메뉴 건너뛰기




Volumn 117, Issue 50, 2013, Pages 16044-16057

Mechanistic insights for formation of an organometallic Co-C bond in the methyl transfer reaction catalyzed by methionine synthase

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON TRANSFER; METHIONINE SYNTHASE; METHYL TRANSFERS; METHYLTRANSFERASES; QUANTUM MECHANICS/MOLECULAR MECHANICS; RADICAL MECHANISM; RADICAL REACTIONS; TRANSITION STATE;

EID: 84890936845     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4093145     Document Type: Article
Times cited : (23)

References (73)
  • 1
    • 23844557871 scopus 로고    scopus 로고
    • Vitamin B12: Chemistry and Biochemistry
    • Kräutler, B. Vitamin B12: Chemistry and Biochemistry Biochem. Soc. Trans. 2005, 33, 806-810
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 806-810
    • Kräutler, B.1
  • 2
    • 0004247468 scopus 로고    scopus 로고
    • In; Banerjee, R. John Wiley & Sons: New York
    • Gerfen, G. J. In Chemistry and Biochemistry of B12; Banerjee, R., Ed.; John Wiley & Sons: New York, 1999; pp 165-195.
    • (1999) Chemistry and Biochemistry of B12 , pp. 165-195
    • Gerfen, G.J.1
  • 3
    • 0041766196 scopus 로고    scopus 로고
    • Catalysis by Cobalamin-Dependent Enzymes
    • Banerjee, R.; Ragsdale, S. W. Catalysis by Cobalamin-Dependent Enzymes Annu. Rev. Biochem. 2003, 72, 209-247
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 209-247
    • Banerjee, R.1    Ragsdale, S.W.2
  • 5
    • 0004247468 scopus 로고    scopus 로고
    • In; Banerjee, R. V. John Wiley & Sons: New York
    • Matthews, R. G. In Chemistry and Biochemistry of B12; Banerjee, R. V., Ed.; John Wiley & Sons: New York, 1999; pp 681-707.
    • (1999) Chemistry and Biochemistry of B12 , pp. 681-707
    • Matthews, R.G.1
  • 6
    • 0030990682 scopus 로고    scopus 로고
    • Structure-Based Perspectives on B12-Dependent Enzymes
    • Ludwig, M. L.; Matthews, R. G. Structure-Based Perspectives on B12-Dependent Enzymes Annu. Rev. Biochem. 1997, 66, 269-313
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 269-313
    • Ludwig, M.L.1    Matthews, R.G.2
  • 8
    • 0004183598 scopus 로고    scopus 로고
    • In; Reedijk, J. Bouwman, E. Marcel Dekker: New York
    • Marzilli, L. G. In Bioinorganic Catalysis; Reedijk, J.; Bouwman, E., Eds.; Marcel Dekker: New York, 1999; pp 423-468.
    • (1999) Bioinorganic Catalysis , pp. 423-468
    • Marzilli, L.G.1
  • 9
    • 21844449665 scopus 로고    scopus 로고
    • Chemistry and Enzymology of Vitamin B12
    • Brown, K. L. Chemistry and Enzymology of Vitamin B12 Chem. Rev. 2005, 105, 2075-2149
    • (2005) Chem. Rev. , vol.105 , pp. 2075-2149
    • Brown, K.L.1
  • 10
    • 72449124231 scopus 로고    scopus 로고
    • Methyltetrahydrofolate:corrinoid/iron-sulfur Protein Methyltransferase (MeTr): Protonation State of the Ligand and Active-Site Residues
    • Alonso, H.; Cummins, P. L.; Gready, J. E. Methyltetrahydrofolate: corrinoid/iron-sulfur Protein Methyltransferase (MeTr): Protonation State of the Ligand and Active-Site Residues J. Phys. Chem. B 2009, 113, 14787-14796
    • (2009) J. Phys. Chem. B , vol.113 , pp. 14787-14796
    • Alonso, H.1    Cummins, P.L.2    Gready, J.E.3
  • 11
    • 0013971068 scopus 로고
    • Role of Corrinoids in the Total Synthesis of Acetate from CO-2 by Clostridium Thermoaceticum
    • Ljungdah, l. L.; Irion, E.; Wood, H. G. Role of Corrinoids in the Total Synthesis of Acetate from CO-2 by Clostridium Thermoaceticum Fed. Proc. 1966, 25, 1642-1948
    • (1966) Fed. Proc. , vol.25 , pp. 1642-1948
    • Ljungdah, L.L.1    Irion, E.2    Wood, H.G.3
