메뉴 건너뛰기




Volumn 36, Issue 1, 2003, Pages 91-145

Mechanisms of metalloenzymes studied by quantum chemical methods

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; METHANE MONOOXYGENASE; MONOPHENOL MONOOXYGENASE; OXYGEN; RIBONUCLEOTIDE REDUCTASE; TRANSITION ELEMENT;

EID: 0037295343     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0033583502003827     Document Type: Review
Times cited : (187)

References (129)
  • 2
    • 0000684952 scopus 로고
    • The oxygen-evolving complex in photosystem II as a metallo-radical enzyme
    • (ed. P. Mathis). Dordrecht: Kluwer
    • BABCOCK, G. T. (1995). The oxygen-evolving complex in photosystem II as a metallo-radical enzyme. In Photosynthesis from light to Biosphere, vol. 2 (ed. P. Mathis), pp. 209. Dordrecht: Kluwer.
    • (1995) Photosynthesis From Light to Biosphere , vol.2 , pp. 209
    • Babcock, G.T.1
  • 3
    • 0000502480 scopus 로고
    • Isopenicillin N synthase: Mechanistic studies
    • BALDWIN, J. E. & BRADLEY, M. (1990). Isopenicillin N synthase: mechanistic studies. Chem. Rev. 90, 1079-1088.
    • (1990) Chem. Rev. , vol.90 , pp. 1079-1088
    • Baldwin, J.E.1    Bradley, M.2
  • 4
    • 0034645606 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical
    • BALDWIN, J., KREBS, C., LEY, B. A., EDMONDSON, D. E., HUYNH, B. H. & BOLLINGER, JR., J. M. (2000). Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical. J. Am. chem. Soc. 122, 12195-12206.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12195-12206
    • Baldwin, J.1    Krebs, C.2    Ley, B.A.3    Edmondson, D.E.4    Huynh, B.H.5    Bollinger J.M., Jr.6
  • 5
    • 0033546705 scopus 로고    scopus 로고
    • The mechanism of the methane to methanol conversion reaction catalyzed by methane monooxygenase (MMO): A density functional study
    • BASCH, H., MOGI, K., MUSAEV, D. G. & MOROKUMA, K. (1999). The mechanism of the methane to methanol conversion reaction catalyzed by methane monooxygenase (MMO): a density functional study. J. Am. chem. Soc. 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
  • 6
    • 0035849242 scopus 로고    scopus 로고
    • Theoretical studies on the mechanism of the methane to methanol conversion reaction catalyzed by methane monooxygenase: O-side vs N-side mechanisms
    • BASCH, H., MUSAEV, D. G., MOGI, K. & MOROKUMA, K. (2001). Theoretical studies on the mechanism of the methane to methanol conversion reaction catalyzed by methane monooxygenase: O-side vs N-side mechanisms. J. phys. Chem. (A) 105, 3615-3622.
    • (2001) J. Phys. Chem. (A) , vol.105 , pp. 3615-3622
    • Basch, H.1    Musaev, D.G.2    Mogi, K.3    Morokuma, K.4
  • 7
    • 85052276626 scopus 로고    scopus 로고
    • The mechanism for dioxygen bond-cleavage in tetrahydropterin-dependent amino acid hydroxylases
    • In Press
    • BASSAN, A., BLOMBERG, M. R. A. & SIEGBAHN, P. E. M. (In Press). The mechanism for dioxygen bond-cleavage in tetrahydropterin-dependent amino acid hydroxylases. Chem. Eur. J.
    • Chem. Eur. J.
    • Bassan, A.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 9
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • BECKE, A. D. (1988). Density-functional exchange-energy approximation with correct asymptotic behavior. Phys. Rev. (A) 38, 3098.
    • (1988) Phys. Rev. (A) , vol.38 , pp. 3098
    • Becke, A.D.1
  • 10
    • 77956779984 scopus 로고
    • Density-functional thermochemistry. I. The effect of the exchange-only gradient correction
    • BECKE, A. D. (1992a). Density-functional thermochemistry. I. The effect of the exchange-only gradient correction. J. chem. Phys. 96, 2155-2160.
    • (1992) J. Chem. Phys. , vol.96 , pp. 2155-2160
    • Becke, A.D.1
  • 11
    • 0001161681 scopus 로고
    • Density-functional thermochemistry. II. The effect of the Perdew-Wang generalizedgradient correlation correction
    • BECKE, A. D. (1992b). Density-functional thermochemistry. II. The effect of the Perdew-Wang generalizedgradient correlation correction. J. chem. Phys. 97, 9173-9177.
    • (1992) J. Chem. Phys. , vol.97 , pp. 9173-9177
    • Becke, A.D.1
  • 12
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • BECKE, A. D. (1993). Density-functional thermochemistry. III. The role of exact exchange. J. chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 13
    • 0000704744 scopus 로고    scopus 로고
    • Optimized density functionals from the extended G2 test set
    • BECKE, A. D. (1998). Optimized density functionals from the extended G2 test set. J. chem. Phys. 108, 9624-9631.
    • (1998) J. Chem. Phys. , vol.108 , pp. 9624-9631
    • Becke, A.D.1
  • 14
    • 0038021215 scopus 로고    scopus 로고
    • Ligand effects in the models and mimics of oxohemocyanin and oxytyrosinase. A density functional study of reversible dioxygen binding and reversible O - O bond cleavage
    • BÉRCES, S. A. (1997). Ligand effects in the models and mimics of oxohemocyanin and oxytyrosinase. A density functional study of reversible dioxygen binding and reversible O - O bond cleavage. Inorg. Chem. 36, 4831-4837.
    • (1997) Inorg. Chem. , vol.36 , pp. 4831-4837
    • Bérces, A.1
  • 16
    • 0035807631 scopus 로고    scopus 로고
    • A quantum chemical approach to the study of reaction mechanisms of redox-active metalloenzymes
    • BLOMBERG, M. R. A. & SIEGBAHN, P. E. M. (2001). A quantum chemical approach to the study of reaction mechanisms of redox-active metalloenzymes. J. phys. Chem. (B) 105, 9375-9386.
