메뉴 건너뛰기




Volumn 48, Issue 5, 2009, Pages 1056-1066

An autocatalytic mechanism for NiFe-hydrogenase: Reduction to Ni(I) followed by oxidative addition

Author keywords

[No Author keywords available]

Indexed keywords

[NIFE]-HYDROGENASE; AUTOCATALYTIC; CATALYTIC TURNOVERS; ELECTROSTATIC INTERACTIONS; FORCE FIELDS; HETEROLYTIC CLEAVAGES; HYBRID DFT; ONIOM APPROACHES; OXIDATION STATE; OXIDATIVE ADDITIONS; POLARIZATION EFFECTS; REACTION MECHANISMS;

EID: 61449143522     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801218n     Document Type: Article
Times cited : (88)

References (50)
  • 1
    • 0026814596 scopus 로고
    • Structure-Function Relationships among the Nickel-Containing Hydrogenases
    • Przbyla, A. E., Robbins, J., Menon, N., and Peck, H. D. (1992) Structure-Function Relationships among the Nickel-Containing Hydrogenases. FEMS Microbiol. Rev. 88, 109-113.
    • (1992) FEMS Microbiol. Rev , vol.88 , pp. 109-113
    • Przbyla, A.E.1    Robbins, J.2    Menon, N.3    Peck, H.D.4
  • 3
    • 0021826804 scopus 로고
    • Electron-Paramagnetic Resonance Studies on the Mechanism of Activation and the Catalytic Cycle of the Nickel-Containing Hydrogenase from Desulfovibrio gigas
    • Teixeira, M., Moura, I., Xavier, A. V., Huynh, B. H., DerVartanian, D. V., Peck, H. D., Jr., LeGall, J., and Moura, J. J. G. (1985) Electron-Paramagnetic Resonance Studies on the Mechanism of Activation and the Catalytic Cycle of the Nickel-Containing Hydrogenase from Desulfovibrio gigas. J. Biol. Chem. 260, 8942-8950.
    • (1985) J. Biol. Chem , vol.260 , pp. 8942-8950
    • Teixeira, M.1    Moura, I.2    Xavier, A.V.3    Huynh, B.H.4    DerVartanian, D.V.5    Peck Jr., H.D.6    LeGall, J.7    Moura, J.J.G.8
  • 5
    • 0032804337 scopus 로고    scopus 로고
    • Structure and Mechanism of Iron-Only Hydrogenases
    • Peters, J. W. (1999) Structure and Mechanism of Iron-Only Hydrogenases. Curr. Opin. Struct. Biol. 9, 670-676.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 670-676
    • Peters, J.W.1
  • 6
    • 1642580510 scopus 로고    scopus 로고
    • UV-A/Blue-Light Inactivation of the 'Metal-Free' Hydrogenase (Hmd) from Methanogenic Archaea: The Enzyme Contains Functional Iron after All
    • Lyon, E. J., Shima, S., Buurman, G., Chowdhuri, S., Batschauer, A., Steinbach, K., and Thauer, R. K. (2004) UV-A/Blue-Light Inactivation of the 'Metal-Free' Hydrogenase (Hmd) from Methanogenic Archaea: The Enzyme Contains Functional Iron after All. Eur. J. Biochem. 271, 195-204.
    • (2004) Eur. J. Biochem , vol.271 , pp. 195-204
    • Lyon, E.J.1    Shima, S.2    Buurman, G.3    Chowdhuri, S.4    Batschauer, A.5    Steinbach, K.6    Thauer, R.K.7
  • 7
    • 0028795716 scopus 로고
    • On the Mechanism of Catalysis by a Metal-Free Hydrogenase from Methanogenic Archaea: Enzymatic Transformation of H-2 without a Metal and Its Analogy to the Chemistry of Alkanes in Superacidic Solution
    • Berkessel, A., and Thauer, R. K. (1995) On the Mechanism of Catalysis by a Metal-Free Hydrogenase from Methanogenic Archaea: Enzymatic Transformation of H-2 without a Metal and Its Analogy to the Chemistry of Alkanes in Superacidic Solution. Angew. Chem., Int. Ed. 34, 2247-2250.