  • 12
    • 0034662752 scopus 로고    scopus 로고
    • Crystal Structure of a Methyltetrahydrofolate- and Corrinoid-Dependent Methyltransferase
    • Doukov, T.; Seravalli, J.; Stezowski, J.; Ragsdale, S. W. Crystal Structure of a Methyltetrahydrofolate- and Corrinoid-Dependent Methyltransferase Structure 2000, 8, 817-830
    • (2000) Structure , vol.8 , pp. 817-830
    • Doukov, T.1    Seravalli, J.2    Stezowski, J.3    Ragsdale, S.W.4
  • 14
    • 0023656557 scopus 로고
    • Mössbauer, EPR, and Optical Studies of the Corrinoid/Iron-Sulfur Protein Involved in the Synthesis of Acetyl Coenzyme A by Clostridium thermoaceticum
    • Ragsdale, S. W.; Lindahl, P. A.; Münck, E. Mössbauer, EPR, and Optical Studies of the Corrinoid/Iron-Sulfur Protein Involved in the Synthesis of Acetyl Coenzyme A by Clostridium thermoaceticum J. Biol. Chem. 1987, 262, 14289-14297
    • (1987) J. Biol. Chem. , vol.262 , pp. 14289-14297
    • Ragsdale, S.W.1    Lindahl, P.A.2    Münck, E.3
  • 15
    • 0000207157 scopus 로고
    • X-ray Absorption Spectroscopy of the Corrinoid/Iron-Sulfur Protein Involved in Acetyl Coenzyme A Synthesis by Clostridium thermoaceticum
    • Wirt, M. D.; Kumar, M.; Ragsdale, S. W.; Chance, M. R. X-ray Absorption Spectroscopy of the Corrinoid/Iron-Sulfur Protein Involved in Acetyl Coenzyme A Synthesis by Clostridium thermoaceticum J. Am. Chem. Soc. 1993, 115, 2146-2150
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2146-2150
    • Wirt, M.D.1    Kumar, M.2    Ragsdale, S.W.3    Chance, M.R.4
  • 17
    • 34250362770 scopus 로고    scopus 로고
    • Structural and Kinetic Evidence for an Extended Hydrogen-bonding Network in Catalysis of Methyl Group Transfer
    • Doukov, T. I.; Hemmi, H.; Drennan, C. L.; Ragsdale, S. W. Structural and Kinetic Evidence for an Extended Hydrogen-bonding Network in Catalysis of Methyl Group Transfer J. Biol. Chem. 2007, 282, 6609-6618
    • (2007) J. Biol. Chem. , vol.282 , pp. 6609-6618
    • Doukov, T.I.1    Hemmi, H.2    Drennan, C.L.3    Ragsdale, S.W.4
  • 18
    • 84873038087 scopus 로고    scopus 로고
    • Methyl Transfer Reaction between MeI and Ni(PPh2CH2CH2SEt)2 Complex. A DFT Study
    • Sitek, P.; Jaworska, M.; Lodowski, P.; Chmielowska, A. Methyl Transfer Reaction Between MeI and Ni(PPh2CH2CH2SEt)2 Complex. A DFT Study Inorg. Chem. Commun. 2013, 29, 65-69
    • (2013) Inorg. Chem. Commun. , vol.29 , pp. 65-69
    • Sitek, P.1    Jaworska, M.2    Lodowski, P.3    Chmielowska, A.4
  • 20
    • 0034649463 scopus 로고    scopus 로고
    • Protonation State of Methyltetrahydrofolate in a Binary Complex with Cobalamin-Dependent Methionine Synthase
    • Smith, A. E.; Matthews, R. G. Protonation State of Methyltetrahydrofolate in a Binary Complex with Cobalamin-Dependent Methionine Synthase Biochemistry 2000, 39, 13880-13890
    • (2000) Biochemistry , vol.39 , pp. 13880-13890
    • Smith, A.E.1    Matthews, R.G.2
  • 21
    • 0025697224 scopus 로고
    • Participation of Cob(I) alamin in the Reaction Catalyzed by Methionine Synthase from Escherichia coli: A Steady-State and Rapid Reaction Kinetic Analysis
    • Banerjee, R. V.; Frasca, V.; Ballou, D. P.; Matthews, R. G. Participation of Cob(I) alamin in the Reaction Catalyzed by Methionine Synthase from Escherichia coli: A Steady-State and Rapid Reaction Kinetic Analysis Biochemistry 1990, 29, 11101-11109
    • (1990) Biochemistry , vol.29 , pp. 11101-11109
    • Banerjee, R.V.1    Frasca, V.2    Ballou, D.P.3    Matthews, R.G.4
  • 22
    • 0030829339 scopus 로고    scopus 로고