    • (2001) J. Phys. Chem. (B) , vol.105 , pp. 9375-9386
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2
  • 18
    • 0034722941 scopus 로고    scopus 로고
    • Modeling cytochrome oxidase - A quantum chemical study of the O - O bond cleavage mechanism
    • BLOMBERG, M. R. A., SIEGBAHN, P. E. M., BABCOCK, G. T. & WIKSTRÖM, M. (2000b). Modeling cytochrome oxidase - a quantum chemical study of the O - O bond cleavage mechanism. J. Am. chem. Soc. 122, 12848-12858.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12848-12858
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2    Babcock, G.T.3    Wikström, M.4
  • 19
    • 0030755238 scopus 로고    scopus 로고
    • A quantum chemical study of hydrogen abstraction from coordinated water by a tyrosyl radical: A model for water oxidation in photosystem II
    • BLOMBERG, M. R. A., SIEGBAHN, P. E. M., STYRING, S., BABCOCK, G. T., ÅKERMARK, B. & KORALL, P. (1997). A quantum chemical study of hydrogen abstraction from coordinated water by a tyrosyl radical: a model for water oxidation in photosystem II. J. Am. chem. Soc. 119, 8285-8292.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8285-8292
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2    Styring, S.3    Babcock, G.T.4    Åkermark, B.5    Korall, P.6
  • 20
    • 0000837297 scopus 로고    scopus 로고
    • Comparisons of results from parametrized configuration interaction (PCI-80) and from hybrid density functional theory with experiments for first row transition metal compounds
    • BLOMBERG, M. R. A., SIEGBAHN, P. E. M. & SVENSSON, M. (1996). Comparisons of results from parametrized configuration interaction (PCI-80) and from hybrid density functional theory with experiments for first row transition metal compounds J. chem. Phys. 104, 9546-9554.
    • (1996) J. Chem. Phys. , vol.104 , pp. 9546-9554
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2    Svensson, M.3
  • 22
    • 0033616098 scopus 로고    scopus 로고
    • Cationic species can be produced in soluble methane monooxygenasecatalyzed hydroxylation reactions; radical intermediates are not involved
    • CHOI, S.-Y., EATON, P. E., KOPP, D. A., LIPPARD, S. J., NEWCOMB, M. & SHEN, R. (1999). Cationic species can be produced in soluble methane monooxygenasecatalyzed hydroxylation reactions; radical intermediates are not involved. J. Am. chem. Soc. 121, 12198-12199.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12198-12199
    • Choi, S.-Y.1    Eaton, P.E.2    Kopp, D.A.3    Lippard, S.J.4    Newcomb, M.5    Shen, R.6
  • 23
    • 0000061390 scopus 로고    scopus 로고
    • Strontium EXAFS reveals the proximity of calcium to the manganese duster of oxygen-evolving photosystem II
    • CINCO, R. M., ROBBLEE, J. H., ROMPEL, A., FERNANDEZ, C., YACHANDRA, V. K., SAUER, K. & KLEIN, M. P. (1998). Strontium EXAFS reveals the proximity of calcium to the manganese duster of oxygen-evolving photosystem II. J. phys. Chem. (B) 102, 8248-8256.
    • (1998) J. Phys. Chem. (B) , vol.102 , pp. 8248-8256
    • Cinco, R.M.1    Robblee, J.H.2    Rompel, A.3    Fernandez, C.4    Yachandra, V.K.5    Sauer, K.6    Klein, M.P.7
  • 24
    • 0000992156 scopus 로고
    • Approximate calculation of the correlation energy for the closed shells
    • COLLE, R. & SALVETTI, O. (1975). Approximate calculation of the correlation energy for the closed shells. Theoret. Chim. Acta 37, 329-334.
    • (1975) Theoret. Chim. Acta , vol.37 , pp. 329-334
    • Colle, R.1    Salvetti, O.2
  • 26
    • 0041401966 scopus 로고
    • Gaussian-2 theory for molecular energies of first- and second-row compounds
    • CURTISS, L. A., RAGLAWACHARI, K., TRUCKS, G. W. & POPLE, J. A. (1991). Gaussian-2 theory for molecular energies of first- and second-row compounds. J. chem. Phys. 94, 7221.
    • (1991) J. Chem. Phys. , vol.94 , pp. 7221
    • Curtiss, L.A.1    Raglawachari, K.2    Trucks, G.W.3    Pople, J.A.4
  • 27
    • 37049067856 scopus 로고
    • Substrate radical intermediates are involved in the soluble methane monooxygemase catalyzed oxidations of methane, methanol and acetonitrile
    • DEIGHTON, N., PODMORE, I. D., SYMONS, M. C. R., WILKINS, P. C. & DALTON, H. (1991). Substrate radical intermediates are involved in the soluble methane monooxygemase catalyzed oxidations of methane, methanol and acetonitrile. J. chem. Soc. chem. Comm. 1086-1088.
    • (1991) J. Chem. Soc. Chem. Comm. , pp. 1086-1088
    • Deighton, N.1    Podmore, I.D.2    Symons, M.C.R.3    Wilkins, P.C.4    Dalton, H.5
  • 28
    • 0032957263 scopus 로고    scopus 로고
    • Structure and biogenesis of topaquinone and related cofactors
    • DOOLEY, D. M. (1999). Structure and biogenesis of topaquinone and related cofactors. J. biol. inorg. Chem. 4, 1-11.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 1-11
    • Dooley, D.M.1
  • 29
    • 0034728629 scopus 로고    scopus 로고
    • Large scale ab initio quantum chemical calculation of the intermediates in the soluble methane monooxygenase catalytic cycle
    • DUNIETZ, B. D., BEACHY, M. D., CAO, Y., WHITTINGTON, D. A., LIPPARD, S. J. & FRIESNER, R. A. (2000). Large scale ab initio quantum chemical calculation of the intermediates in the soluble methane monooxygenase catalytic cycle. J. Am. chem. Soc. 122, 2828-2839.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2828-2839
    • Dunietz, B.D.1    Beachy, M.D.2    Cao, Y.3    Whittington, D.A.4    Lippard, S.J.5    Friesner, R.A.6
  • 30
    • 0034093759 scopus 로고    scopus 로고
    • Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase
    • ERLANDSEN, H., BJØRGO, E., FLATMARK, T. & STEVENS, R. C. (2000). Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase. Biochemistry 39, 2208-2217.
