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Volumn 39, Issue 10, 2006, Pages 729-738

Modeling enzymatic reactions involving transition metals

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; METHANE; OXIDOREDUCTASE; TRANSITION ELEMENT;

EID: 33750615773     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar050123u     Document Type: Article
Times cited : (283)

References (46)
  • 1
    • 0030986743 scopus 로고    scopus 로고
    • The Mechanism of C-H Activation by Di-Iron Methane Monooxygenases: Quantum Chemical Studies
    • Siegbahn, P. E. M.; Crabtree, R. H. The Mechanism of C-H Activation by Di-Iron Methane Monooxygenases: Quantum Chemical Studies. J. Am. Chem. Soc. 1997, 119, 3103-3113.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3103-3113
    • Siegbahn, P.E.M.1    Crabtree, R.H.2
  • 2
    • 0040193886 scopus 로고
    • Simulations of Quantum-Mechanical Corrections for Rate-Constants of Hydride-Transfer Reactions in Enzymes and Solutions
    • Hwang, K. K.; Chu, Z. T.; Yadav, A.; Warshel, A. Simulations of Quantum-Mechanical Corrections for Rate-Constants of Hydride-Transfer Reactions in Enzymes and Solutions J. Phys. Chem. 1991, 95, 8445-8448.
    • (1991) J. Phys. Chem. , vol.95 , pp. 8445-8448
    • Hwang, K.K.1    Chu, Z.T.2    Yadav, A.3    Warshel, A.4
  • 3
    • 0000189651 scopus 로고
    • Density-Functional Thermochemistry. 3. The Role of Exact Exchange
    • Becke, A. D. Density-Functional Thermochemistry. 3. The Role of Exact Exchange. J. Chem. Phys. 1993, 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 5
    • 0037295343 scopus 로고    scopus 로고
    • Mechanisms of Metalloenzymes Studied by Quantum Chemical Methods
    • Siegbahn, P. E. M. Mechanisms of Metalloenzymes Studied by Quantum Chemical Methods. Q. Rev. Biophys. 2003, 36, 91-145.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 91-145
    • Siegbahn, P.E.M.1
  • 6
    • 33746218430 scopus 로고    scopus 로고
    • The Performance of Hybrid DFT on Mechanisms Involving Transition Metal Complexes in Enzymes
    • in press
    • Siegbahn, P. E. M. The Performance of Hybrid DFT on Mechanisms Involving Transition Metal Complexes in Enzymes. J. Biol. Inorg. Chem., in press.
    • J. Biol. Inorg. Chem.
    • Siegbahn, P.E.M.1
  • 8
    • 18744363035 scopus 로고    scopus 로고
    • Agreement between Experiment and Hybrid DFT Calculations for O-H Bond Dissociation Enthalpies in Manganese Complexes
    • Lundberg, M.; Siegbahn, P. E. M. Agreement Between Experiment and Hybrid DFT Calculations for O-H Bond Dissociation Enthalpies in Manganese Complexes. J. Comput. Chem. 2005, 26, 661-667.