    • Cobalamin-Dependent Methionine Synthase is a Modular Protein with Distinct Regions for Binding Homocysteine, Methyltetrahydrofolate, Cobalamin, and Adenosylmethionine
    • Goulding, C. W.; Postigo, D.; Matthews, R. G. Cobalamin-Dependent Methionine Synthase is a Modular Protein with Distinct Regions for Binding Homocysteine, Methyltetrahydrofolate, Cobalamin, and Adenosylmethionine Biochemistry. 1997, 36, 8082-8090
    • (1997) Biochemistry. , vol.36 , pp. 8082-8090
    • Goulding, C.W.1    Postigo, D.2    Matthews, R.G.3
  • 23
    • 0028769662 scopus 로고
    • How a Protein Binds B12: A 3.0 A X-ray Structure of B12-Binding Domains of Methionine Synthase
    • Drennan, C. L.; Huang, S.; Drummond, J. T.; Matthews, R. G.; Lidwig, M. L. How a Protein Binds B12: A 3.0 A X-ray Structure of B12-Binding Domains of Methionine Synthase Science 1994, 266, 1669-1674
    • (1994) Science , vol.266 , pp. 1669-1674
    • Drennan, C.L.1    Huang, S.2    Drummond, J.T.3    Matthews, R.G.4    Lidwig, M.L.5
  • 24
    • 0031470779 scopus 로고    scopus 로고
    • Cobalamin-Dependent Methionine Synthase from Escherichia coli: Involvement of Zinc in Homocysteine Activation
    • Goulding, C. W.; Matthews, R. G. Cobalamin-Dependent Methionine Synthase from Escherichia coli: Involvement of Zinc in Homocysteine Activation Biochemistry 1997, 36, 15749-15757
    • (1997) Biochemistry , vol.36 , pp. 15749-15757
    • Goulding, C.W.1    Matthews, R.G.2
  • 25
    • 0035969951 scopus 로고    scopus 로고
    • Characterization of the Zinc Sites in Cobalamin-Independent and Cobalamin-Dependent Methionine Synthase using Zinc and Selenium X-ray Absorption Spectroscopy
    • Peariso, K.; Zhou, Z. S.; Smith, A. E.; Matthews, R. G.; Penner-Hahn, J. E. Characterization of the Zinc Sites in Cobalamin-Independent and Cobalamin-Dependent Methionine Synthase using Zinc and Selenium X-ray Absorption Spectroscopy Biochemistry 2001, 40, 987-993
    • (2001) Biochemistry , vol.40 , pp. 987-993
    • Peariso, K.1    Zhou, Z.S.2    Smith, A.E.3    Matthews, R.G.4    Penner-Hahn, J.E.5
  • 27
    • 0030589146 scopus 로고    scopus 로고
    • The Structure of the C-terminal Domain of Methionine Synthase: Presenting S-Adenosylmethionine for Reductive Methylation of B12
    • Dixon, M. M.; Huang, S.; Matthews, R. G.; Ludwig, M. The Structure of the C-terminal Domain of Methionine Synthase: Presenting S-Adenosylmethionine for Reductive Methylation of B12 Structure 1996, 4, 1263-1275
    • (1996) Structure , vol.4 , pp. 1263-1275
    • Dixon, M.M.1    Huang, S.2    Matthews, R.G.3    Ludwig, M.4
  • 28
    • 41949094246 scopus 로고    scopus 로고
    • A Disulfide-Stabilized Conformer of Methionine Synthase Reveals an Unexpected Role for the Histidine Ligand of the Cobalamin Cofactor
    • Datta, S.; Koutmos, M.; Pattridge, K. A.; Ludwig, M. L.; Matthews, R. G. A Disulfide-Stabilized Conformer of Methionine Synthase Reveals an Unexpected Role for the Histidine Ligand of the Cobalamin Cofactor Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 4115-4120
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4115-4120
    • Datta, S.1    Koutmos, M.2    Pattridge, K.A.3    Ludwig, M.L.4    Matthews, R.G.5
  • 29
    • 0034860912 scopus 로고    scopus 로고
    • Cobalamin-Dependent Methyltransferases
    • Matthews, R. G. Cobalamin-Dependent Methyltransferases Acc. Chem. Res. 2001, 34, 681-689
    • (2001) Acc. Chem. Res. , vol.34 , pp. 681-689
    • Matthews, R.G.1
  • 30
    • 0005342197 scopus 로고
    • Methyl Transfer from Nitrogen to Cobalt: Model for the B12-Dependent Methyl Transfer Enzymes
    • No.