    • (2000) Biochemistry , vol.39 , pp. 2208-2217
    • Erlandsen, H.1    BjØrgo, E.2    Flatmark, T.3    Stevens, R.C.4
  • 31
    • 0000313831 scopus 로고
    • Active-site mutations in cytochrome c peroxidase: A critical role for histidine-52 in the rate of formation of compound I
    • ERMAN, J. E. & VITELLO, L. B. (1992). Active-site mutations in cytochrome c peroxidase: a critical role for histidine-52 in the rate of formation of compound I. J. Am. chem. Soc. 114, 6592-6593.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6592-6593
    • Erman, J.E.1    Vitello, L.B.2
  • 32
    • 0030726657 scopus 로고    scopus 로고
    • Crystal structure of methylcoenzyme M reductase: The key enzyme of biological methane formation
    • ERMLER, U., GRABARSE, W., SHIMA, S., GOUBEAUD, M. & THAUER, R. K. (1997). Crystal structure of methylcoenzyme M reductase: the key enzyme of biological methane formation. Science 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
  • 33
    • 0009411657 scopus 로고
    • Reactions of nonheme iron(II) centers with dioxygen in biology and chemistry
    • FEIG, A. L. & LIPPARD, S. J. (1994). Reactions of nonheme iron(II) centers with dioxygen in biology and chemistry. Chem. Rev. 94, 759-805.
    • (1994) Chem. Rev. , vol.94 , pp. 759-805
    • Feig, A.L.1    Lippard, S.J.2
  • 34
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7 Å resolution
    • FINZEL, B. C., POULUS, T. L. & KRAUT, J. (1984). Crystal structure of yeast cytochrome c peroxidase refined at 1.7 Å resolution. J. biol. Chem. 259, 13027.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027
    • Finzel, B.C.1    Poulus, T.L.2    Kraut, J.3
  • 35
    • 0001749787 scopus 로고    scopus 로고
    • Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
    • FLATMARK, T. & STEVENS, R. C. (1999). Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms. Chem. Rev. 99, 2137-2160.
    • (1999) Chem. Rev. , vol.99 , pp. 2137-2160
    • Flatmark, T.1    Stevens, R.C.2
  • 37
    • 1542356431 scopus 로고    scopus 로고
    • Solvent effects 5. The influence of cavity shape, truncation of electrostatics, and electron correlation on ab initio reaction field calculations
    • FORESMAN, J. B., KEITH, T. A., WIBERG, K. B., SNOONIAN, J. & FRISCH, M. J. (1996). Solvent effects 5. The influence of cavity shape, truncation of electrostatics, and electron correlation on ab initio reaction field calculations. J. phys. Chem. 100, 16098.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16098
    • Foresman, J.B.1    Keith, T.A.2    Wiberg, K.B.3    Snoonian, J.4    Frisch, M.J.5
  • 40
    • 0029654151 scopus 로고
    • - transfer in the oxidation of toluene by permanganate
    • - transfer in the oxidation of toluene by permanganate. Science 269, 1849-1851.
    • (1995) Science , vol.269 , pp. 1849-1851
    • Gardner, K.A.1    Mayer, J.M.2
  • 41
    • 0034836363 scopus 로고    scopus 로고
    • Activation of the C - H bond of methane by intermediate Q of methane monooxygenase: A theoretical study
    • GHERMAN, B. F., DUNIETZ, B. D., WHITTINGTON, D. A., LIPPARD, S. J. & FRIESNER, F. A. (2001). Activation of the C - H bond of methane by intermediate Q of methane monooxygenase: a theoretical study. J. Am. chem. Soc. 123, 3836-3837.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3836-3837
    • Gherman, B.F.1    Dunietz, B.D.2    Whittington, D.A.3    Lippard, S.J.4    Friesner, F.A.5
  • 42
    • 0032578427 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: Self-hydroxylation of Phe300 and the pterin-binding site
    • GOODWILL, K. E., SABATIER, C. & STEVENS, R. C. (1998). Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: self-hydroxylation of Phe300 and the pterin-binding site. Biochemistry 37, 13437-13445.
    • (1998) Biochemistry , vol.37 , pp. 13437-13445
    • Goodwill, K.E.1    Sabatier, C.2    Stevens, R.C.3
  • 43
    • 0037012442 scopus 로고    scopus 로고
    • Dynamics of alkane hydroxylation at the non-heme diiron center in methane monooxygenase
    • GUALLAR, V., GHERMAN, B. F., MILLER, W. H., LIPPARD, S. J., FRIESNER, R. A. (2002). Dynamics of alkane hydroxylation at the non-heme diiron center in methane monooxygenase. J. Am. chem. Soc. 124, 3377-3384.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3377-3384
    • Guallar, V.1    Gherman, B.F.2    Miller, W.H.3    Lippard, S.J.4    Friesner, R.A.5
  • 44
    • 0001652762 scopus 로고    scopus 로고
    • Development and assessment of new exchange-correlation functionals
    • HAMPRECHT, F. A., COHEN, A., TOZER, D. J. & HANDY, N. C. (1998). Development and assessment of new exchange-correlation functionals. J. chem. Phys. 109, 6264-6271.
