메뉴 건너뛰기




Volumn 5, Issue 4, 2010, Pages 377-392

Structural elucidation of cisoid and transoid cyclization pathways of a sesquiterpene synthase using 2-fluorofarnesyl diphosphates

Author keywords

[No Author keywords available]

Indexed keywords

2 EPI PREZIZAENE; 2 FLUOROFARNESYL DIPHOSPHATES; 4 EPI ALPHA ACORADIENE; 4 EPI EREMOPHILENE; 5 EPI ARISTOLOCHENE; ALPHA ACORADIENE; ALPHA CEDRENE; API ALPHA BISABOLOL; BETA CURCUMENE; BISABOLOL; FARNESOL; FARNESYL DIPHOSPHATE; GERMACRENE A; NEROLIDOL; PREMNASPIRODIENE; SESQUITERPENE; SYNTHETASE; TERPENOID DERIVATIVE; TOBACCO 5 EPI ARISTOLOCHENE SYNTHASE; UNCLASSIFIED DRUG;

EID: 77951133659     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb900295g     Document Type: Article
Times cited : (61)

References (57)
  • 1
    • 34250785114 scopus 로고    scopus 로고
    • The function of terpene natural products in the natural world
    • Gershenzon, J. and Dudareva, N. (2007) The function of terpene natural products in the natural world Nat. Chem. Biol. 3, 408-414
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 408-414
    • Gershenzon, J.1    Dudareva, N.2
  • 2
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang, P., Ko, T., and Wang, A. (2002) Structure, mechanism and function of prenyltransferases Eur. J. Biochem. 269, 3339-3354
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3339-3354
    • Liang, P.1    Ko, T.2    Wang, A.3
  • 3
    • 0000181440 scopus 로고
    • The isoprene rule and the biogenesis of terpenic compounds
    • Ruzicka, L., Eschenmoser, A., and Heusser, H. (1953) The isoprene rule and the biogenesis of terpenic compounds Experentia 9, 357-367
    • (1953) Experentia , vol.9 , pp. 357-367
    • Ruzicka, L.1    Eschenmoser, A.2    Heusser, H.3
  • 4
    • 0001312578 scopus 로고
    • Isoprenoid biosynthesis. Stereochemistry of the cyclization of allylic pyrophosphates
    • Cane, D. (1985) Isoprenoid biosynthesis. Stereochemistry of the cyclization of allylic pyrophosphates Acc. Chem. Res. 18, 220-226
    • (1985) Acc. Chem. Res. , vol.18 , pp. 220-226
    • Cane, D.1
  • 5
    • 0030796451 scopus 로고    scopus 로고
    • Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase
    • Starks, C., Back, K., Chappell, J., and Noel, J. (1997) Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase Science 277, 1815-1820
    • (1997) Science , vol.277 , pp. 1815-1820
    • Starks, C.1    Back, K.2    Chappell, J.3    Noel, J.4
  • 6
    • 0030777210 scopus 로고    scopus 로고
    • Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology
    • Lesburg, C., Zhai, G., Cane, D., and Christianson, D. (1997) Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology Science 277, 1820-1824
    • (1997) Science , vol.277 , pp. 1820-1824
    • Lesburg, C.1    Zhai, G.2    Cane, D.3    Christianson, D.4
  • 7
    • 33847049467 scopus 로고    scopus 로고
    • X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate
    • Shishova, E., Di Costanzo, L., Cane, D., and Christianson, D. (2007) X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate Biochemistry 46, 1941-1951
    • (2007) Biochemistry , vol.46 , pp. 1941-1951
    • Shishova, E.1    Di Costanzo, L.2    Cane, D.3    Christianson, D.4
  • 8
    • 51049091699 scopus 로고    scopus 로고
    • Protonation of a neutral (S)-?-bisabolene intermediate is involved in (S)-?-macrocarpene formation by the maize sesquiterpene synthases TPS6 and TPS11
    • K'llner, T., Schnee, C., Li, S., Svatos, A., Schneider, B., Gershenzon, J., and Degenhardt, J. (2008) Protonation of a neutral (S)-?-bisabolene intermediate is involved in (S)-?-macrocarpene formation by the maize sesquiterpene synthases TPS6 and TPS11 J. Biol. Chem. 283, 20779-20788
    • (2008) J. Biol. Chem. , vol.283 , pp. 20779-20788
    • K'llner, T.1    Schnee, C.2    Li, S.3    Svatos, A.4    Schneider, B.5    Gershenzon, J.6    Degenhardt, J.7