    • (1995) Angew. Chem., Int. Ed , vol.34 , pp. 2247-2250
    • Berkessel, A.1    Thauer, R.K.2
  • 8
    • 0000739582 scopus 로고    scopus 로고
    • Thauer, R. K., Klein, A. R., and Hartmann, G. C. (1996) Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst. Chem. Rev. 96, 3031-3042.
    • Thauer, R. K., Klein, A. R., and Hartmann, G. C. (1996) Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst. Chem. Rev. 96, 3031-3042.
  • 9
    • 7444269837 scopus 로고    scopus 로고
    • Carbon Monoxide as an Intrinsic Ligand to Iron in the Active Site of the Iron-Sulfur-Cluster-Free Hydrogenase H-2-Forming Methylene-tetrahydromethanopterin Dehydrogenase As Revealed by Infrared Spectroscopy
    • Lyon, E. J., Shima, S., Boecher, R., Thauer, R. K., Grevels, F.-W., Bill, E., Roseboom, W., and Albracht, S. P. J. (2004) Carbon Monoxide as an Intrinsic Ligand to Iron in the Active Site of the Iron-Sulfur-Cluster-Free Hydrogenase H-2-Forming Methylene-tetrahydromethanopterin Dehydrogenase As Revealed by Infrared Spectroscopy. J. Am. Chem. Soc. 126, 14239-14248.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 14239-14248
    • Lyon, E.J.1    Shima, S.2    Boecher, R.3    Thauer, R.K.4    Grevels, F.-W.5    Bill, E.6    Roseboom, W.7    Albracht, S.P.J.8
  • 10
    • 0033768628 scopus 로고    scopus 로고
    • Characterization of the Hydrogen-Deuterium Exchange Activities of the Energy-Transducing Hupsl Hydrogenase and H-2-Signaling Hupuv Hydrogenase in Rhodobacter capsulatus
    • Vignais, P. M., Dimon, B., Zorin, N. A., Tomiyama, M., and Colbeau, A. A. (2000) Characterization of the Hydrogen-Deuterium Exchange Activities of the Energy-Transducing Hupsl Hydrogenase and H-2-Signaling Hupuv Hydrogenase in Rhodobacter capsulatus. J. Bacteriol. 182, 5997-6004.
    • (2000) J. Bacteriol , vol.182 , pp. 5997-6004
    • Vignais, P.M.1    Dimon, B.2    Zorin, N.A.3    Tomiyama, M.4    Colbeau, A.A.5
  • 11
    • 0035844249 scopus 로고    scopus 로고
    • The H-2 Sensor of Ralstonia eutropha: Biochemical Characteristics, Spectroscopic Properties, and Its Interaction with a Histidine Protein Kinase
    • Bernhard, M., Buhrke, T., Bleijlevens, B., De Lacey, A. L., Fernandez, V. M., Albracht, S. P. J., and Friedrich, B. (2001) The H-2 Sensor of Ralstonia eutropha: Biochemical Characteristics, Spectroscopic Properties, and Its Interaction with a Histidine Protein Kinase. J. Biol. Chem. 276, 15592-15597.
    • (2001) J. Biol. Chem , vol.276 , pp. 15592-15597
    • Bernhard, M.1    Buhrke, T.2    Bleijlevens, B.3    De Lacey, A.L.4    Fernandez, V.M.5    Albracht, S.P.J.6    Friedrich, B.7
  • 12
    • 35748956722 scopus 로고    scopus 로고
    • Activation and inactivation of hydrogenase function and the catalytic cycle: Spectroelectrochemical studies
    • De Lacey, A. L., Fernandez, V. M., Rousset, M., and Cammack, R. (2007) Activation and inactivation of hydrogenase function and the catalytic cycle: Spectroelectrochemical studies. Chem. Rev. 107, 4304-4330.