    • Pratt, J. M.; Norris, P. R.; Hamza, M. S. A.; Bolton, R., Methyl Transfer from Nitrogen to Cobalt: Model for the B12-Dependent Methyl Transfer Enzymes. J. Chem. Soc., Chem. Commun. 1994, No. 11, 1333-1334.
    • (1994) J. Chem. Soc., Chem. Commun. , vol.11 , pp. 1333-1334
    • Pratt, J.M.1    Norris, P.R.2    Hamza, M.S.A.3    Bolton, R.4
  • 31
    • 0028846885 scopus 로고
    • Mechanistic Studies of the Methyltransferase from Clostridium thermoaceticum: Origin of the pH Dependence of the Methyl Group Transfer from Methyl Tetrahydrofolate to the Corrinoid/Iron-Sulfur Protein
    • Zhao, S.; Roberts, D. L.; Ragsdale, S. W. Mechanistic Studies of the Methyltransferase from Clostridium thermoaceticum: Origin of the pH Dependence of the Methyl Group Transfer from Methyl Tetrahydrofolate to the Corrinoid/Iron-Sulfur Protein Biochemistry 1995, 34, 15075-15078
    • (1995) Biochemistry , vol.34 , pp. 15075-15078
    • Zhao, S.1    Roberts, D.L.2    Ragsdale, S.W.3
  • 32
    • 79953770148 scopus 로고    scopus 로고
    • How Is a Co-Methyl Intermediate Formed in the Reaction of Cobalamin-Dependent Methionine Synthase? Theoretical Evidence for a Two-Step Methyl Cation Transfer Mechanism
    • Chen, S.-L.; Blomberg, M. R. A.; Siegbahn, P. E. M. How Is a Co-Methyl Intermediate Formed in the Reaction of Cobalamin-Dependent Methionine Synthase? Theoretical Evidence for a Two-Step Methyl Cation Transfer Mechanism J. Phys. Chem. B 2011, 115, 4066-4077
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4066-4077
    • Chen, S.-L.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 34
  • 35
    • 28644432877 scopus 로고    scopus 로고
    • Very Fast Empirical Prediction and Rationalization of Protein pKa Values
    • Li, H.; Robertson, A. D.; Jensen, J. H. Very Fast Empirical Prediction and Rationalization of Protein pKa Values Proteins 2005, 61, 704-721
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 36
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKa Predictions
    • Olsson, M. H. M.; Søndergaard, C. R.; Rostkowski, M.; Jensen, J. H. PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKa Predictions J. Chem. Theory Comput. 2011, 7, 525-537
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Søndergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 37
    • 0035849162 scopus 로고    scopus 로고
    • Parameters for the Amber Force Field for the Molecular Mechanics Modeling of the Cobalt Corrinoids
    • Marques, H. M.; Ngoma, B.; Egan, T. J.; Brown, K. L. Parameters for the Amber Force Field for the Molecular Mechanics Modeling of the Cobalt Corrinoids J. Mol. Struct. 2001, 561, 71-91
    • (2001) J. Mol. Struct. , vol.561 , pp. 71-91
    • Marques, H.M.1    Ngoma, B.2    Egan, T.J.3    Brown, K.L.4
  • 42
    • 0039892284 scopus 로고
    • Density Functional Calculations of Molecular Bond Energies
    • Becke, A. D. Density Functional Calculations of Molecular Bond Energies J. Chem. Phys. 1986, 84, 4524-4529
    • (1986) J. Chem. Phys. , vol.84 , pp. 4524-4529
    • Becke, A.D.1
  • 43
    • 5944261746 scopus 로고
    • Density-Functional Approximation for the Correlation-Energy of the Inhomogenous Electron Gas
    • Perdew, J. P. Density-Functional Approximation for the Correlation-Energy of the Inhomogenous Electron Gas Phys. Rev. B 1986, 33, 8822-8824
    • (1986) Phys. Rev. B , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 44
    • 84986492477 scopus 로고
    • Atomic Charges Derived from Semiempirical Methods
    • Besler, B. H.; Merz, K. M.; Kollman, P. A. Atomic Charges Derived from Semiempirical Methods J. Comput. Chem. 1990, 11, 431-439
    • (1990) J. Comput. Chem. , vol.11 , pp. 431-439
    • Besler, B.H.1    Merz, K.M.2    Kollman, P.A.3
  • 45
    • 84890488500 scopus 로고    scopus 로고
    • version 9.2; Schrödinger, LLC: New York.