  • 9
    • 33646148490 scopus 로고    scopus 로고
    • Amorpha-4,11-diene synthase: Mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate
    • Picaud, S., Mercke, P., He, X., Sterner, O., Brodelius, M., Cane, D., and Brodelius, P. (2006) Amorpha-4,11-diene synthase: mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate Arch. Biochem. Biophys. 448, 150-155
    • (2006) Arch. Biochem. Biophys. , vol.448 , pp. 150-155
    • Picaud, S.1    Mercke, P.2    He, X.3    Sterner, O.4    Brodelius, M.5    Cane, D.6    Brodelius, P.7
  • 10
    • 0001392969 scopus 로고
    • Trichodiene biosynthesis and the role of nerolidyl pyrophosphate in the enzymatic cyclization of farnesyl pyrophosphate
    • Cane, D. and Ha, H. (1988) Trichodiene biosynthesis and the role of nerolidyl pyrophosphate in the enzymatic cyclization of farnesyl pyrophosphate J. Am. Chem. Soc. 110, 6865-6870
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 6865-6870
    • Cane, D.1    Ha, H.2
  • 11
    • 0033568097 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of epi-cedrol synthase, a sesquiterpene cyclase from Artemisia annua L
    • Mercke, P., Crock, J., Croteau, R., and Brodelius, P. (1999) Cloning, expression, and characterization of epi-cedrol synthase, a sesquiterpene cyclase from Artemisia annua L Arch. Biochem. Biophys. 369, 213-222
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 213-222
    • Mercke, P.1    Crock, J.2    Croteau, R.3    Brodelius, P.4
  • 12
    • 69949157277 scopus 로고    scopus 로고
    • Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor. Mechanism and stereochemistry of the enzymatic formation of epi-isozizaene
    • Lin, X. and Cane, D. (2009) Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor. Mechanism and stereochemistry of the enzymatic formation of epi-isozizaene J. Am. Chem. Soc. 131, 6332-6333
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6332-6333
    • Lin, X.1    Cane, D.2
  • 13
    • 0001836628 scopus 로고    scopus 로고
    • Cyclization enzymes in the biosynthesis of monoterpenes, sesquiterpenes, and diterpenes
    • Davis, E. M. and Croteau, R. (2000) Cyclization enzymes in the biosynthesis of monoterpenes, sesquiterpenes, and diterpenes Top. Curr. Chem. 209, 53-95
    • (2000) Top. Curr. Chem. , vol.209 , pp. 53-95
    • Davis, E.M.1    Croteau, R.2
  • 14
    • 0003379315 scopus 로고
    • Post-infectional inhibitors from plants. 4. Structure of capsidiol - Antifungal sesquiterpene from sweet peppers
    • Gordon, M., Stoessl, A., and Stothers, J. (1973) Post-infectional inhibitors from plants. 4. Structure of capsidiol-antifungal sesquiterpene from sweet peppers Can. J. Chem. 51, 748-752
    • (1973) Can. J. Chem. , vol.51 , pp. 748-752
    • Gordon, M.1    Stoessl, A.2    Stothers, J.3
  • 15
    • 33646145081 scopus 로고    scopus 로고
    • Biosynthetic potential of sesquiterpene synthases: Alternative products of tobacco 5-epi-aristolochene synthase
    • O'Maille, P. E., Chappell, J., and Noel, J. (2006) Biosynthetic potential of sesquiterpene synthases: alternative products of tobacco 5-epi-aristolochene synthase Arch. Biochem. Biophys. 448, 73-82
    • (2006) Arch. Biochem. Biophys. , vol.448 , pp. 73-82
    • O'maille, P.E.1    Chappell, J.2    Noel, J.3
  • 16
    • 0006796521 scopus 로고    scopus 로고
    • 2 nd ed., American Chemical Society and Oxford University Press, Oxford
    • Fox, R. B. and Powell, W. H. (2001) Nomenclature of Organic Compounds, 2 nd ed., pp 306 ? 308, American Chemical Society and Oxford University Press, Oxford.
    • (2001) Nomenclature of Organic Compounds , pp. 306-308
    • Fox, R.B.1    Powell, W.H.2
  • 18
    • 77951111516 scopus 로고    scopus 로고
    • Bisabolyl-derived sesquiterpenes from tobacco 5-epi-aristolochene synthase-catalyzed cyclization of (2 Z, 6 E)-farnesyl diphosphate
    • accepted for publication.