    • (2007) Chem. Rev , vol.107 , pp. 4304-4330
    • De Lacey, A.L.1    Fernandez, V.M.2    Rousset, M.3    Cammack, R.4
  • 13
    • 20744457727 scopus 로고    scopus 로고
    • NiFe]-hydrogenases: Spectroscopic and electrochemical definition of reactions and intermediates
    • Armstrong, F. A., and Albracht, S. P. J. (2005) [NiFe]-hydrogenases: Spectroscopic and electrochemical definition of reactions and intermediates. Philos. Trans. R. Soc. London, Ser. A 363, 937-954.
    • (2005) Philos. Trans. R. Soc. London, Ser. A , vol.363 , pp. 937-954
    • Armstrong, F.A.1    Albracht, S.P.J.2
  • 14
    • 0142152415 scopus 로고    scopus 로고
    • Direct Detection of a Hydrogen Ligand in the [NiFe] Center of the Regulatory H-2-Sensing Hydrogenase from Ralstonia eutropha in Its Reduced State by HYSCORE and ENDOR Spectroscopy
    • Brecht, M., van Gastel, M., Buhrke, T., Friedrich, B., and Lubitz, W. (2003) Direct Detection of a Hydrogen Ligand in the [NiFe] Center of the Regulatory H-2-Sensing Hydrogenase from Ralstonia eutropha in Its Reduced State by HYSCORE and ENDOR Spectroscopy. J. Am. Chem. Soc. 125, 13075.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 13075
    • Brecht, M.1    van Gastel, M.2    Buhrke, T.3    Friedrich, B.4    Lubitz, W.5
  • 15
    • 0037425515 scopus 로고    scopus 로고
    • Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfiovibrio vulgaris Miyazaki F
    • Foerster, S., Stein, M., Brecht, M., Ogata, H., Higuchi, Y., and Lubitz, W. (2003) Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfiovibrio vulgaris Miyazaki F. J. Am. Chem. Soc. 125, 83-93.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 83-93
    • Foerster, S.1    Stein, M.2    Brecht, M.3    Ogata, H.4    Higuchi, Y.5    Lubitz, W.6
  • 16
    • 12944326891 scopus 로고    scopus 로고
    • An Orientation-Selected ENDOR and HYSCORE Study of the Ni-C Active State of Desulfovibrio vulgaris Miyazaki F Hydrogenase
    • Foerster, S., van Gastel, M., Brecht, M., and Lubitz, W. (2005) An Orientation-Selected ENDOR and HYSCORE Study of the Ni-C Active State of Desulfovibrio vulgaris Miyazaki F Hydrogenase. J. Biol. Inorg. Chem. 10, 51.
    • (2005) J. Biol. Inorg. Chem , vol.10 , pp. 51
    • Foerster, S.1    van Gastel, M.2    Brecht, M.3    Lubitz, W.4
  • 18
    • 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
  • 19
    • 0037009993 scopus 로고    scopus 로고
    • Structural Studies of the Carbon Monoxide Complex of [NiFe]Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the Initial Activation Site for Dihydrogen
    • Ogata, H., Mizoguchi, Y., Mizuno, N., Miki, K., Adachi, S.-I., Yasuoka, N, Yagi, T., Yamauchi, O., Hirota, S., and Higuchi, Y. (2002) Structural Studies of the Carbon Monoxide Complex of [NiFe]Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the Initial Activation Site for Dihydrogen. J. Am. Chem. Soc. 124, 11628-11635.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 11628-11635
    • Ogata, H.1    Mizoguchi, Y.2    Mizuno, N.3    Miki, K.4    Adachi, S.-I.5    Yasuoka, N.6    Yagi, T.7    Yamauchi, O.8    Hirota, S.9    Higuchi, Y.10
  • 21
    • 27644552110 scopus 로고    scopus 로고
    • Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-ray Analyses: Conversion of the Ready to the Unready State
    • Ogata, H., Hirota, S., Nakahara, A., Komori, H., Shibata, N., Kato, T., Kano, K., and Higuchi, Y. (2005) Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-ray Analyses: Conversion of the Ready to the Unready State. Structure 13, 1635-1642.
