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Volumn 580, Issue 2, 2006, Pages 363-367

A radical solution for the biosynthesis of the H-cluster of hydrogenase

Author keywords

H cluster biosynthesis; Hydrogenase; Prebiotic chemistry; Radical SAM

Indexed keywords

CARBON MONOXIDE; CYANIDE; GLYCINE; HYDROGENASE; IRON; S ADENOSYLMETHIONINE;

EID: 30644471959     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.12.040     Document Type: Article
Times cited : (69)

References (36)
  • 1
    • 0034886919 scopus 로고    scopus 로고
    • Meyer J: Classification and phylogeny of hydrogenases
    • P.M. Vignais, and B. Billoud 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
  • 2
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • M.W. Adams The structure and mechanism of iron-hydrogenases Biochim. Biophys. Acta 1020 1990 115 145
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.1
  • 3
    • 0002987888 scopus 로고
    • Interaction between H2-producing and methane-producing species
    • H. Schelgel G. Gottschalk N. Pfennig Akademie der Wissenshaften
    • M. Wolin Interaction between H2-producing and methane-producing species H. Schelgel G. Gottschalk N. Pfennig Microbial Production and Utlization of Gases 1976 Akademie der Wissenshaften 141 150
    • (1976) Microbial Production and Utlization of Gases , pp. 141-150
    • Wolin, M.1
  • 4
    • 0033956391 scopus 로고    scopus 로고
    • Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha
    • R.P. Happe, and W. Roseboom Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha FEBS Lett. 466 2000 259 263
    • (2000) FEBS Lett. , vol.466 , pp. 259-263
    • Happe, R.P.1    Roseboom, W.2
  • 5
    • 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
    • A.J. Pierik, and M. Hulstein 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 1998 572 578
    • (1998) Eur. J. Biochem. , vol.258 , pp. 572-578
    • Pierik, A.J.1    Hulstein, M.2
  • 6
    • 0028889166 scopus 로고
    • Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
    • A. Volbeda, and M.H. Charon Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas Nature 373 1995 580 587
    • (1995) Nature , vol.373 , pp. 580-587
    • Volbeda, A.1    Charon, M.H.2
  • 7
    • 0037173571 scopus 로고    scopus 로고
    • Fe-only hydrogenases: Structure, function and evolution
    • Y. Nicolet, and C. Cavazza Fe-only hydrogenases: structure, function and evolution J. Inorg. Biochem. 91 2002 1 8
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 1-8
    • Nicolet, Y.1    Cavazza, C.2
  • 8
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Y. Nicolet, and C. Piras Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center Struct. Fold. Des. 7 1999 13 23
    • (1999) Struct. Fold. Des. , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2
  • 9
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase CpI from Clostridium pasteurianum to 1.8 angstrom resolution
    • J.W. Peters, and W.N. Lanzilotta X-ray crystal structure of the Fe-only hydrogenase CpI from Clostridium pasteurianum to 1.8 angstrom resolution Science 282 1998 1853 1858
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2
  • 10
    • 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
    • Y. Nicolet, and A.L. de Lacey 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 2001 1596 1601
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1596-1601
    • Nicolet, Y.1    De Lacey, A.L.2
  • 11
    • 0346890205 scopus 로고    scopus 로고
    • Taming of a poison: Biosynthesis of the NiFe-hydrogenase cyanide ligands
    • S. Reissmann, and E. Hochleitner Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands Science 299 2003 1067 1070
    • (2003) Science , vol.299 , pp. 1067-1070
    • Reissmann, S.1    Hochleitner, E.2
  • 12
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • M.C. Posewitz, and P.W. King Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase J. Biol. Chem. 279 2004 25711 25720
    • (2004) J. Biol. Chem. , vol.279 , pp. 25711-25720
    • Posewitz, M.C.1    King, P.W.2
  • 13
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • J.K. Rubach, and X. Brazzolotto 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
  • 14
    • 0035478116 scopus 로고    scopus 로고
    • Adenosylmethionine as a source of 5′-deoxyadenosyl radicals
    • M. Fontecave, and E. Mulliez Adenosylmethionine as a source of 5′-deoxyadenosyl radicals Curr. Opin. Chem. Biol. 5 2001 506 511
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 506-511
    • Fontecave, M.1    Mulliez, E.2
  • 15
    • 0034912671 scopus 로고    scopus 로고
    • Radical mechanisms of enzymatic catalysis
    • P.A. Frey Radical mechanisms of enzymatic catalysis Annu. Rev. Biochem. 2001 70 2004 121 148
    • (2004) Annu. Rev. Biochem. 2001 , vol.70 , pp. 121-148
    • Frey, P.A.1
  • 16
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • H.J. Sofia, and G. Chen Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods Nucleic Acids Res. 29 2001 1097 1106
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2
  • 17
    • 0037174377 scopus 로고    scopus 로고
    • An anchoring role for FeS clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme
    • C.J. Walsby, and D. Ortillo An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme J. Am. Chem. Soc. 124 2002 11270 11271
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2
  • 18
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein
    • J.R. Miller, and R.W. Busby Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein Biochemistry 39 2000 15166 15178
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1    Busby, R.W.2
  • 19