    • (2005) J. Comput. Chem. , vol.26 , pp. 661-667
    • Lundberg, M.1    Siegbahn, P.E.M.2
  • 9
    • 0037305747 scopus 로고    scopus 로고
    • High-Level ab Initio Calculations on the Energetics of Low-Lying Spin States of Biologically Relevant Transition Metal Complexes: A First Progress Report
    • Ghosh, A.; Taylor, P. R. High-Level ab Initio Calculations on the Energetics of Low-Lying Spin States of Biologically Relevant Transition Metal Complexes: A First Progress Report. Curr. Opin. Chem. Biol. 2003, 7, 113-124.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 113-124
    • Ghosh, A.1    Taylor, P.R.2
  • 12
    • 0038171471 scopus 로고    scopus 로고
    • A Comparison of O-O Bond-Cleavage for Dicopper Complexes in Enzymes and Synthetic Systems
    • Siegbahn, P. E. M. A Comparison of O-O Bond-Cleavage for Dicopper Complexes in Enzymes and Synthetic Systems. J. Biol. Inorg. Chem. 2003, 8, 577-585.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 577-585
    • Siegbahn, P.E.M.1
  • 15
    • 24344484047 scopus 로고    scopus 로고
    • On Possible Pitfalls in ab Initio Quantum Mechanics/Molecular Mechanics Minimization Approaches for Studies of Enzymatic Reactions
    • Klahn, M.; Braun-Sand, S.; Rosta, E.; Warshel, A. On Possible Pitfalls in ab Initio Quantum Mechanics/Molecular Mechanics Minimization Approaches for Studies of Enzymatic Reactions. J. Phys. Chem. B 2005, 109, 15645-15650.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15645-15650
    • Klahn, M.1    Braun-Sand, S.2    Rosta, E.3    Warshel, A.4
  • 16
    • 0035889788 scopus 로고    scopus 로고
    • Modeling Aspects of Mechanisms for Reactions Catalyzed by Metalloenzymes
    • Siegbahn, P. E. M. Modeling Aspects of Mechanisms for Reactions Catalyzed by Metalloenzymes. J. Comput. Chem. 2001, 22, 1634-1645.
    • (2001) J. Comput. Chem. , vol.22 , pp. 1634-1645
    • Siegbahn, P.E.M.1
  • 17
    • 33746181702 scopus 로고    scopus 로고
    • Quantum Chemistry Applied to the Mechanisms of Transition Metal Containing Enzymes - Cytochrome c Oxidase a Particularly Challenging Case
    • in press
    • Blomberg, M. R. A.; Siegbahn, P. E. M. Quantum Chemistry Applied to the Mechanisms of Transition Metal Containing Enzymes - Cytochrome c Oxidase a Particularly Challenging Case. J. Comput. Chem., in press.
    • J. Comput. Chem.
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2
  • 18
    • 0036932975 scopus 로고    scopus 로고
    • A Theoretical Study of the Mechanism for Peptide Hydrolysis by Thermolysin
    • Pelmenschikov, V.; Blomberg, M. R. A.; Siegbahn, P. E. M. A Theoretical Study of the Mechanism for Peptide Hydrolysis by Thermolysin. J. Biol. Inorg. Chem. 2002, 7, 284-298.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 284-298
    • Pelmenschikov, V.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 19
    • 3943071836 scopus 로고    scopus 로고
    • The Catalytic Cycle of Catechol Oxidase
    • Siegbahn, P. E. M. The Catalytic Cycle of Catechol Oxidase. J. Biol. Inorg. Chem. 2004, 9, 577-590.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 577-590
    • Siegbahn, P.E.M.1
  • 20
    • 1542377662 scopus 로고    scopus 로고
    • Dioxygen Activation in Methane Monooxygenase: A Theoretical Study
    • Gherman, B. F.; Bark, M.-H.; Lippard, S. J.; Friesner, R. A. Dioxygen Activation in Methane Monooxygenase: a Theoretical Study. J. Am. Chem. Soc. 2004, 126, 2978-2990.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2978-2990
    • Gherman, B.F.1    Bark, M.-H.2    Lippard, S.J.3    Friesner, R.A.4
  • 21
    • 0035944088 scopus 로고    scopus 로고
    • Density Functional Studies of Oxidized and Reduced Methane Monooxygenase. Optimized Geometries and Exchange Coupling of Active Site Clusters
    • Lovell, T.; Li, J.; Noodleman, L. Density Functional Studies of Oxidized and Reduced Methane Monooxygenase. Optimized Geometries and Exchange Coupling of Active Site Clusters. Inorg. Chem. 2001, 40, 5251-5266.