    • (2005) Structure , vol.13 , pp. 1635-1642
    • Ogata, H.1    Hirota, S.2    Nakahara, A.3    Komori, H.4    Shibata, N.5    Kato, T.6    Kano, K.7    Higuchi, Y.8
  • 22
    • 0001067991 scopus 로고    scopus 로고
    • Nickel-Iron Hydrogenases
    • Messerschmidt, A, Huber, R, Poulos, T, and Wieghardt, K, Eds, John Wiley & Sons, Chichester, U.K
    • Frey, M., and Fontecilla-Camps, J. C. (2001) Nickel-Iron Hydrogenases. In Handbook of Metalloproteins (Messerschmidt, A., Huber, R., Poulos, T., and Wieghardt, K., Eds.) Vol. 2, pp 880-896, John Wiley & Sons, Chichester, U.K.
    • (2001) Handbook of Metalloproteins , vol.2 , pp. 880-896
    • Frey, M.1    Fontecilla-Camps, J.C.2
  • 23
    • 2342552466 scopus 로고    scopus 로고
    • Relativistic DFT Calculation of the Reaction Cycle Intermediates of [NiFe] Hydrogenase: A Contribution to Understanding the Enzymatic Mechanism
    • Stein, M., and Lubitz, W. (2004) Relativistic DFT Calculation of the Reaction Cycle Intermediates of [NiFe] Hydrogenase: A Contribution to Understanding the Enzymatic Mechanism. J. Inorg. Biochem. 98, 862-877.
    • (2004) J. Inorg. Biochem , vol.98 , pp. 862-877
    • Stein, M.1    Lubitz, W.2
  • 24
    • 0036525727 scopus 로고    scopus 로고
    • Quantum Chemical Calculations of [NiFe] Hydrogenase
    • Stein, M., and Lubitz, W. (2002) Quantum Chemical Calculations of [NiFe] Hydrogenase. Curr. Opin. Chem. Biol. 6, 243-249.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 243-249
    • Stein, M.1    Lubitz, W.2
  • 25
    • 2542565159 scopus 로고    scopus 로고
    • Hydrogen-Induced Activation of the [NiFe]-Hydrogenase from Allochromatium vinosum As Studied by Stopped-Flow Infrared Spectroscopy
    • Kurkin, S., George, S. J., Thorneley, R. N. F., and Albracht, S. P. J. (2004) Hydrogen-Induced Activation of the [NiFe]-Hydrogenase from Allochromatium vinosum As Studied by Stopped-Flow Infrared Spectroscopy. Biochemistry 43, 6820-6831.
    • (2004) Biochemistry , vol.43 , pp. 6820-6831
    • Kurkin, S.1    George, S.J.2    Thorneley, R.N.F.3    Albracht, S.P.J.4
  • 26
    • 0029137283 scopus 로고
    • Stoichiometric Reductive Titrations of Desulfovibrio gigas Hydrogenase
    • Roberts, L. M., and Lindahl, P. A. (1995) Stoichiometric Reductive Titrations of Desulfovibrio gigas Hydrogenase. J. Am. Chem. Soc. 117, 2565-2572.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 2565-2572
    • Roberts, L.M.1    Lindahl, P.A.2
  • 27
    • 0033549110 scopus 로고    scopus 로고
    • A Hybrid Density Functional Theory Molecular Mechanics Study of Nickel-Iron Hydrogenase: Investigation of the Active Site Redox States
    • Amara, P., Volbeda, A., Fontecilla-Camps, J. C., and Field, M. J. (1999) A Hybrid Density Functional Theory Molecular Mechanics Study of Nickel-Iron Hydrogenase: Investigation of the Active Site Redox States. J. Am. Chem. Soc. 121, 4468-4477.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 4468-4477
    • Amara, P.1    Volbeda, A.2    Fontecilla-Camps, J.C.3    Field, M.J.4
  • 28
    • 23644437690 scopus 로고    scopus 로고
    • DFT Investigations of Models Related to the Active Site of [NiFe] and [Fe] Hydrogenases
    • Bruschi, M., Zampella, G., Fantucci, P., and De Gioia, L. (2005) DFT Investigations of Models Related to the Active Site of [NiFe] and [Fe] Hydrogenases. Coord. Chem. Rev. 249, 1620-1640.