    • (1998) J. Chem. Phys. , vol.109 , pp. 6264-6271
    • Hamprecht, F.A.1    Cohen, A.2    Tozer, D.J.3    Handy, N.C.4
  • 45
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-l-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • HEGG, E. L. & QUE, JR., L. (1997). The 2-His-l-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur. J. Biochem. 250, 625-629.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que L., Jr.2
  • 46
    • 0034706037 scopus 로고    scopus 로고
    • Catalytic mechanism of galactose oxidase. A theoretical study
    • HIMO, F., ERIKSSON, L. A., MASERAS, F. & SIEGBAHN, P. E. M. (2000). Catalytic mechanism of galactose oxidase, A theoretical study. J. Am. chem. Soc. 122, 8031-8036.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8031-8036
    • Himo, F.1    Eriksson, L.A.2    Maseras, F.3    Siegbahn, P.E.M.4
  • 47
    • 0034248628 scopus 로고    scopus 로고
    • A very stable substrate radical relevant for class I ribonucleotide reductase (RNR)
    • HIMO, F. & SIEGBAHN, P. E. M. (2000). A very stable substrate radical relevant for class I ribonucleotide reductase (RNR). J. phys. Chem. 104, 7502-7509.
    • (2000) J. Phys. Chem. , vol.104 , pp. 7502-7509
    • Himo, F.1    Siegbahn, P.E.M.2
  • 49
    • 10644250257 scopus 로고
    • Inhomogeneous electron gas
    • HOHENBERG, P. & KOHN, W. (1964). Inhomogeneous electron gas. Phys. Rev. (B) 136, 864-871.
    • (1964) Phys. Rev. (B) , vol.136 , pp. 864-871
    • Hohenberg, P.1    Kohn, W.2
  • 52
    • 0003934843 scopus 로고
    • Schrödinger, Inc., Portland, OR
    • JAGUAR 4.0 (1991-2000). Schrödinger, Inc., Portland, OR.
    • (1991) JAGUAR 4.0
  • 53
    • 0000783838 scopus 로고    scopus 로고
    • Pterin-dependent amino acid hydroxylases
    • KAPPOCK, T. J. & CARADONNA, J. P. (1996). Pterin-dependent amino acid hydroxylases. Chem. Rev. 96, 2659-2756.
    • (1996) Chem. Rev. , vol.96 , pp. 2659-2756
    • Kappock, T.J.1    Caradonna, J.P.2
  • 54
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • KLABUNDE, T., EICKEN, C., SACCETTINI, J. C. & KREBS, B. (1998). Crystal structure of a plant catechol oxidase containing a dicopper center. Nature struct. Biol. 5, 1084-1090.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Saccettini, J.C.3    Krebs, B.4
  • 55
  • 56
    • 0001482056 scopus 로고    scopus 로고
    • Density functional theory applications to transition metal problems
    • (Editor-in-chief P. v. R. Schleyer). Chichester: Wiley
    • KOCH, W. & HERTWIG, R. H. (1998). Density functional theory applications to transition metal problems. In Encyclopedia of Computational Chemistry (Editor-in-chief P. v. R. Schleyer). Chichester: Wiley.
    • (1998) Encyclopedia of Computational Chemistry
    • Koch, W.1    Hertwig, R.H.2
  • 57
    • 0042113153 scopus 로고
    • Self-consistent equations including exchange and correlation effects
    • KOHN, W. & SHAM, L. J. (1965). Self-consistent equations including exchange and correlation effects. Phys. Rev. (A) 140, 1133-1138.
    • (1965) Phys. Rev. (A) , vol.140 , pp. 1133-1138
    • Kohn, W.1    Sham, L.J.2
  • 58
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation energy formula into a functional of the electron density
    • LEE, C., YANG, W. & PARR, R. G. (1988). Development of the Colle-Salvetti correlation energy formula into a functional of the electron density. Phys. Rev. (B) 37, 785-789.
    • (1988) Phys. Rev. (B) , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 59
    • 0021455512 scopus 로고
    • Organometallic bond dissociation energies: Laser pyrolysis of iron pentacarbonyl, chromium hexacarbonyl, molybdenum hexacarbonyl, and tungsten hexacarbonyl
    • LEWIS, K. E., GOLDEN, D. M. & SMITH, G. P. (1984). Organometallic bond dissociation energies: laser pyrolysis of iron pentacarbonyl, chromium hexacarbonyl, molybdenum hexacarbonyl, and tungsten hexacarbonyl. J. Am. chem. Soc. 106, 3905-3912.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 3905-3912
    • Lewis, K.E.1    Golden, D.M.2    Smith, G.P.3
  • 60
    • 0000769188 scopus 로고
    • 6 (M = Cr, Mo, W) revisited: The performance of density functional theory and the influence of relativistic effects
    • 6 (M = Cr, Mo, W) revisited: the performance of density functional theory and the influence of relativistic effects. J. phys. Chem. 98, 4838-4841.
    • (1994) J. Phys. Chem. , vol.98 , pp. 4838-4841
    • Li, J.1    Schreckenbach, G.2    Ziegler, T.3
  • 62
    • 0000093330 scopus 로고    scopus 로고
    • A quantum chemical study of the mechanism of tyrosinase
    • LIND, T., SIEGBAHN, P. E. M. & CRABTREE, R. H. (1999). A quantum chemical study of the mechanism of tyrosinase. J. phys. Chem. 103, 1193-1202.
    • (1999) J. Phys. Chem. , vol.103 , pp. 1193-1202
    • Lind, T.1    Siegbahn, P.E.M.2    Crabtree, R.H.3
  • 64
    • 0000353336 scopus 로고
    • Radical clock substrate probes and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane monooxygenase
    • LIU, K. E., JOHNSON, C. C., NEWCOMB, M. & LIPPARD, S. J. (1993). Radical clock substrate probes and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane monooxygenase. J. Am. chem. Soc. 115, 939-947.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 939-947
    • Liu, K.E.1    Johnson, C.C.2    Newcomb, M.3    Lippard, S.J.4
  • 65
    • 0029776459 scopus 로고    scopus 로고
    • Large kinetic isotope effects in methane oxidation catalyzed by methane monooxygenase: Evidence for C - H bond cleavage in a reaction cycle intermediate
    • NESHIEM, J. C. & LIPSCOMB, J. D. (1996). Large kinetic isotope effects in methane oxidation catalyzed by methane monooxygenase: Evidence for C - H bond cleavage in a reaction cycle intermediate. Biochemistry 35, 10240-10247.
