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Volumn 31, Issue 3-4, 2010, Pages 144-152

Hydrogenase active sites: A new paradigm for natural product-inspired synthesis based on organometallic chemistry

Author keywords

Hydrogenase; Organoiron; Small molecule models; Synthetic analogues

Indexed keywords


EID: 78649599681     PISSN: 02603594     EISSN: 15489574     Source Type: Journal    
DOI: 10.1080/02603594.2010.517463     Document Type: Article
Times cited : (10)

References (22)
  • 1
    • 78649574675 scopus 로고
    • Leaving No Stone Unturned: Pathways In Organometallic Chemistry
    • Washington, DC
    • Stone, F. Gordon A. 1993. Leaving No Stone Unturned: Pathways In Organometallic Chemistry, American Chemical Society, Washington, DC. 2.
    • (1993) American Chemical Society , pp. 2
    • Stone, F.G.A.1
  • 2
    • 77952832586 scopus 로고    scopus 로고
    • Organometallic chemistry of B12 coenzymes
    • Metal-Carbon Bonds in Enzymes and Cofactors, Astrid, Sigel, Helmut, Sigel, and Roland K. O. Sigel (eds.), The Royal Society of Chemistry, Cambridge, UK
    • Krautler, Bernhard. 2009. Organometallic chemistry of B12 coenzymes. In Metal Ions in Life Sciences, Vol. 6: Metal-Carbon Bonds in Enzymes and Cofactors, Astrid, Sigel, Helmut, Sigel, and Roland K. O. Sigel (eds.), p. 1-51, The Royal Society of Chemistry, Cambridge, UK.
    • (2009) Metal Ions In Life Sciences , vol.6 , pp. 1-51
    • Krautler, B.1
  • 3
    • 77949846558 scopus 로고    scopus 로고
    • The Royal Society of Chemistry, Cambridge, UK
    • Matthews, Rowena G. 2009. Cobalamin- and corrinoid-dependent enzymes. In Metal Ions in Life Sciences, Vol. 6: Metal-Carbon Bonds in Enzymes and Cofactors, Astrid, Sigel, Helmut, Sigel and Roland K. O. Sigel (eds.), p. 53-114, The Royal Society of Chemistry, Cambridge, UK.
    • (2009) Cobalamin- and Corrinoid-dependent Enzymes Metal Ions In Life Sciences , vol.6 , pp. 53-114
    • Matthews, R.G.1
  • 4
    • 0028048410 scopus 로고
    • Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from chromatium vinosum
    • Bagley, Kimberly A., Carla J. Van Garderen, Min Chen, William H. Woodruff, Evert C. Duin, and Simon P. J. Albracht. 1994. Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from chromatium vinosum. Biochemistry, 33: 9229-9236.
    • (1994) Biochemistry , vol.33 , pp. 9229-9236
    • Bagley, K.A.1    van Garderen, C.J.2    Chen, M.3    Woodruff, W.H.4    Duin, E.C.5    Albracht, S.P.J.6
  • 6
    • 0028889166 scopus 로고
    • Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
    • Volbeda, Anne, Marie-Helene Charon, Claudine Piras, E. Claude Hatchikian, Michel Frey, and Juan C. Fontecilla-Camps. 1995. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature, 373: 580-587.
    • (1995) Nature , vol.373 , pp. 580-587
    • Volbeda, A.1    Marie-Helene, C.2    Piras, C.3    Claude, H.E.4    Frey, M.5    Fontecilla-Camps, J.C.6
  • 7
    • 0031180380 scopus 로고    scopus 로고
    • Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
    • Montet, Yael, Patricia Amara, Anne Volbeda, Xavier Vernede, E. Claude Hatchikian, Martin J. Field, Michel Frey, and Juan C. Fontecilla-Camps. 1997. Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics. Nat. Struct. Biol., 4: 523-526.