    • (2001) Inorg. Chem. , vol.40 , pp. 5251-5266
    • Lovell, T.1    Li, J.2    Noodleman, L.3
  • 22
    • 84962425632 scopus 로고    scopus 로고
    • O-O Bond Cleavage and Alkane Hydroxylation in Methane Monooxygenase
    • Siegbahn, P. E. M. O-O Bond Cleavage and Alkane Hydroxylation in Methane Monooxygenase. J. Biol. Inorg. Chem. 2001, 6, 27-45.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 27-45
    • Siegbahn, P.E.M.1
  • 23
    • 0033546705 scopus 로고    scopus 로고
    • Mechanism of the Methane Methanol Conversion Reaction Catalyzed by Methane Monooxygenase: A Density Functional Study
    • Basch, H.; Mogi, K.; Musaev, D. G.; Morokuma, K. Mechanism of the Methane Methanol Conversion Reaction Catalyzed by Methane Monooxygenase: A Density Functional Study. J. Am. Chem. Soc. 1999, 121, 7249-7256.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7249-7256
    • Basch, H.1    Mogi, K.2    Musaev, D.G.3    Morokuma, K.4
  • 24
    • 15044356424 scopus 로고    scopus 로고
    • Crystal Structure of a Membrane-Bound Metalloenzyme That Catalyses the Biological Oxidation of Methane
    • Lieberman, R. L.; Rosenzweig, A. C. Crystal Structure of a Membrane-Bound Metalloenzyme That Catalyses the Biological Oxidation of Methane. Nature 2005, 434, 177-182.
    • (2005) Nature , vol.434 , pp. 177-182
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 25
    • 21944432511 scopus 로고    scopus 로고
    • Theoretical Perspective on the Structure and Mechanism of Cytochrome P450 Enzymes
    • Shaik, S.; Kumar, D.; de Visser, S. P.; Altun, A.; Thiel, W. Theoretical Perspective on the Structure and Mechanism of Cytochrome P450 Enzymes. Chem. Rev. 2005, 105, 2279-2328.
    • (2005) Chem. Rev. , vol.105 , pp. 2279-2328
    • Shaik, S.1    Kumar, D.2    De Visser, S.P.3    Altun, A.4    Thiel, W.5
  • 26
    • 0030726657 scopus 로고    scopus 로고
    • Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation
    • Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, R. K. Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation. Science 1997, 278, 1457-1462.
    • (1997) Science , vol.278 , pp. 1457-1462
    • Ermler, U.1    Grabarse, W.2    Shima, S.3    Goubeaud, M.4    Thauer, R.K.5
  • 27
    • 0037123266 scopus 로고    scopus 로고
    • A Mechanism from Quantum Chemical Studies for Methane Formation in Methanogenesis
    • Pelmenschikov, V.; Blomberg, M. R. A.; Siegbahn, P. E. M.; Crabtree, R. H. A Mechanism from Quantum Chemical Studies for Methane Formation in Methanogenesis. J. Am. Chem. Soc. 2002, 124, 4039-4049.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4039-4049
    • Pelmenschikov, V.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3    Crabtree, R.H.4
  • 28
    • 0347264753 scopus 로고    scopus 로고
    • Crystal Structure of Naphthalene Dioxygenase: Side-On Binding of Dioxygen to Iron
    • Karlsson, A.; Parales, J. V.; Parales, R. E.; Gibson, D. T.; Eklund, H.; Ramaswamy, S. Crystal Structure of Naphthalene Dioxygenase: Side-On Binding of Dioxygen to Iron. Science 2003, 299, 1039-1042.
