., Rubach J.K., Gaillard J., Gambarelli S., Atta M., and Fontecave M. The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster. J Biol Chem 281 (2006) 769-774
    • (2006) J Biol Chem , vol.281 , pp. 769-774
    • Brazzolotto, X.1    Rubach, J.K.2    Gaillard, J.3    Gambarelli, S.4    Atta, M.5    Fontecave, M.6
  • 44
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • King P.W., Posewitz M.C., Ghirardi M.L., and Seibert M. Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system. J Bacteriol 188 (2006) 2163-2172
    • (2006) J Bacteriol , vol.188 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 45
    • 30644471959 scopus 로고    scopus 로고
    • A radical solution for the biosynthesis of the H-cluster of hydrogenase
    • An interesting discussion of potential mechanisms for the complete biosynthesis of the [FeFe] dinuclear cluster.
    • Peters J.W., Szilagyi R.K., Naumov A., and Douglas T. A radical solution for the biosynthesis of the H-cluster of hydrogenase. FEBS Lett 580 (2006) 363-367. An interesting discussion of potential mechanisms for the complete biosynthesis of the [FeFe] dinuclear cluster.
    • (2006) FEBS Lett , vol.580 , pp. 363-367
    • Peters, J.W.1    Szilagyi, R.K.2    Naumov, A.3    Douglas, T.4
  • 47
    • 0035902555 scopus 로고    scopus 로고
    • Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion
    • Ugulava N.B., Sacanell C.J., and Jarrett J.T. Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion. Biochemistry 40 (2001) 8352-8358
    • (2001) Biochemistry , vol.40 , pp. 8352-8358
    • Ugulava, N.B.1    Sacanell, C.J.2    Jarrett, J.T.3
  • 48
    • 13244284641 scopus 로고    scopus 로고
    • The structure of the TrmE GTP-binding protein and its implications for tRNA modification
    • Scrima A., Vetter I.R., Armengod M.E., and Wittinghofer A. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J 24 (2005) 23-33
    • (2005) EMBO J , vol.24 , pp. 23-33
    • Scrima, A.1    Vetter, I.R.2    Armengod, M.E.3    Wittinghofer, A.4
  • 49
    • 4644221775 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism
    • Mansy S.S., and Cowan J.A. Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism. Acc Chem Res 37 (2004) 719-725
    • (2004) Acc Chem Res , vol.37 , pp. 719-725
    • Mansy, S.S.1    Cowan, J.A.2
  • 50
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D.C., Dean D.R., Smith A.D., and Johnson M.K. Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74 (2005) 247-281
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 52
    • 26444605816 scopus 로고    scopus 로고
    • Gene products of the hupGHIJ operon are involved in maturation of the iron-sulfur subunit of the [NiFe] hydrogenase from Rhizobium leguminosarum bv. viciae
    • Manyani H., Rey L., Palacios J.M., Imperial J., and Ruiz-Argüeso T. Gene products of the hupGHIJ operon are involved in maturation of the iron-sulfur subunit of the [NiFe] hydrogenase from Rhizobium leguminosarum bv. viciae. J Bacteriol 187 (2005) 7018-7026
    • (2005) J Bacteriol , vol.187 , pp. 7018-7026
    • Manyani, H.1    Rey, L.2    Palacios, J.M.3    Imperial, J.4    Ruiz-Argüeso, T.5
  • 53
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins
    • Dubini A., and Sargent F. Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Lett 549 (2003) 141-146
    • (2003) FEBS Lett , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 54
    • 33846043578 scopus 로고    scopus 로고
    • A dynamic Zn site in Helicobacter pylori HypA: a potential mechanism for metal-specific protein activity
    • Kennedy D.C., Herbst R.W., Iwig J.S., Chivers P.T., and Maroney M.J. A dynamic Zn site in Helicobacter pylori HypA: a potential mechanism for metal-specific protein activity. JACS 129 (2007) 16-17
    • (2007) JACS , vol.129 , pp. 16-17
    • Kennedy, D.C.1    Herbst, R.W.2    Iwig, J.S.3    Chivers, P.T.4    Maroney, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.