    • (1997) Nat. Struct Biol , vol.4 , pp. 523-526
    • Montet, Y.1    Amara, P.2    Volbeda, A.3    Vernede, X.4    Claude, H.E.5    Field, M.J.6    Frey, M.7    Fontecilla-Camps, J.C.8
  • 8
    • 0030884784 scopus 로고    scopus 로고
    • Analysis of an organometallic iron site model for the heterodimetallic unit of [NiFe]-hydrogenase
    • Darensbourg, Donald J., Joseph H. Reibenspies, Chia-Huei Lai, Way-Zen Lee, and Marcetta Y. Darensbourg. 1997. Analysis of an organometallic iron site model for the heterodimetallic unit of [NiFe]-hydrogenase. J. Am. Chem. Soc., 119: 7903-7904.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 7903-7904
    • Darensbourg, D.J.1    Reibenspies, J.H.2    Lai, C.-H.3    Lee, W.-Z.4    Darensbourg, M.Y.5
  • 9
    • 0032494399 scopus 로고    scopus 로고
    • 2(CO) unit to electronic changes as related to its role in [NiFe]-hydrogenase
    • Lai, Chia-Huei, Way-Zen Lee, Matthew L. Miller, Joseph H. Reibenspies, Donald J. Darensbourg, and Marcetta Y. Darensbourg. 1998. Responses of the Fe(CN)2(CO) unit to electronic changes as related to its role in [NiFe]-hydrogenase. J. Am. Chem. Soc., 120: 10103-10114.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 10103-10114
    • Lai, C.-H.1    Lee, W.-Z.2    Miller, M.L.3    Reibenspies, J.H.4    Darensbourg, D.J.5    Darensbourg, M.Y.6
  • 10
    • 35748930865 scopus 로고    scopus 로고
    • Structure=function relationships of [NiFe]- and [FeFe]- hydrogenases
    • Fontecilla-Camps, Juan C., Anne Volbeda, Christine Cavazza, and Yvain Nicolet. 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
  • 13
    • 34047241285 scopus 로고    scopus 로고
    • 2 activation
    • Shima, Seigo and Rolf K. Thauer. 2007. A third type of hydrogenase catalyzing H2 activation. Chem. Rec., 7: 37-46
    • (2007) Chem. Rec , vol.7 , pp. 37-46
    • Shima, S.1    Thauer, R.K.2
  • 14
    • 58949101261 scopus 로고    scopus 로고
    • The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex
    • Hiromoto, Takeshi, Kenichi Ataka, Oliver Pilak, Sonja Vogt, Marco Salomone Stagni, Wolfram Meyer-Klaucke, Eberhard Warkentin, Rudolf K. Thauer, Seigo Shima, and Ulrich Ermler. 2009. The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Letters, 583: 585-590
    • (2009) FEBS Letters , vol.583 , pp. 585-590
    • Hiromoto, T.1    Ataka, K.2    Pilak, O.3    Vogt, S.4    Stagni, M.S.5    Meyer-Klaucke, W.6    Warkentin, E.7    Thauer, R.K.8    Shima, S.9    Ermler, U.10
  • 16
    • 76149108206 scopus 로고    scopus 로고
    • Synthesis and reactivity of iron acyl complexes modeling the active site of [Fe]-hydrogenase
    • Chen, Dafa, Rosario Scopelliti, and Xile Hu. 2010. Synthesis and reactivity of iron acyl complexes modeling the active site of [Fe]-hydrogenase. J. Am. Chem. Soc., 132: 928-929.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 928-929
    • Chen, D.1    Scopelliti, R.2    Xile, H.3
  • 17
    • 67650280684 scopus 로고    scopus 로고
    • Oxidative addition to thioesters to iron(0): Active-site models for hmd, nature's third hydrogenase
    • Royer, Aaron M., Thomas B. Rauchfuss, and Danielle L. Gray. 2009. Oxidative addition to thioesters to iron(0): Active-site models for hmd, nature's third hydrogenase. Organometallics, 28: 3618-3620.