    • Faraldos, J. A., O'Maille, P. E., Dellas, N., Noel, J., and Coates, R. M. (2009) Bisabolyl-derived sesquiterpenes from tobacco 5-epi-aristolochene synthase-catalyzed cyclization of (2 Z, 6 E)-farnesyl diphosphate. J. Am. Chem. Soc., accepted for publication.
    • (2009) J. Am. Chem. Soc.
    • Faraldos, J.A.1    O'maille, P.E.2    Dellas, N.3    Noel, J.4    Coates, R.M.5
  • 20
    • 8844224770 scopus 로고    scopus 로고
    • A single-vial analytical and quantitative gas chromatography-mass spectrometry assay for terpene synthases
    • O'Maille, P. E., Chappell, J., and Noel, J. (2004) A single-vial analytical and quantitative gas chromatography-mass spectrometry assay for terpene synthases Anal. Biochem. 335, 210-217
    • (2004) Anal. Biochem. , vol.335 , pp. 210-217
    • O'maille, P.E.1    Chappell, J.2    Noel, J.3
  • 21
    • 35349024916 scopus 로고    scopus 로고
    • Aristolochene synthase-catalyzed cyclization of 2-fluorofarnesyl- diphosphate to 2-fluorogermacrene A
    • Miller, D., Yu, F., and Allemann, R. (2007) Aristolochene synthase-catalyzed cyclization of 2-fluorofarnesyl-diphosphate to 2-fluorogermacrene A ChemBiochem 8, 1819-1825
    • (2007) ChemBiochem , vol.8 , pp. 1819-1825
    • Miller, D.1    Yu, F.2    Allemann, R.3
  • 24
    • 47249119324 scopus 로고    scopus 로고
    • X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal binding sequence for catalysis
    • Shishova, E., Yu, F., Miller, D. J., Faraldos, J., Zhao, Y., Coates, R., Allemann, R., Cane, D., and Christianson, D. (2008) X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal binding sequence for catalysis J. Biol. Chem. 283, 15431-15439
    • (2008) J. Biol. Chem. , vol.283 , pp. 15431-15439
    • Shishova, E.1    Yu, F.2    Miller, D.J.3    Faraldos, J.4    Zhao, Y.5    Coates, R.6    Allemann, R.7    Cane, D.8    Christianson, D.9
  • 25
    • 0037019526 scopus 로고    scopus 로고
    • Concomitant C-ring expansion and D-ring formation in lanosterol biosynthesis from squalene without violation of Markovnikov's rule
    • Hess, B. (2002) Concomitant C-ring expansion and D-ring formation in lanosterol biosynthesis from squalene without violation of Markovnikov's rule J. Am. Chem. Soc. 124, 10286-10287
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10286-10287
    • Hess, B.1
  • 26
    • 67650546952 scopus 로고    scopus 로고
    • Consequences of conformational preorganization in sesquiterpene biosynthesis: Theoretical studies on the formation of the bisabolene, curcumene, acoradiene, zizaene, cedrene, duprezianene, and sesquithuriferol sesquiterpenes
    • Hong, Y. and Tantillo, D. (2009) Consequences of conformational preorganization in sesquiterpene biosynthesis: theoretical studies on the formation of the bisabolene, curcumene, acoradiene, zizaene, cedrene, duprezianene, and sesquithuriferol sesquiterpenes J. Am. Chem. Soc. 131, 7999-8015
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7999-8015
    • Hong, Y.1    Tantillo, D.2
  • 27
    • 34250780393 scopus 로고    scopus 로고
    • Conformational analysis of (+)-germacrene A by variable-temperature NMR and NOE spectroscopy
    • Faraldos, J. A., Wu, S., Chappell, J., and Coates, R. M. (2007) Conformational analysis of (+)-germacrene A by variable-temperature NMR and NOE spectroscopy Tetrahedron 63, 7733-7742
    • (2007) Tetrahedron , vol.63 , pp. 7733-7742
    • Faraldos, J.A.1    Wu, S.2    Chappell, J.3    Coates, R.M.4
  • 28
    • 0021879909 scopus 로고
    • Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate
    • Croteau, R., Felton, N., and Wheeler, C. (1985) Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (?)-bornyl pyrophosphate J. Biol. Chem. 260, 5956-5962 (Pubitemid 15072495)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.10 , pp. 5956-5962