    • (1996) Biochemistry , vol.35 , pp. 10240-10247
    • Neshiem, J.C.1    Lipscomb, J.D.2
  • 66
    • 0034728622 scopus 로고    scopus 로고
    • Cytochrome P450-catalyzed hydroxylation of mechanistic probes that distinguish between radicals and cations. Evidence for cationic but not for radical intermediates
    • NEWCOMB, M., SHEN, R., CHOI, S.-Y., TOY, P. H., HOLLENBERG, P. F., VAZ, A. D. & COON, M. J. (2000). Cytochrome P450-catalyzed hydroxylation of mechanistic probes that distinguish between radicals and cations. Evidence for cationic but not for radical intermediates. J. Am. chem. Soc. 122, 2677-2686.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2677-2686
    • Newcomb, M.1    Shen, R.2    Choi, S.-Y.3    Toy, P.H.4    Hollenberg, P.F.5    Vaz, A.D.6    Coon, M.J.7
  • 67
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • NORDLUND, P. & EKLUND, H. (1993). Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. molec. Biol. 232, 123-164.
    • (1993) J. Molec. Biol. , vol.232 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 68
    • 0002439105 scopus 로고    scopus 로고
    • Structure-function of nonheme iron proteins with oxygen- and nitrogen-dominated coordination
    • (eds. I. Bertini, A. Sigel & H. Sigel). New York: Marcel Dekker
    • NORDLUND, P. (2001). Structure-function of nonheme iron proteins with oxygen- and nitrogen-dominated coordination. In Handbook of Metalloproteins (eds. I. Bertini, A. Sigel & H. Sigel), pp. 461-570. New York: Marcel Dekker.
    • (2001) Handbook of Metalloproteins , pp. 461-570
    • Nordlund, P.1
  • 69
    • 0024296029 scopus 로고    scopus 로고
    • Structure and assembly of protocatechuate 3,4-dioxygenase
    • OHLENDORF, D. H., LIPSCOMB, J. D. & WEBER, P. C. (1998). Structure and assembly of protocatechuate 3,4-dioxygenase. Nature 336, 403-405.
    • (1998) Nature , vol.336 , pp. 403-405
    • Ohlendorf, D.H.1    Lipscomb, J.D.2    Weber, P.C.3
  • 70
    • 0030773396 scopus 로고    scopus 로고
    • 2, NO and CO by electrostatic interactions with the bound ligand
    • 2, NO and CO by electrostatic interactions with the bound ligand. J. biol. inorg. Chem. 2, 544-552.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 544-552
    • Olson, J.S.1    Philips G.N., Jr.2
  • 73
    • 0037123266 scopus 로고    scopus 로고
    • A mechanism for methane formation in methanogenesis from quantum chemical studies
    • PELMENSCHIKOV, V., BLOMBERG, M. R. A., SIEGBAHN, P. E. M. & CRABTREE, R. H. (2002a). A mechanism for methane formation in methanogenesis from quantum chemical studies. J. Am. chem. Soc. 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
  • 74
    • 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. (2002b). A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J. biol. inorg. Chem. 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
  • 75
    • 0037020639 scopus 로고    scopus 로고
    • Catalytical mechanism of matrix metalloproteinases: Two-layered ONIOM study
    • In Press
    • PELMENSCHIKOV, V. & SIEGBAHN, P. E. M. (In Press). Catalytical mechanism of matrix metalloproteinases: two-layered ONIOM study. Inorg. Chem.
    • Inorg. Chem.
    • Pelmenschikov, V.1    Siegbahn, P.E.M.2
  • 77
    • 26144450583 scopus 로고
    • Self-interaction correction to density functional approximations for manyelectron systems
    • PERDEW, J. P. & ZUNGER, A. (1981). Self-interaction correction to density functional approximations for manyelectron systems. Phys. Rev. (B) 23, 5048-5079.
    • (1981) Phys. Rev. (B) , vol.23 , pp. 5048-5079
    • Perdew, J.P.1    Zunger, A.2
  • 78
    • 5944261746 scopus 로고
    • Density-functional approximation for the correlation energy of the inhomogeneous electron gas
    • PERDEW, J. P. (1986). Density-functional approximation for the correlation energy of the inhomogeneous electron gas. Phys. Rev. (B) 33, 8822-8824.
    • (1986) Phys. Rev. (B) , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 79
    • 33645898818 scopus 로고
    • Accurate and simple analytic representation of the electron gas correlation energy
    • PERDEW, J. P. & WANG, Y. (1992). Accurate and simple analytic representation of the electron gas correlation energy. Phys. Rev. (B) 45, 13244.
    • (1992) Phys. Rev. (B) , vol.45 , pp. 13244
    • Perdew, J.P.1    Wang, Y.2
  • 80
    • 0035902391 scopus 로고    scopus 로고
    • A theoretical study of the mechanism for the reductive half-reaction of pea seedling amine oxidase (PSAO)
    • PRABHAKAR, R. & SIEGBAHN, P. E. M. (2001). A theoretical study of the mechanism for the reductive half-reaction of pea seedling amine oxidase (PSAO). J. phys. Chem. (B) 105, 4400-4408.