    • (2005) Coord. Chem. Rev , vol.249 , pp. 1620-1640
    • Bruschi, M.1    Zampella, G.2    Fantucci, P.3    De Gioia, L.4
  • 29
    • 35748942883 scopus 로고    scopus 로고
    • Computational Studies of [NiFe] and [FeFe] Hydrogenases
    • Siegbahn, P. E. M., Tye, J. W., and Hall, M. B. (2007) Computational Studies of [NiFe] and [FeFe] Hydrogenases. Chem. Rev. 107, 4414-4435.
    • (2007) Chem. Rev , vol.107 , pp. 4414-4435
    • Siegbahn, P.E.M.1    Tye, J.W.2    Hall, M.B.3
  • 31
    • 17644387260 scopus 로고    scopus 로고
    • Proton and Electron Transfers in [NiFe] Hydrogenase
    • Siegbahn, P. E. M. (2004) Proton and Electron Transfers in [NiFe] Hydrogenase. Adv. Inorg. Chem. 56, 101-125.
    • (2004) Adv. Inorg. Chem , vol.56 , pp. 101-125
    • Siegbahn, P.E.M.1
  • 32
    • 0037160427 scopus 로고    scopus 로고
    • High-Spin Ni(II), a Surprisingly Good Structural Model for [NiFe] Hydrogenase
    • Fan, H.-J., and Hall, M. B. (2002) High-Spin Ni(II), a Surprisingly Good Structural Model for [NiFe] Hydrogenase. J. Am. Chem. Soc. 124, 394-395.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 394-395
    • Fan, H.-J.1    Hall, M.B.2
  • 33
    • 8644223114 scopus 로고    scopus 로고
    • A Theoretical Study of Spin States in Ni-S-4 Complexes and Models of the [NiFe] Hydrogenase Active Site
    • Bruschi, M., De Gioia, L., Zampella, G., Reiher, M., Fantucci, P., and Stein, M. (2004) A Theoretical Study of Spin States in Ni-S-4 Complexes and Models of the [NiFe] Hydrogenase Active Site. J. Biol. Inorg. Chem. 9, 873-884.
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 873-884
    • Bruschi, M.1    De Gioia, L.2    Zampella, G.3    Reiher, M.4    Fantucci, P.5    Stein, M.6
  • 34
    • 41049100490 scopus 로고    scopus 로고
    • High Level ab Initio and DFT Calculations of Models of the Catalytically Active Ni-Fe Hydrogenases
    • Jayapal, P., Robinson, D., Sundararajan, M., Hillier, I. H., and McDouall, J. J. W. (2008) High Level ab Initio and DFT Calculations of Models of the Catalytically Active Ni-Fe Hydrogenases. Phys. Chem. Chem. Phys. 10, 1734-1738.
    • (2008) Phys. Chem. Chem. Phys , vol.10 , pp. 1734-1738
    • Jayapal, P.1    Robinson, D.2    Sundararajan, M.3    Hillier, I.H.4    McDouall, J.J.W.5
  • 35
    • 33645516017 scopus 로고    scopus 로고
    • Density Functional Study of the Catalytic Cycle of Nickel-Iron [NiFe] Hydrogenases and the Involvement of High-Spin Nickel(II)
    • Pardo, A., de Lacey, A., Fernandez, V. M., Fan, Y., and Hall, M. B. (2006) Density Functional Study of the Catalytic Cycle of Nickel-Iron [NiFe] Hydrogenases and the Involvement of High-Spin Nickel(II). J. Biol. Inorg. Chem. 11, 286-306.
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 286-306
    • Pardo, A.1    de Lacey, A.2    Fernandez, V.M.3    Fan, Y.4    Hall, M.B.5
  • 36
    • 34547702865 scopus 로고    scopus 로고
    • Hybrid Density Functional Study of the Oxidized States of NiFe-Hydrogenase
    • Siegbahn, P. E. M. (2007) Hybrid Density Functional Study of the Oxidized States of NiFe-Hydrogenase. C. R. Chim. 10, 766-774.