    • Croteau, R.1    Felton, N.M.2    Wheeler, C.J.3
  • 29
    • 35348952662 scopus 로고    scopus 로고
    • Interception of the enzymatic conversion of farnesyl diphosphate to 5-epi-aristolochene by using a fluoro substrate analogue: 1-fluorogermacrene A from (2 E,6 Z)-6-fluorofarnesyl diphosphate
    • Faraldos, J. A., Zhao, Y., O'Maille, P. E., Noel, J., and Coates, R. M. (2007) Interception of the enzymatic conversion of farnesyl diphosphate to 5-epi-aristolochene by using a fluoro substrate analogue: 1-fluorogermacrene A from (2 E,6 Z)-6-fluorofarnesyl diphosphate ChemBioChem 8, 1826-1833
    • (2007) ChemBioChem , vol.8 , pp. 1826-1833
    • Faraldos, J.A.1    Zhao, Y.2    O'maille, P.E.3    Noel, J.4    Coates, R.M.5
  • 30
    • 19744366357 scopus 로고    scopus 로고
    • Taxadiene synthase-catalyzed cyclization of 6-fluorogeranylgeranyl diphosphate to 7-fluoroverticillenes
    • Jin, Y. H., Williams, D., Croteau, R., and Coates, R. M. (2005) Taxadiene synthase-catalyzed cyclization of 6-fluorogeranylgeranyl diphosphate to 7-fluoroverticillenes J. Am. Chem. Soc. 127, 7834-7842
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7834-7842
    • Jin, Y.H.1    Williams, D.2    Croteau, R.3    Coates, R.M.4
  • 32
    • 25444446571 scopus 로고    scopus 로고
    • Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase
    • Vedula, L., Cane, D., and Christianson, D. (2005) Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase Biochemistry 44, 12719-12727
    • (2005) Biochemistry , vol.44 , pp. 12719-12727
    • Vedula, L.1    Cane, D.2    Christianson, D.3
  • 33
    • 0034725457 scopus 로고    scopus 로고
    • Identification of a short (C15) chain Z -isoprenyl diphosphate synthase and a homologous long (C50) chain isoprenyl diphosphate synthase in Mycobacterium tuberculosis
    • Schulbach, M., Brennan, P., and Crick, D. (2000) Identification of a short (C15) chain Z -isoprenyl diphosphate synthase and a homologous long (C50) chain isoprenyl diphosphate synthase in Mycobacterium tuberculosis J. Biol. Chem. 275, 22876-22881
    • (2000) J. Biol. Chem. , vol.275 , pp. 22876-22881
    • Schulbach, M.1    Brennan, P.2    Crick, D.3
  • 34
    • 0035853684 scopus 로고    scopus 로고
    • Purification, enzymatic characterization, and inhibition of the Z -farnesyl diphosphate synthase from Mycobacterium tuberculosis
    • Schulbach, M., Mahapatra, S., Macchia, M., Barontini, S., Papi, C., Minutolo, F., Bertini, S., Brennan, P., and Crick, D. (2001) Purification, enzymatic characterization, and inhibition of the Z -farnesyl diphosphate synthase from Mycobacterium tuberculosis J. Biol. Chem. 276, 11624-11630
    • (2001) J. Biol. Chem. , vol.276 , pp. 11624-11630
    • Schulbach, M.1    Mahapatra, S.2    MacChia, M.3    Barontini, S.4    Papi, C.5    Minutolo, F.6    Bertini, S.7    Brennan, P.8    Crick, D.9
  • 35
    • 33845400832 scopus 로고    scopus 로고
    • Farnesyl diphosphate synthase: The art of compromise between substrate selectivity and stereoselectivity
    • Thulasiram, H. and Poulter, C. D. (2006) Farnesyl diphosphate synthase: the art of compromise between substrate selectivity and stereoselectivity J. Am. Chem. Soc. 128, 15819-15823
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15819-15823
    • Thulasiram, H.1    Poulter, C.D.2
  • 36
    • 0000481337 scopus 로고
    • Trisammonium geranyl diphosphate
    • Collect. Wiley, New York
    • Woodside, A., Huang, Z., and Poulter, C. D. (1993) Trisammonium geranyl diphosphate, in Organic Synthesis, Collect. Vol. 8, pp 616 ? 620, Wiley, New York.