    • Suite 2011: Maestro, version 9.2; Schrödinger, LLC: New York, 2011.
    • (2011) Suite 2011: Maestro
  • 46
    • 0026672645 scopus 로고
    • Formation of a Square-Planar Co(I) B12 Intermediate. Implications for Enzyme Catalysis
    • Wirt, M. D.; Sagi, I.; Chance, M. R. Formation of a Square-Planar Co(I) B12 Intermediate. Implications for Enzyme Catalysis Biophys. J. 1992, 63, 412-417
    • (1992) Biophys. J. , vol.63 , pp. 412-417
    • Wirt, M.D.1    Sagi, I.2    Chance, M.R.3
  • 47
    • 79955920997 scopus 로고    scopus 로고
    • Role of the Axial Base in the Modulation of the Cob(I)alamin Electronic Properties: Insight from QM/MM, DFT, and CASSCF Calculations
    • Kumar, N.; Alfonso-Prieto, M.; Rovira, C.; Lodowski, P.; Jaworska, M.; Kozlowski, P. M. Role of the Axial Base in the Modulation of the Cob(I)alamin Electronic Properties: Insight from QM/MM, DFT, and CASSCF Calculations J. Chem. Theory Comput. 2011, 7, 1541-1551
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 1541-1551
    • Kumar, N.1    Alfonso-Prieto, M.2    Rovira, C.3    Lodowski, P.4    Jaworska, M.5    Kozlowski, P.M.6
  • 48
    • 4243943295 scopus 로고    scopus 로고
    • Generalized Gradient Approximation Made Simple
    • Perdew, J. P.; Burke, K.; Ernzerhof, M. Generalized Gradient Approximation Made Simple Phys. Rev. Lett. 1996, 77, 3865-3868
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 3865-3868
    • Perdew, J.P.1    Burke, K.2    Ernzerhof, M.3
  • 49
    • 0038702224 scopus 로고    scopus 로고
    • Comparison of the Chemical Properties of Iron and Cobalt Porphyrins and Corrins
    • Jensen, K. P.; Ryde, U. Comparison of the Chemical Properties of Iron and Cobalt Porphyrins and Corrins ChemBioChem 2003, 4, 413-424
    • (2003) ChemBioChem , vol.4 , pp. 413-424
    • Jensen, K.P.1    Ryde, U.2
  • 50
    • 20344391383 scopus 로고    scopus 로고
    • Electronic Structure of Cob(I)alamin: The Story of an Unusual Nucleophile
    • Jensen, K. P. Electronic Structure of Cob(I)alamin: The Story of an Unusual Nucleophile J. Phys. Chem. B 2005, 109, 10505-10512
    • (2005) J. Phys. Chem. B , vol.109 , pp. 10505-10512
    • Jensen, K.P.1
  • 51
    • 33747197724 scopus 로고    scopus 로고
    • Performance of DFT in Modeling Electronic and Structural Properties of Cobalamins
    • Kuta, J.; Patchkovskii, S.; Zgierski, M. Z.; Kozlowski, P. M. Performance of DFT in Modeling Electronic and Structural Properties of Cobalamins J. Comput. Chem. 2006, 27, 1429-1437
    • (2006) J. Comput. Chem. , vol.27 , pp. 1429-1437
    • Kuta, J.1    Patchkovskii, S.2    Zgierski, M.Z.3    Kozlowski, P.M.4
  • 52
    • 34547438769 scopus 로고    scopus 로고
    • Reductive Cleavage Mechanism of Methylcobalamin: Elementary Steps of Co-C Bond Breaking
    • Kozlowski, P. M.; Kuta, J.; Galezowski, W. Reductive Cleavage Mechanism of Methylcobalamin: Elementary Steps of Co-C Bond Breaking J. Phys. Chem. B 2007, 111, 7638-7645
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7638-7645
    • Kozlowski, P.M.1    Kuta, J.2    Galezowski, W.3
  • 53
    • 84874094947 scopus 로고    scopus 로고
    • Electronic Structure of One-Electron-Oxidized Form of the Methylcobalamin Cofactor: Spin Density Distribution and Pseudo-Jahn-Teller Effect