    • (2003) Science , vol.299 , pp. 1039-1042
    • Karlsson, A.1    Parales, J.V.2    Parales, R.E.3    Gibson, D.T.4    Eklund, H.5    Ramaswamy, S.6
  • 31
    • 3042717031 scopus 로고    scopus 로고
    • A Theoretical Study of the cis-Dihydroxylation Mechanism in Naphthalene 1,2-Dioxygenase
    • Bassan, A.; Blomberg, M. R. A.; Siegbahn, P. E. M. A Theoretical Study of the cis-Dihydroxylation Mechanism in Naphthalene 1,2-Dioxygenase. J. Biol. Inorg. Chem. 2004, 9, 439-452.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 439-452
    • Bassan, A.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 32
    • 9244227570 scopus 로고    scopus 로고
    • Quantum Chemical Studies of Dioxygen Activation by Mononuclear Non-Heme Iron Enzymes with the 2-His-1-Carboxylate Facial Triad
    • Bassan, A.; Borowski, T.; Siegbahn, P. E. M. Quantum Chemical Studies of Dioxygen Activation by Mononuclear Non-Heme Iron Enzymes with the 2-His-1-Carboxylate Facial Triad. Dalton Trans. 2004, 20, 3153-3162.
    • (2004) Dalton Trans. , vol.20 , pp. 3153-3162
    • Bassan, A.1    Borowski, T.2    Siegbahn, P.E.M.3
  • 33
    • 0037465347 scopus 로고    scopus 로고
    • (4-Hydroxyphenyl)pyruvate Dioxygenase from Streptomyces avermitilis: The Basis for Ordered Substrate Addition
    • Johnson-Winters K.; Purpero, V. M.; Kavana, M.; Nelson, T.; Moran, G. R. (4-Hydroxyphenyl)pyruvate Dioxygenase from Streptomyces avermitilis: The Basis for Ordered Substrate Addition. Biochemistry 2003, 42, 2072-2080.
    • (2003) Biochemistry , vol.42 , pp. 2072-2080
    • Johnson-Winters, K.1    Purpero, V.M.2    Kavana, M.3    Nelson, T.4    Moran, G.R.5
  • 34
    • 0043022281 scopus 로고    scopus 로고
    • Dioxygenase Enzymes: Catalytic Mechanisms and Chemical Models
    • Bugg, T. D. H. Dioxygenase Enzymes: Catalytic Mechanisms and Chemical Models. Tetrahedron 2003, 59, 7075-7101.
    • (2003) Tetrahedron , vol.59 , pp. 7075-7101
    • Bugg, T.D.H.1
  • 35
    • 2442605525 scopus 로고    scopus 로고
    • A Hybrid Density Functional Study of O-O Bond Cleavage and Phenyl Ring Hydroxylation for a Biomimetic Non-Heme Iron Complex
    • Borowski, T.; Bassan, A.; Siegbahn, P. E. M. A Hybrid Density Functional Study of O-O Bond Cleavage and Phenyl Ring Hydroxylation for a Biomimetic Non-Heme Iron Complex. Inorg. Chem. 2004, 43, 3277-3291.
    • (2004) Inorg. Chem. , vol.43 , pp. 3277-3291
    • Borowski, T.1    Bassan, A.2    Siegbahn, P.E.M.3
  • 36
    • 4644341669 scopus 로고    scopus 로고
    • 4-Hydroxyphenylpyruvate Dioxygenase: A Hybrid Density Functional Study of the Catalytic Reaction Mechanism
    • Borowski, T.; Bassan, A.; Siegbahn, P. E. M. 4-Hydroxyphenylpyruvate Dioxygenase: A Hybrid Density Functional Study of the Catalytic Reaction Mechanism. Biochemistry 2004, 43, 12331-12342.