    • (1993) Organic Synthesis , vol.8 , pp. 616-620
    • Woodside, A.1    Huang, Z.2    Poulter, C.D.3
  • 37
    • 0027879008 scopus 로고
    • Automated processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automated processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26, 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • - (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowton, K. (2004) Coot: model-building tools for molecular graphics Acta Crystallogr. D 60, 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowton, K.2
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G., Vagin, A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D 53, 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.2    Dodson, E.J.3
  • 43
    • 0032212015 scopus 로고    scopus 로고
    • Incorporation of prior phase information strengthens maximum-likelihood structure refinement
    • Pannu, N., Murshudov, G., Dodson, E., and Read, R. (1998) Incorporation of prior phase information strengthens maximum-likelihood structure refinement Acta Crystallogr. D 54, 1285-1294
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1285-1294
    • Pannu, N.1    Murshudov, G.2    Dodson, E.3    Read, R.4
  • 44
    • 13844301139 scopus 로고    scopus 로고
    • Direct incorporation of experimental phase information in model refinement
    • Skubak, P., Murshudov, G., and Pannu, N. (2004) Direct incorporation of experimental phase information in model refinement Acta Crystallogr. D 60, 2196-2201
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2196-2201
    • Skubak, P.1    Murshudov, G.2    Pannu, N.3
  • 45
    • 0347693074 scopus 로고    scopus 로고
    • Fisher's information in maximum-likelihood macromolecular crystallographic refinement
    • Steiner, R., Lebedev, A., and Murshudov, G. (2003) Fisher's information in maximum-likelihood macromolecular crystallographic refinement Acta Crystallogr. D 59, 2114-2124
    • (2003) Acta Crystallogr. D , vol.59 , pp. 2114-2124
    • Steiner, R.1    Lebedev, A.2    Murshudov, G.3
  • 47
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M., Isupov, M., and Murshudov, G. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D 57, 122-133
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-133
    • Winn, M.1    Isupov, M.2    Murshudov, G.3
  • 48
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn, M., Murshudov, G., and Papiz, M. (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions Acta Crystallogr. D 374, 300-321
    • (2003) Acta Crystallogr. D , vol.374 , pp. 300-321
    • Winn, M.1    Murshudov, G.2    Papiz, M.3
  • 49
    • 77951099962 scopus 로고    scopus 로고
    • Gaussian, Inc., Pittsburgh, PA
    • Frisch, M. et al. (1998) Gaussian, Inc., Pittsburgh, PA.
    • (1998)
    • Frisch, M.1
  • 50
    • 0000189651 scopus 로고
    • Density-functional thermochemistry 3. the role of exact exchange
    • Becke, A. (1993) Density-functional thermochemistry 3. The role of exact exchange J. Chem. Phys. 98, 5648-5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.1
  • 51
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee, C., Yang, W., and Parr, R. (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density Phys. Rev. B 37, 785
    • (1988) Phys. Rev. B , vol.37 , pp. 785
    • Lee, C.1    Yang, W.2    Parr, R.3
  • 52
    • 33748545144 scopus 로고
    • The influence of polarization functions on molecular orbital hydrogenation energies
    • Hariharan, P. and Pople, J. (1973) The influence of polarization functions on molecular orbital hydrogenation energies Theor. Chim. Acta 28, 213
    • (1973) Theor. Chim. Acta , vol.28 , pp. 213
    • Hariharan, P.1    Pople, J.2
  • 53
    • 36549095692 scopus 로고
    • An improved algorithm for reaction path following
    • Gonzalez, C. and Schlegel, H. (1989) An improved algorithm for reaction path following J. Chem. Phys. 90, 2154
    • (1989) J. Chem. Phys. , vol.90 , pp. 2154
    • Gonzalez, C.1    Schlegel, H.2
  • 54
    • 33750614386 scopus 로고
    • Reaction path following in mass-weighted internal coordinates
    • Gonzalez, C. and Schlegel, H. (1990) Reaction path following in mass-weighted internal coordinates J. Phys. Chem. 94, 5523
    • (1990) J. Phys. Chem. , vol.94 , pp. 5523
    • Gonzalez, C.1    Schlegel, H.2
  • 55
    • 33645216534 scopus 로고    scopus 로고
    • Mechanistic insights into triterpene synthesis from quantum mechanical calculations. Detection of systematic errors in B3LYP cyclization energies
    • Matsuda, S. and Wilson, W. (2006) Mechanistic insights into triterpene synthesis from quantum mechanical calculations. Detection of systematic errors in B3LYP cyclization energies Org. Biomol. Chem. 4, 530
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 530
    • Matsuda, S.1    Wilson, W.2
  • 56
    • 11244326290 scopus 로고    scopus 로고
    • Exchange functionals with improved long-range behavior and adiabatic connection methods without adjustable parameters: The m PW and m PW1PW models
    • Adamo, C. and Barone, V. (1998) Exchange functionals with improved long-range behavior and adiabatic connection methods without adjustable parameters: The m PW and m PW1PW models J. Chem. Phys. 108, 664
    • (1998) J. Chem. Phys. , vol.108 , pp. 664
    • Adamo, C.1    Barone, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.