    • Kumar, N.; Kuta, J.; Galezowski, W.; Kozlowski, P. M. Electronic Structure of One-Electron-Oxidized Form of the Methylcobalamin Cofactor: Spin Density Distribution and Pseudo-Jahn-Teller Effect Inorg. Chem. 2013, 52, 1762-1771
    • (2013) Inorg. Chem. , vol.52 , pp. 1762-1771
    • Kumar, N.1    Kuta, J.2    Galezowski, W.3    Kozlowski, P.M.4
  • 54
    • 34147151135 scopus 로고    scopus 로고
    • First Principles Study of Coenzyme B12. Crystal Packing Forces Effect on Axial Bond Lengths
    • Rovira, C.; Kozlowski, P. M. First Principles Study of Coenzyme B12. Crystal Packing Forces Effect on Axial Bond Lengths J. Phys. Chem. B 2007, 111, 3251-3257
    • (2007) J. Phys. Chem. B , vol.111 , pp. 3251-3257
    • Rovira, C.1    Kozlowski, P.M.2
  • 55
    • 84874024887 scopus 로고    scopus 로고
    • Electronic Structure of the S1 State in Methylcobalamin: Insight from CASSCF/MC-XQDPT2, EOM-CCSD, and TD-DFT Calculations
    • Kornobis, K.; Kumar, N.; Lodowski, P.; Jaworska, M.; Piecuch, P.; Lutz, J. J.; Wong, B. M.; Kozlowski, P. M. Electronic Structure of the S1 State in Methylcobalamin: Insight from CASSCF/MC-XQDPT2, EOM-CCSD, and TD-DFT Calculations J. Comput. Chem. 2013, 34, 987-1004
    • (2013) J. Comput. Chem. , vol.34 , pp. 987-1004
    • Kornobis, K.1    Kumar, N.2    Lodowski, P.3    Jaworska, M.4    Piecuch, P.5    Lutz, J.J.6    Wong, B.M.7    Kozlowski, P.M.8
  • 56
    • 84860184198 scopus 로고    scopus 로고
    • Charge Separation Propensity of the Coenzyme B12-Tyrosine Complex in Adenosylcobalamin-Dependent Methylmalonyl-CoA Mutase Enzyme
    • Kumar, N.; Liu, S.; Kozlowski, P. M. Charge Separation Propensity of the Coenzyme B12-Tyrosine Complex in Adenosylcobalamin-Dependent Methylmalonyl-CoA Mutase Enzyme J. Phys.Chem. Lett. 2012, 3, 1035-1038
    • (2012) J. Phys.Chem. Lett. , vol.3 , pp. 1035-1038
    • Kumar, N.1    Liu, S.2    Kozlowski, P.M.3
  • 57
    • 79951836039 scopus 로고    scopus 로고
    • Electronically Excited States of Vitamin B12: Benchmark Calculations Including Time-Dependent Density Functional Theory and Correlated ab Initio Methods
    • Kornobis, K.; Kumar, N.; Wong, B. M.; Lodowski, P.; Jaworska, M.; Andruniow, T.; Ruud, K.; Kozlowski, P. M. Electronically Excited States of Vitamin B12: Benchmark Calculations Including Time-Dependent Density Functional Theory and Correlated ab Initio Methods J. Phys. Chem. A 2011, 115, 1280-1292
    • (2011) J. Phys. Chem. A , vol.115 , pp. 1280-1292
    • Kornobis, K.1    Kumar, N.2    Wong, B.M.3    Lodowski, P.4    Jaworska, M.5    Andruniow, T.6    Ruud, K.7    Kozlowski, P.M.8
  • 58
    • 77349115125 scopus 로고    scopus 로고
    • P450 Enzymes: Their Structure, Reactivity, and Selectivity - Modeled by QM/MM Calculations
    • Shaik, S.; Cohen, S.; Wang, Y.; Chen, H.; Kumar, D.; Thiel, W. P450 Enzymes: Their Structure, Reactivity, and Selectivity-Modeled by QM/MM Calculations Chem. Rev. 2009, 110, 949-1017
    • (2009) Chem. Rev. , vol.110 , pp. 949-1017
    • Shaik, S.1    Cohen, S.2    Wang, Y.3    Chen, H.4    Kumar, D.5    Thiel, W.6
  • 59
    • 77956092331 scopus 로고    scopus 로고
    • ONIOM Study on a Missing Piece in Our Understanding of Heme Chemistry: Bacterial Tryptophan 2,3-Dioxygenase with Dual Oxidants