    • (2001) J. Phys. Chem. (B) , vol.105 , pp. 4400-4408
    • Prabhakar, R.1    Siegbahn, P.E.M.2
  • 81
    • 0032493345 scopus 로고    scopus 로고
    • Dioxygen activation and bond cleavage by mixed valence cytochrome c oxidase
    • PROSHLYAKOV, D. A., PRESSLER, M. A. & BABCOCK, G. T. (1998). Dioxygen activation and bond cleavage by mixed valence cytochrome c oxidase. Proc. natl. Acad. Sci. USA 95, 8020-8025.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8020-8025
    • Proshlyakov, D.A.1    Pressler, M.A.2    Babcock, G.T.3
  • 82
    • 0343986411 scopus 로고    scopus 로고
    • One motif - Many different reactions
    • QUE, L. J. (2000). One motif - many different reactions. Nature struct. Biol. 7, 182-184.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 182-184
    • Que, L.J.1
  • 86
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • ROACH, P. L., CLIFTON, I. J., HENSGENS, C. M. H., SHUBATA, N., SCHOFIELD, C. J., HADJU, J. & BALDWIN, J. E. (1997). Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 387, 827-830.
    • (1997) Nature , vol.387 , pp. 827-830
    • Roach, P.L.1    Clifton, I.J.2    Hensgens, C.M.H.3    Shubata, N.4    Schofield, C.J.5    Hadju, J.6    Baldwin, J.E.7
  • 87
    • 3242866521 scopus 로고    scopus 로고
    • Recombinant horseradish peroxidase isoenzyme C: The effect of distal haem cavity mutations (His42 to Leu and Arg38 to Leu) on compound I formation and substrate binding
    • RODRIGUEZ-LOPEZ, J. N., SMITH A. T. & THORNELEY, R. N. F. (1996). Recombinant horseradish peroxidase isoenzyme C: the effect of distal haem cavity mutations (His42 to Leu and Arg38 to Leu) on compound I formation and substrate binding. J. biol. inorg. Chem. 1, 136-142.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 136-142
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.F.3
  • 88
    • 0034017752 scopus 로고    scopus 로고
    • A comparative study of galactose oxidase and active site analogs based on QM/MM CarParinello simulations
    • ROTHLISBERGER, U., CARLONI, P., DOCLO, K. & PARINELLO, M. (2000). A comparative study of galactose oxidase and active site analogs based on QM/MM CarParinello simulations. J. biol. inorg. Chem. 5, 236-250.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 236-250
    • Rothlisberger, U.1    Carloni, P.2    Doclo, K.3    Parinello, M.4
  • 90
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structures of free form and two substrate complexes of an extradiol ringcleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102
    • SENDA, T., SUGAYAMA, K., NARITA, H., Y, YAMAMOTO, T., KIMBARA, K., FUKUDA, M., SATO, M., YANO, K. & MITSUI, Y. (1996). Three-dimensional structures of free form and two substrate complexes of an extradiol ringcleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. J. molec. Biol. 255, 735-752.
    • (1996) J. Molec. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Sugayama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 91
    • 21344458504 scopus 로고    scopus 로고
    • Electronic structure calculations for molecules containing transition metals
    • (eds. I. Prigogine & S. A. Rice). Chichester: J. Wiley
    • SIEGBAHN, P. E. M. (1996). Electronic structure calculations for molecules containing transition metals. In Advances in Chemical Physics, vol. 93, New Methods in Computational Quantum Mechanics (eds. I. Prigogine & S. A. Rice), pp. 333-387. Chichester: J. Wiley.
    • (1996) Advances in Chemical Physics, Vol. 93, New Methods in Computational Quantum Mechanics , vol.93 , pp. 333-387
    • Siegbahn, P.E.M.1
  • 92
    • 0002808803 scopus 로고    scopus 로고
    • Quantum chemical studies of transition metal catalyzed enzyme reactions
    • (ed. P. Comba & L. Banci). Dordrecht: Kluwer Academic Publishers
    • SIEGBAHN, P. E. M. (1997). Quantum chemical studies of transition metal catalyzed enzyme reactions. In Molecular Modeling and Dynamics of Bioinorganic Systems (ed. P. Comba & L. Banci), pp. 233-253. Dordrecht: Kluwer Academic Publishers.
    • (1997) Molecular Modeling and Dynamics of Bioinorganic Systems , pp. 233-253
    • Siegbahn, P.E.M.1
  • 93
    • 0032569201 scopus 로고    scopus 로고
    • A theoretical study of the substrate mechanism of ribonucleotide reductase
    • SIEGBAHN, P. E. M. (1998). A theoretical study of the substrate mechanism of ribonucleotide reductase. J. Am. chem. Soc. 120, 8417-8429.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8417-8429
    • Siegbahn, P.E.M.1
  • 94
    • 33846334797 scopus 로고    scopus 로고
    • Theoretical model studies of the iron dimer complex of MMO and RNR
    • SIEGBAHN, P. E. M. (1999). Theoretical model studies of the iron dimer complex of MMO and RNR. Inorg. Chem. 38, 2880-2889.
    • (1999) Inorg. Chem. , vol.38 , pp. 2880-2889
    • Siegbahn, P.E.M.1
  • 95
    • 0034717445 scopus 로고    scopus 로고
    • Theoretical models for the oxygen radical mechanism of water oxidation and of the water oxidizing complex of photosystem II
    • SIEGBAHN, P. E. M. (2000). Theoretical models for the oxygen radical mechanism of water oxidation and of the water oxidizing complex of photosystem II. J. inorg. Chem. 39, 2923-2935.
    • (2000) J. Inorg. Chem. , vol.39 , pp. 2923-2935
    • Siegbahn, P.E.M.1
  • 96
    • 0035606221 scopus 로고    scopus 로고
    • A quantum chemical study of the mechanism of manganese catalase
    • SIEGBAHN, P. E. M. (2001a). A quantum chemical study of the mechanism of manganese catalase. Theor. chem. Acc. 105, 197-206.
    • (2001) Theor. Chem. Acc. , vol.105 , pp. 197-206
    • Siegbahn, P.E.M.1
  • 97
    • 0035889788 scopus 로고    scopus 로고
    • Modeling aspects of mechanisms for reactions catalyzed by metalloenzymes
    • SIEGBAHN, P. E. M. (2001b). Modeling aspects of mechanisms for reactions catalyzed by metalloenzymes. J. comp. Chem. 22, 1634-1645.