    • (2009) Organometallics , vol.28 , pp. 3618-3620
    • Royer, A.M.1    Rauchfuss, T.B.2    Gray, D.L.3
  • 18
    • 77957575808 scopus 로고    scopus 로고
    • The third hydrogenase: A ferracyclic carba- moyl with close structural analogy to the active site of hmd
    • Ed., (in press)
    • Turrell, Peter J., Joseph A. Wright, Jamie N. T. Peck, Vasily S. Oganesyan, and Christopher J. Pickett. 2010. The third hydrogenase: a ferracyclic carba-moyl with close structural analogy to the active site of hmd. Angew. Chem. Int. Ed., (in press).
    • (2010) Angew. Chem. Int
    • Turrell, P.J.1    Joseph A.W.Jamie, N.T.2    Peck, V.S.O.3    Christopher, J.P.4
  • 19
    • 0034716327 scopus 로고    scopus 로고
    • Dinuclear and mononuclear iron(II)-thiolate complexes with mixed CO=CN- ligands: Synthetic advances for iron sites of [Fe]-only hydrogenases
    • Liaw, Wen-Feng, Nan-Hung Lee, Chien-Hong Chen, Chien-Ming Lee, Gene-Hsiang Lee, and Shie-Ming Peng. 2000. Dinuclear and mononuclear iron(II)-thiolate complexes with mixed CO=CN- ligands: synthetic advances for iron sites of [Fe]-only hydrogenases. J. Am. Chem. Soc., 122: 488-494.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 488-494
    • Liaw, W.-F.1    Lee, N.-H.2    Chen, C.-H.3    Lee, C.-M.4    Gene-Hsiang, L.5    Shie-Ming, P.6
  • 20
    • 0035904392 scopus 로고    scopus 로고
    • Experimental evidence for the noninnocence of o- aminothiophenolates: Coordination chemistry of o-iminothionebenzosemi- quinonate(1-) p-radicals with Ni(II), Pd(II), Pt(II)
    • Herebian, Diran, Eberhard Bothe, Eckhard Bill, Thomas Weyhermuller, and Karl Wieghardt. 2001. Experimental evidence for the noninnocence of o- aminothiophenolates: Coordination chemistry of o-iminothionebenzosemi- quinonate(1-) p-radicals with Ni(II), Pd(II), Pt(II). J. Am. Chem. Soc., 123: 10012-10023.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 10012-10023
    • Herebian, D.1    Bothe, E.2    Bill, E.3    Weyhermuller, T.4    Wieghardt, K.5
  • 21
    • 77649209702 scopus 로고    scopus 로고
    • Analysis of a penta- coordinate iron dicarbonyl as synthetic analogue of the hmd or mono-iron hydrogenase active site
    • Liu, Tianbiao, Bin Li, Codrina V. Popescu, Andrey Bilko, Lisa M. Pérez, Michael B. Hall, and Marcetta Y. Darensbourg. 2010. Analysis of a penta- coordinate iron dicarbonyl as synthetic analogue of the hmd or mono-iron hydrogenase active site. Chem A Eur. Journal, 16: 3083-3089.
    • (2010) Chem a Eur. Journal , vol.16 , pp. 3083-3089
    • Liu, T.1    Li, B.2    Popescu, C.V.3    Bilko, A.4    Pérez, L.M.5    Hall, M.B.6    Darensbourg, M.Y.7
  • 22
    • 77954307688 scopus 로고    scopus 로고
    • A cyclodextrin host=guest approach to a hydrogenase active site biomimetic cavity
    • Singleton, Michael L., Joseph H. Reibenspies, and Marcetta Y. Darensbourg. 2010. A cyclodextrin host=guest approach to a hydrogenase active site biomimetic cavity. J. Am. Chem. Soc., 132: 8870-8871.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 8870-8871
    • Singleton, M.L.1    Reibenspies, J.H.2    Darensbourg, M.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.