    • Chung, L. W.; Li, X.; Sugimoto, H.; Shiro, Y.; Morokuma, K. ONIOM Study on a Missing Piece in Our Understanding of Heme Chemistry: Bacterial Tryptophan 2,3-Dioxygenase with Dual Oxidants J. Am. Chem. Soc. 2010, 132, 11993-12005
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11993-12005
    • Chung, L.W.1    Li, X.2    Sugimoto, H.3    Shiro, Y.4    Morokuma, K.5
  • 61
    • 57649094924 scopus 로고    scopus 로고
    • Cobalamin-Dependent and Cobamide-Dependent Methyltransferases
    • Matthews, R. G.; Kutmos, M.; Datta, S. Cobalamin-Dependent and Cobamide-Dependent Methyltransferases Curr. Opin. Struct. Biol. 2008, 18, 658-666
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 658-666
    • Matthews, R.G.1    Kutmos, M.2    Datta, S.3
  • 62
    • 0242666823 scopus 로고    scopus 로고
    • Conversion of Homocysteine to Methionine by Methionine Synthase: A Density Functional Study
    • Jensen, K. P.; Ryde, U. Conversion of Homocysteine to Methionine by Methionine Synthase: A Density Functional Study J. Am. Chem. Soc. 2003, 125, 13970-13971
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13970-13971
    • Jensen, K.P.1    Ryde, U.2
  • 63
    • 0003467672 scopus 로고
    • In, 4 th ed. John Wiley & Sons: New York
    • March, J. In Advanced Organic Chemistry, 4 th ed.; John Wiley & Sons: New York, 1992; pp 250-252.
    • (1992) Advanced Organic Chemistry , pp. 250-252
    • March, J.1
  • 64
    • 77957828811 scopus 로고    scopus 로고
    • Reductive Cleavage Mechanism of Co-C Bond in Cobalamin-Dependent Methionine Synthase
    • Alfonso-Prieto, M.; Biarnes, X.; Kumar, M.; Rovira, C.; Kozlowski, P. M. Reductive Cleavage Mechanism of Co-C Bond in Cobalamin-Dependent Methionine Synthase J. Phys. Chem. B 2010, 114, 12965-12971
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12965-12971
    • Alfonso-Prieto, M.1    Biarnes, X.2    Kumar, M.3    Rovira, C.4    Kozlowski, P.M.5
  • 65
    • 79955892772 scopus 로고    scopus 로고
    • Electronic Structure of Cofactor-Substrate Reactant Complex Involved in the Methyl Transfer Reaction Catalyzed by Cobalamin-Dependent Methionine Synthase
    • Kumar, N.; Jaworska, M.; Lodowski, P.; Kumar, M.; Kozlowski, P. M. Electronic Structure of Cofactor-Substrate Reactant Complex Involved in the Methyl Transfer Reaction Catalyzed by Cobalamin-Dependent Methionine Synthase J. Phys. Chem. B 2011, 115, 6722-6731
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6722-6731
    • Kumar, N.1    Jaworska, M.2    Lodowski, P.3    Kumar, M.4    Kozlowski, P.M.5
  • 66
    • 0024364303 scopus 로고
    • Cloning and Sequence Analysis of the Escherichia coli MetH Gene Encoding Cobalamin-Dependent Methionine Synthase and Isolation of a Tryptic Fragment Containing the Cobalamin-Binding Domain
    • Banerjee, R. V.; Johnston, N. L.; Sobeski, J. K.; Datta, P.; Matthews, R. G. Cloning and Sequence Analysis of the Escherichia coli MetH Gene Encoding Cobalamin-Dependent Methionine Synthase and Isolation of a Tryptic Fragment Containing the Cobalamin-Binding Domain J. Biol. Chem. 1989, 264, 13888-13895
    • (1989) J. Biol. Chem. , vol.264 , pp. 13888-13895
    • Banerjee, R.V.1    Johnston, N.L.2    Sobeski, J.K.3    Datta, P.4    Matthews, R.G.5
  • 67
    • 0347717891 scopus 로고    scopus 로고
    • Cobalamin-Dependent and Cobalamin-Independent Methionine Synthases: Are There Two Solutions to the Same Chemical Problem?