    • (2001) J. Comp. Chem. , vol.22 , pp. 1634-1645
    • Siegbahn, P.E.M.1
  • 98
    • 84962425632 scopus 로고    scopus 로고
    • O - O bond cleavage and alkane hydroxylation in methane monooxygenase
    • SIEGBAHN, P. E. M. (2001c). O - O bond cleavage and alkane hydroxylation in methane monooxygenase. J. biol. inorg. Chem. 6, 27-45.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 27-45
    • Siegbahn, P.E.M.1
  • 99
    • 0037050182 scopus 로고    scopus 로고
    • A comparison of dioxygen bond-cleavage in ribonucleotide reductase (RNR) and methane monooxygenase (MMO)
    • SIEGBAHN, P. E. M. (2002). A comparison of dioxygen bond-cleavage in ribonucleotide reductase (RNR) and methane monooxygenase (MMO). Chem. Phys. Lett. 351, 311-318.
    • (2002) Chem. Phys. Lett. , vol.351 , pp. 311-318
    • Siegbahn, P.E.M.1
  • 100
    • 0001363007 scopus 로고    scopus 로고
    • Transition-metal systems in biochemistry studied by highaccuracy quantum chemical methods
    • SIEGBAHN, P. E. M. & BLOMBERG, M. R. A. (2000). Transition-metal systems in biochemistry studied by highaccuracy quantum chemical methods. Chem. Rev. 100, 421-437.
    • (2000) Chem. Rev. , vol.100 , pp. 421-437
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 101
    • 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. (1997). The mechanism of C - H activation by di-iron methane monooxygenases: quantum chemical studies. J. Am. chem. Soc. 119, 3103-3113.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3103-3113
    • Siegbahn, P.E.M.1    Crabtree, R.H.2
  • 102
    • 0033550515 scopus 로고    scopus 로고
    • Manganese oxyl radical intermediates and O - O bond formation in photosynthetic oxygen evolution and a proposed role for the calcium cofactor in photosystem II
    • SIEGBAHN, P. E. M. & CRABTREE, R. H. (1999). Manganese oxyl radical intermediates and O - O bond formation in photosynthetic oxygen evolution and a proposed role for the calcium cofactor in photosystem II. J. Am. chem. Soc. 121, 117-127.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 117-127
    • Siegbahn, P.E.M.1    Crabtree, R.H.2
  • 103
    • 0031863619 scopus 로고    scopus 로고
    • Mechanism of methane monooxygenase - A structural and quantum chemical perspective
    • SIEGBAHN, P. E. M., CRABTREE, R. H. & NORDLUND, P. (1998b). Mechanism of methane monooxygenase - a structural and quantum chemical perspective. J. biol. inorg. Chem. 3, 314-317.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 314-317
    • Siegbahn, P.E.M.1    Crabtree, R.H.2    Nordlund, P.3
  • 104
    • 0000660599 scopus 로고    scopus 로고
    • Hydrogen atom transfer in ribonucleotide reductase (RNR)
    • SIEGBAHN, P. E. M., ERIKSSON, L., HIMO, F. & PAVLOV, M. (1998a). Hydrogen atom transfer in ribonucleotide reductase (RNR). J. phys. Chem. (B) 102, 10622-10629.
    • (1998) J. Phys. Chem. (B) , vol.102 , pp. 10622-10629
    • Siegbahn, P.E.M.1    Eriksson, L.2    Himo, F.3    Pavlov, M.4
  • 105
  • 108
    • 33751157732 scopus 로고
    • Ab initio calculations of vibrational absorption and circular dichroism spectra using SCF, MP2, and density functional theory force fields
    • STEPHENS, P. J., DEVLIN, F. J., CHABALOWSKI, C. F. & FRISCH, M. J. (1994). Ab initio calculations of vibrational absorption and circular dichroism spectra using SCF, MP2, and density functional theory force fields. J. phys. Chem. 98, 11623.
    • (1994) J. Phys. Chem. , vol.98 , pp. 11623
    • Stephens, P.J.1    Devlin, F.J.2    Chabalowski, C.F.3    Frisch, M.J.4
  • 109
    • 0029740493 scopus 로고    scopus 로고
    • Reconsideration of X, the diiton intermediate formed during cofactor assembly in E. coli ribonucleotide reductase
    • STURGEON, B. E., BURDI, D., CHEN, S., HUYNH, B.-H., EDMONDSON, D. E., STUBBE, J. & HOFFMAN, B. M. (1996). Reconsideration of X, the diiton intermediate formed during cofactor assembly in E. coli ribonucleotide reductase. J. Am. chem. Soc. 118, 7551-7557.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7551-7557
    • Sturgeon, B.E.1    Burdi, D.2    Chen, S.3    Huynh, B.-H.4    Edmondson, D.E.5    Stubbe, J.6    Hoffman, B.M.7
  • 112
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • THAUER, R. K. (1998). Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiol. 144, 2377-2406.
    • (1998) Microbiol. , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 114
    • 0035902336 scopus 로고    scopus 로고
    • A density functional study of possible intermediates of the reaction of dioxygen molecule wih nonheme iron complexes. 2. 'Water-assisted' model studies
    • TORRENT, M., MUSAEV, D. G., MOROKUMA, K. & BASCH, H. (2001). A density functional study of possible intermediates of the reaction of dioxygen molecule wih nonheme iron complexes. 2. 'Water-assisted' model studies. J. phys. Chem. (B) 105, 4453-4463.
    • (2001) J. Phys. Chem. (B) , vol.105 , pp. 4453-4463
    • Torrent, M.1    Musaev, D.G.2    Morokuma, K.3    Basch, H.4
  • 115
    • 0037116512 scopus 로고    scopus 로고
    • Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monooxygenase and ribonucleotide reductase
    • TORRENT, M., VREVEN, T., MUSAEV, D. G., MOROKUMA, K., FARKAS, & SCHLEGEL, H. B. (2002). Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monooxygenase and ribonucleotide reductase. J. Am. chem. Soc. 123, 192-193.