    • (2007) C. R. Chim , vol.10 , pp. 766-774
    • Siegbahn, P.E.M.1
  • 39
    • 23644443536 scopus 로고    scopus 로고
    • H/D Exchange Reactions and Mechanistic Aspects of the Hydrogenases
    • Vignais, P. M. (2005) H/D Exchange Reactions and Mechanistic Aspects of the Hydrogenases. Coord. Chem. Rev. 249, 1677-1690.
    • (2005) Coord. Chem. Rev , vol.249 , pp. 1677-1690
    • Vignais, P.M.1
  • 40
    • 64349085779 scopus 로고    scopus 로고
    • Center of [NiFe] Hydrogenases
    • Ph.D. Thesis, Technischen Universität Berlin
    • Trofantchouk, O. (2001) Center of [NiFe] Hydrogenases. EPR, ENDOR and FTIR Studies Ph.D. Thesis, Technischen Universität Berlin.
    • (2001) EPR, ENDOR and FTIR Studies
    • Trofantchouk, O.1
  • 42
    • 33645845675 scopus 로고    scopus 로고
    • Modeling Polarization in Proteins and Protein - ligand Complexes: Methods and Preliminary Results
    • Friesner, R. A. (2005) Modeling Polarization in Proteins and Protein - ligand Complexes: Methods and Preliminary Results. Adv. Protein Chem. 72, 79-104.
    • (2005) Adv. Protein Chem , vol.72 , pp. 79-104
    • Friesner, R.A.1
  • 46
    • 0030799641 scopus 로고    scopus 로고
    • Nature and Electronic Structure of the Ni-X Dinuclear Center of Desulfovibrio gigas Hydrogenase. Implications for the Enzymatic Mechanism
    • Dole, F., Fournel, A., Magro, V., Hatchikian, E. C., Bertrand, P., and Guigliarelli, B. (1997) Nature and Electronic Structure of the Ni-X Dinuclear Center of Desulfovibrio gigas Hydrogenase. Implications for the Enzymatic Mechanism. Biochemistry 36, 7847-7854.
    • (1997) Biochemistry , vol.36 , pp. 7847-7854
    • Dole, F.1    Fournel, A.2    Magro, V.3    Hatchikian, E.C.4    Bertrand, P.5    Guigliarelli, B.6
  • 47
    • 0026754807 scopus 로고
    • The Nickel Site in Active Desulfovibrio baculatus [NiFeSe] Hydrogenase Is Diamagnetic: Multifield Saturation Magnetization Measurement of the Spin State of Ni(II)
    • Wang, C. P., Franco, R., Moura, J. J. G., Moura, I., and Day, E. P. (1992) The Nickel Site in Active Desulfovibrio baculatus [NiFeSe] Hydrogenase Is Diamagnetic: Multifield Saturation Magnetization Measurement of the Spin State of Ni(II). J. Biol. Chem. 267, 7378-7380.
    • (1992) J. Biol. Chem , vol.267 , pp. 7378-7380
    • Wang, C.P.1    Franco, R.2    Moura, J.J.G.3    Moura, I.4    Day, E.P.5
  • 48
    • 0001071744 scopus 로고
    • Electronic and Magnetic Properties of Nickel-Substituted Rubredoxin: A Variable-Temperature Magnetic Circular-Dichroism Study
    • Kowal, A. T., Zambrano, I. C., Moura, I., Moura, J. J. G., LeGall, J., and Johnsson, M. K. (1988) Electronic and Magnetic Properties of Nickel-Substituted Rubredoxin: A Variable-Temperature Magnetic Circular-Dichroism Study. Inorg. Chem. 27, 1162-1166.
    • (1988) Inorg. Chem , vol.27 , pp. 1162-1166
    • Kowal, A.T.1    Zambrano, I.C.2    Moura, I.3    Moura, J.J.G.4    LeGall, J.5    Johnsson, M.K.6
  • 50
    • 33746218430 scopus 로고    scopus 로고
    • The Performance of Hybrid DFT on Mechanisms Involving Transition Metal Complexes in Enzymes
    • Siegbahn, P. E. M. (2006) The Performance of Hybrid DFT on Mechanisms Involving Transition Metal Complexes in Enzymes. J. Biol. Inorg. Chem. 11, 695-701.
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 695-701
    • Siegbahn, P.E.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.