    • Matthews, R. G.; Smith, A. E.; Zhou, Z. S.; Taurog, R. E.; Bandarian, V.; Evans, J. C.; Ludwig, M. Cobalamin-Dependent and Cobalamin-Independent Methionine Synthases: Are There Two Solutions to the Same Chemical Problem? Helv. Chim. Acta 2003, 86, 3939-3954
    • (2003) Helv. Chim. Acta , vol.86 , pp. 3939-3954
    • Matthews, R.G.1    Smith, A.E.2    Zhou, Z.S.3    Taurog, R.E.4    Bandarian, V.5    Evans, J.C.6    Ludwig, M.7
  • 68
    • 0028075318 scopus 로고
    • The Reductive Acetyl Coenzyme A Pathway: Sequence and Heterologous Expression of Active Methyltetrahydrofolate:Corrinoid/Iron-Sulfur Protein Methyltransferase from Clostridium thermoaceticum
    • Roberts, D. L.; Zhao, S.; Doukov, T.; Ragsdale, S. W. The Reductive Acetyl Coenzyme A Pathway: Sequence and Heterologous Expression of Active Methyltetrahydrofolate:Corrinoid/Iron-Sulfur Protein Methyltransferase from Clostridium thermoaceticum J. Bacteriol. 1994, 176, 6127-6130
    • (1994) J. Bacteriol. , vol.176 , pp. 6127-6130
    • Roberts, D.L.1    Zhao, S.2    Doukov, T.3    Ragsdale, S.W.4
  • 69
    • 0028988304 scopus 로고
    • The Energy Conserving N5-Methyltetrahydromethanopterin:Coenzyme M Methyltransferase Complex from Methanobacterium thermoautotrophicum is Composed of Eight Different Subunits
    • Harms, U.; Weiss, D. S.; Gärtner, P.; Linder, D.; Thauer, R. K. The Energy Conserving N5-Methyltetrahydromethanopterin:Coenzyme M Methyltransferase Complex from Methanobacterium thermoautotrophicum is Composed of Eight Different Subunits Eur. J. Biochem. 1995, 228, 640-648
    • (1995) Eur. J. Biochem. , vol.228 , pp. 640-648
    • Harms, U.1    Weiss, D.S.2    Gärtner, P.3    Linder, D.4    Thauer, R.K.5
  • 70
    • 0033551086 scopus 로고    scopus 로고
    • A Corrinoid-Dependent Catabolic Pathway for Growth of a Methylobacterium Strain with Chloromethane
    • Vannelli, T.; Messmer, M.; Studer, A.; Vuilleumier, S.; Leisinger, T. A Corrinoid-Dependent Catabolic Pathway for Growth of a Methylobacterium Strain with Chloromethane Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 4615-4620
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4615-4620
    • Vannelli, T.1    Messmer, M.2    Studer, A.3    Vuilleumier, S.4    Leisinger, T.5
  • 71
    • 0031799184 scopus 로고    scopus 로고
    • Clustered Genes Encoding the Methyltransferases of Methanogenesis from Monomethylamine
    • Burke, S. A.; Lo, S. L.; Krzycki, J. A. Clustered Genes Encoding the Methyltransferases of Methanogenesis from Monomethylamine J. Bacteriol. 1998, 180, 3432-3440
    • (1998) J. Bacteriol. , vol.180 , pp. 3432-3440
    • Burke, S.A.1    Lo, S.L.2    Krzycki, J.A.3
  • 72
    • 33846809521 scopus 로고    scopus 로고
    • Insight into the Mechanism of Biological Methanol Activation Based on the Crystal Structure of the Methanol-Cobalamin Methyltransferase Complex
    • Hagemeier, C. H.; Kruer, M.; Thauer, R. K.; Warkentin, E.; Ermler, U. Insight into the Mechanism of Biological Methanol Activation Based on the Crystal Structure of the Methanol-Cobalamin Methyltransferase Complex Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 18917-18922
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18917-18922
    • Hagemeier, C.H.1    Kruer, M.2    Thauer, R.K.3    Warkentin, E.4    Ermler, U.5
  • 73
    • 0030879503 scopus 로고    scopus 로고
    • Methanol: Coenzyme M Methyltransferase from Methanosarcina Barkeri
    • Sauer, K.; Thauer, R. K. Methanol: Coenzyme M Methyltransferase from Methanosarcina Barkeri Eur. J. Biochem. 1997, 249, 280-285
    • (1997) Eur. J. Biochem. , vol.249 , pp. 280-285
    • Sauer, K.1    Thauer, R.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.