    • 0030759916 scopus 로고    scopus 로고
    • [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase
    • E.C. Duin, and M.E. Lafferty [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase Biochemistry 36 1997 11811 11820
    • (1997) Biochemistry , vol.36 , pp. 11811-11820
    • Duin, E.C.1    Lafferty, M.E.2
  • 20
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form
    • R. Kulzer, and T. Pils Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form J. Biol. Chem. 273 1998 4897 4903
    • (1998) J. Biol. Chem. , vol.273 , pp. 4897-4903
    • Kulzer, R.1    Pils, T.2
  • 21
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • R.M. Cicchillo, and S.J. Booker Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide J. Am. Chem. Soc. 127 2005 2860 2861
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 22
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • D.C. Johnson, and D.R. Dean 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
  • 23
    • 0027953134 scopus 로고
    • Biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • R.M. Allen, and R. Chatterjee Biosynthesis of the iron-molybdenum cofactor of nitrogenase Crit. Rev. Biotechnol. 14 1994 225 249
    • (1994) Crit. Rev. Biotechnol. , vol.14 , pp. 225-249
    • Allen, R.M.1    Chatterjee, R.2
  • 24
    • 23644437690 scopus 로고    scopus 로고
    • DFT investigations of models related to the active site of [NiFe] and [Fe] hydrogenases
    • M. Bruschi, and G. Zampella DFT investigations of models related to the active site of [NiFe] and [Fe] hydrogenases Coord. Chem. Rev. 249 2005 1620 1640
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 1620-1640
    • Bruschi, M.1    Zampella, G.2
  • 25
    • 0038670391 scopus 로고    scopus 로고
    • Fundamental properties of small molecule models of Fe-only hydrogenase: Computations relative to the definition of an entatic state in the active site
    • I.P. Georgakaki, and L.M. Thomson Fundamental properties of small molecule models of Fe-only hydrogenase: computations relative to the definition of an entatic state in the active site Coord. Chem.Rev. 238 2003 255 266
    • (2003) Coord. Chem.Rev. , vol.238 , pp. 255-266
    • Georgakaki, I.P.1    Thomson, L.M.2
  • 26
    • 0037044954 scopus 로고    scopus 로고
    • Mechanism of H-2 metabolism on Fe-only hydrogenases
    • Z.P. Liu, and P. Hu Mechanism of H-2 metabolism on Fe-only hydrogenases J. Chem. Phys. 117 2002 8177 8180
    • (2002) J. Chem. Phys. , vol.117 , pp. 8177-8180
    • Liu, Z.P.1    Hu, P.2
  • 27
    • 22544445555 scopus 로고    scopus 로고
    • Density functional study on dihydrogen activation at the H cluster in Fe-only hydrogenases
    • T.J. Zhou, and Y.R. Mo Density functional study on dihydrogen activation at the H cluster in Fe-only hydrogenases Inorg. Chem. 44 2005 4941 4946
    • (2005) Inorg. Chem. , vol.44 , pp. 4941-4946
    • Zhou, T.J.1    Mo, Y.R.2
  • 28
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • A.D. Becke Density-functional exchange-energy approximation with correct asymptotic behavior Phys. Rev. A 38 1988 3098 3100
    • (1988) Phys. Rev. a , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 29
    • 5944261746 scopus 로고
    • Density-functional approximation for the correlation energy of the inhomogeneous electron gas
    • J.P. Perdew Density-functional approximation for the correlation energy of the inhomogeneous electron gas Phys. Rev. B 33 1986 8822 8824
    • (1986) Phys. Rev. B , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 30
    • 0006073669 scopus 로고
    • Ab initio effective core potentials for molecular calculations. Potentials for the transition metal atoms Na to Bi
    • W.R. Wadt, and P.J. Hay Ab initio effective core potentials for molecular calculations. Potentials for the transition metal atoms Na to Bi J. Chem. Phys. 82 1985 284 298
    • (1985) J. Chem. Phys. , vol.82 , pp. 284-298
    • Wadt, W.R.1    Hay, P.J.2
  • 32
    • 11744256643 scopus 로고
    • Molecular interactions in solution: An overview of methods based on continuous distributions of the solvent
    • J. Tomasi, and M. Persico Molecular interactions in solution: an overview of methods based on continuous distributions of the solvent Chem. Rev. 94 1994 2027 2094
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Persico, M.2
  • 33
    • 0034714224 scopus 로고    scopus 로고
    • Primordial carbonylated iron-sulfur compounds and the synthesis of pyruvate
    • G.D. Cody, and N.Z. Boctor Primordial carbonylated iron-sulfur compounds and the synthesis of pyruvate Science 289 2000 1337 1340
    • (2000) Science , vol.289 , pp. 1337-1340
    • Cody, G.D.1    Boctor, N.Z.2
  • 34
    • 0038649226 scopus 로고    scopus 로고
    • A possible prebiotic formation of ammonia from dinitrogen on iron sulfide surfaces
    • M. Dorr, and J. Kassbohrer A possible prebiotic formation of ammonia from dinitrogen on iron sulfide surfaces Angew. Chem. Int. Ed. 42 2003 1540 1543
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 1540-1543
    • Dorr, M.1    Kassbohrer, J.2
  • 35
    • 0026444704 scopus 로고
    • Groundworks for an evolutionary biochemistry: The iron-sulphur world
    • G. Wachtershauser Groundworks for an evolutionary biochemistry: the iron-sulphur world Prog. Biophys. Mol. Biol. 58 1992 85 201
    • (1992) Prog. Biophys. Mol. Biol. , vol.58 , pp. 85-201
    • Wachtershauser, G.1
  • 36
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • F. Berkovitch, and Y. Nicolet Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme Science 303 2004 76 79
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2


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