    • (2002) J. Am. Chem. Soc. , vol.123 , pp. 192-193
    • Torrent, M.1    Vreven, T.2    Musaev, D.G.3    Morokuma, K.4    Farkas5    Schlegel, H.B.6
  • 116
    • 33748502321 scopus 로고    scopus 로고
    • Principles of small molecule activation by metalloenzymes as exemplified by the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • VALENTINE, A. M. & LIPPARD, S. J. (1997). Principles of small molecule activation by metalloenzymes as exemplified by the soluble methane monooxygenase from Methylococcus capsulatus (Bath). J. chem. Soc. Dalton Trans. 3933-3940.
    • (1997) J. Chem. Soc. Dalton Trans. , pp. 3933-3940
    • Valentine, A.M.1    Lippard, S.J.2
  • 117
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron aclusters
    • WALLAR, B. J. & LIPSCOMB, J. D. (1996). Dioxygen activation by enzymes containing binuclear non-heme iron aclusters. Chem. Rev. 96, 2625-2657.
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2657
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 118
    • 0031837180 scopus 로고    scopus 로고
    • Substrate binding and C - H bond activation in the soluble methane monooxygenase hydroxylase
    • WHITTINGTON, D. A., VALENTINE, A. M. & LIPPARD, S. J. (1998). Substrate binding and C - H bond activation in the soluble methane monooxygenase hydroxylase. J. biol. inorg. Chem. 3, 307-313.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 307-313
    • Whittington, D.A.1    Valentine, A.M.2    Lippard, S.J.3
  • 119
    • 0033520695 scopus 로고    scopus 로고
    • Reaction mechanism of compound I formation in heme peroxidases: A density functional theory study
    • WIRSTRAM, M., BLOMBERG, M. R. A. & SIEGBAHN, P. E. M. (1999). Reaction mechanism of compound I formation in heme peroxidases: a density functional theory study. J. Am. chem. Soc. 121, 10178-10185.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10178-10185
    • Wirstram, M.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 120
    • 0033832158 scopus 로고    scopus 로고
    • A mechanistic study of isopenicillin N formation using density functional theory
    • WIRSTRAM, M. & SIEGBAHN, P. E. M. (2000). A mechanistic study of isopenicillin N formation using density functional theory. J. Am. chem. Soc. 122, 8539-8547.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8539-8547
    • Wirstram, M.1    Siegbahn, P.E.M.2
  • 121
    • 0024975122 scopus 로고
    • Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution
    • VOLBEDA, A. & HOL, W. G. (1989). Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution. J. molec. Biol. 209, 249.
    • (1989) J. Molec. Biol. , vol.209 , pp. 249
    • Volbeda, A.1    Hol, W.G.2
  • 122
    • 0041920499 scopus 로고    scopus 로고
    • A novel form for the exchange-correlation energy functional
    • VAN VOORHIS, T. & SCUSERIA, G. E. (1998). A novel form for the exchange-correlation energy functional. J. chem. Phys. 109, 400-410.
    • (1998) J. Chem. Phys. , vol.109 , pp. 400-410
    • Van Voorhis, T.1    Scuseria, G.E.2
  • 123
    • 0000216001 scopus 로고
    • Accurate spin-dependent electron liquid correlation energies for local spin-density calculations: A critical analysis
    • VOSKO, S. H., WILK, L. & NUSAIR, M. (1980). Accurate spin-dependent electron liquid correlation energies for local spin-density calculations: a critical analysis. Can. J. Phys. 58, 1200-1211.
    • (1980) Can. J. Phys. , vol.58 , pp. 1200-1211
    • Vosko, S.H.1    Wilk, L.2    Nusair, M.3
  • 124
    • 0040070502 scopus 로고    scopus 로고
    • Manganese cluster in photosynthesis: Where plants oxidize water to dioxygen
    • YACHANDRA, V. K., SAUER, K. & KLEIN, M. P. (1996). Manganese cluster in photosynthesis: where plants oxidize water to dioxygen. Chem. Rev. 96, 2927-2950.
    • (1996) Chem. Rev. , vol.96 , pp. 2927-2950
    • Yachandra, V.K.1    Sauer, K.2    Klein, M.P.3
  • 126
    • 0000524754 scopus 로고    scopus 로고
    • Methane hydroxylation on a diiron model of soluble methane monooxygenase
    • YOSHIZAWA, K., OHTA, T., SHIOTA, Y. & YAMABE, T. (1998). Methane hydroxylation on a diiron model of soluble methane monooxygenase. Bull chem. Soc. Jpn. 71, 1899.
    • (1998) Bull Chem. Soc. Jpn , vol.71 , pp. 1899
    • Yoshizawa, K.1    Ohta, T.2    Shiota, Y.3    Yamabe, T.4
  • 127
    • 0033627381 scopus 로고    scopus 로고
    • Conversion of methane to methanol on diiron and dicopper enzyme models of methane monooxygenase: A theoretical study on a concerted reaction pathway
    • YOSHIZAWA, K., SUZUKI, A., SHIOTA, Y. & YAMABE, T. (2000). Conversion of methane to methanol on diiron and dicopper enzyme models of methane monooxygenase: a theoretical study on a concerted reaction pathway. Bull chem. Soc. Jpn. 73, 815-827.
    • (2000) Bull Chem. Soc. Jpn , vol.73 , pp. 815-827
    • Yoshizawa, K.1    Suzuki, A.2    Shiota, Y.3    Yamabe, T.4
  • 128
    • 0344791553 scopus 로고
    • Approximate density functional theory as a practical tool in molecular energetics and dynamics
    • ZIEGLER, T. (1991). Approximate density functional theory as a practical tool in molecular energetics and dynamics. Chem. Rev. 91, 651-667.
    • (1991) Chem. Rev. , vol.91 , pp. 651-667
    • Ziegler, T.1
  • 129
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • ZOUNI, A., WITT, H.-T., KERN, J., FROMME, P., KRAUSS, N., SAENGER, W. & ORTH, P. (2001). Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409, 739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.-T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.