    • (2004) Biochemistry , vol.43 , pp. 12331-12342
    • Borowski, T.1    Bassan, A.2    Siegbahn, P.E.M.3
  • 38
    • 29044431814 scopus 로고    scopus 로고
    • Catalytic Reaction Mechanism of Homogentisate Dioxygenase: A Hybrid DFT Study
    • Borowski, T.; Georgiev, V.; Siegbahn, P. E. M. Catalytic Reaction Mechanism of Homogentisate Dioxygenase: A Hybrid DFT Study. J. Am. Chem. Soc. 2005, 127, 17303-17314.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17303-17314
    • Borowski, T.1    Georgiev, V.2    Siegbahn, P.E.M.3
  • 39
    • 0033832158 scopus 로고    scopus 로고
    • A Mechanistic Study of Isopenicillin N Formation Using Density Functional Theory
    • Wirstam, M.; Siegbahn, P. E. M. A Mechanistic Study of Isopenicillin N Formation Using Density Functional Theory. J. Am. Chem. Soc. 2000, 122, 8539-8547.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8539-8547
    • Wirstam, M.1    Siegbahn, P.E.M.2
  • 40
    • 1542289159 scopus 로고    scopus 로고
    • Mechanism of Dioxygen Activation in 2-Oxoglutarate-Dependent Enzymes: A Hybrid DFT Study
    • Borowski, T.; Bassan, A.; Siegbahn, P. E. M. Mechanism of Dioxygen Activation in 2-Oxoglutarate-Dependent Enzymes: A Hybrid DFT Study. Chem.-Eur. J. 2004, 10, 1031-1041.
    • (2004) Chem.-Eur. J. , vol.10 , pp. 1031-1041
    • Borowski, T.1    Bassan, A.2    Siegbahn, P.E.M.3
  • 41
    • 4644341669 scopus 로고    scopus 로고
    • 4-Hydroxyphenylpyruvate Dioxygenase: A Hybrid Density Functional Study of the Catalytic Reaction Mechanism
    • Borowski, T.; Bassan, A.; Siegbahn, P. E. M. 4-Hydroxyphenylpyruvate Dioxygenase: A Hybrid Density Functional Study of the Catalytic Reaction Mechanism. Biochemistry 2004, 43, 12331-12342.
    • (2004) Biochemistry , vol.43 , pp. 12331-12342
    • Borowski, T.1    Bassan, A.2    Siegbahn, P.E.M.3
  • 42
    • 0037415072 scopus 로고    scopus 로고
    • Mechanism of Dioxygen Cleavage in Tetrahydrobiopterin-Dependent Amino Acid Hydroxylases
    • Bassan, A.; Blomberg, M. R. A.; Siegbahn, P. E. M. Mechanism of Dioxygen Cleavage in Tetrahydrobiopterin-Dependent Amino Acid Hydroxylases. Chem.-Eur. J. 2003, 9, 106-115.
    • (2003) Chem.-Eur. J. , vol.9 , pp. 106-115
    • Bassan, A.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 43
    • 3242811958 scopus 로고    scopus 로고
    • Mechanism for Catechol Ring-Cleavage by Non-Heme Iron Extradiol Dioxygenases
    • Siegbahn, P. E. M.; Haeffner, F. Mechanism for Catechol Ring-Cleavage by Non-Heme Iron Extradiol Dioxygenases. J. Am. Chem. Soc. 2004, 126, 8919-8932.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8919-8932
    • Siegbahn, P.E.M.1    Haeffner, F.2
  • 44
    • 33845209179 scopus 로고    scopus 로고
    • Ethylene Biosynthesis by 1-Aminocyclopropane-1-Carboxylic Acid Oxidase. A DFT Study
    • in press
    • Bassan, A.; Borowski, T.; Schofield, C. J.; Siegbahn, P. E. M. Ethylene Biosynthesis by 1-Aminocyclopropane-1-Carboxylic Acid Oxidase. A DFT Study. Chem.-Eur. J., in press.
    • Chem.-Eur. J.
    • Bassan, A.1    Borowski, T.2    Schofield, C.J.3    Siegbahn, P.E.M.4
  • 45
    • 3042717031 scopus 로고    scopus 로고
    • A Theoretical Study of the cis-Dihydroxylation Mechanism in Naphthalene 1,2-Dioxygenase
    • Bassan, A.; Blomberg, M. R. A.; Siegbahn, P. E. M. A Theoretical Study of the cis-Dihydroxylation Mechanism in Naphthalene 1,2-Dioxygenase. J. Biol. Inorg. Chem. 2004, 9, 439-452.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 439-452
    • Bassan, A.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3


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