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Volumn 1043, Issue , 2014, Pages 54-63

Interaction between glyphosate and mitochondrial succinate dehydrogenase

Author keywords

DFT calculations; Glyphosate; ONIOM; Potential energy surface (PES); SCRF; Succinate dehydrogenase

Indexed keywords


EID: 84962408657     PISSN: 2210271X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.comptc.2014.05.018     Document Type: Article
Times cited : (20)

References (51)
  • 1
    • 0000630286 scopus 로고
    • The site of the inhibition of the shikimate pathway by glyphosate. II. Interference of glyphosate with chorismate formation in vivo and in vitro
    • Amrhein N., Deus B., Gehrke P., Steinrucken H.C. The site of the inhibition of the shikimate pathway by glyphosate. II. Interference of glyphosate with chorismate formation in vivo and in vitro. Plant Physiol. 1980, 66:830-834.
    • (1980) Plant Physiol. , vol.66 , pp. 830-834
    • Amrhein, N.1    Deus, B.2    Gehrke, P.3    Steinrucken, H.C.4
  • 5
    • 77958088138 scopus 로고    scopus 로고
    • Glyphosate-based herbicides produce teratogenic effects on vertebrates by impairing retinoic acid signaling
    • Paganelli A., Gnazzo V., Acosta H., Lopez S.L., Carrasco A.E. Glyphosate-based herbicides produce teratogenic effects on vertebrates by impairing retinoic acid signaling. Chem. Res. Toxicol. 2010, 23:1586-1595.
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1586-1595
    • Paganelli, A.1    Gnazzo, V.2    Acosta, H.3    Lopez, S.L.4    Carrasco, A.E.5
  • 6
    • 77956267334 scopus 로고    scopus 로고
    • Morphological damages of a glyphosate-treated human keratinocyte cell line revealed by a micro- to nanoscale microscopic investigation
    • Elie-Caille C., Heu C., Guyon C., Nicod L. Morphological damages of a glyphosate-treated human keratinocyte cell line revealed by a micro- to nanoscale microscopic investigation. Cell. Biol. Toxicol. 2010, 26:331-339.
    • (2010) Cell. Biol. Toxicol. , vol.26 , pp. 331-339
    • Elie-Caille, C.1    Heu, C.2    Guyon, C.3    Nicod, L.4
  • 7
    • 77249107555 scopus 로고    scopus 로고
    • Studies on glyphosate-induced carcinogenicity in mouse skin: a proteomic approach
    • George J., Prasad S., Mahmood Z., Shukla Y. Studies on glyphosate-induced carcinogenicity in mouse skin: a proteomic approach. J. Proteomics. 2010, 73:951-964.
    • (2010) J. Proteomics. , vol.73 , pp. 951-964
    • George, J.1    Prasad, S.2    Mahmood, Z.3    Shukla, Y.4
  • 10
    • 34247172635 scopus 로고    scopus 로고
    • Cysteine turnover in human cell lines is influenced by glyphosate
    • Hultberg M. Cysteine turnover in human cell lines is influenced by glyphosate. Environ. Toxicol. Pharmacol. 2007, 24:19-22.
    • (2007) Environ. Toxicol. Pharmacol. , vol.24 , pp. 19-22
    • Hultberg, M.1
  • 13
    • 58949088463 scopus 로고    scopus 로고
    • Genotoxicity of the herbicide formulation Roundup® (glyphosate) in broad-snouted caiman (Caiman latirostris) evidenced by the Comet assay and the Micronucleus test
    • Poletta G.L., Larriera A., Kleinsorge E., Mudry M.D. Genotoxicity of the herbicide formulation Roundup® (glyphosate) in broad-snouted caiman (Caiman latirostris) evidenced by the Comet assay and the Micronucleus test. Mutation Res. 2009, 672:95-102.
    • (2009) Mutation Res. , vol.672 , pp. 95-102
    • Poletta, G.L.1    Larriera, A.2    Kleinsorge, E.3    Mudry, M.D.4
  • 14
    • 61849171735 scopus 로고    scopus 로고
    • Glyphosate formulations induce apoptosis and necrosis in human umbilical, embryonic, and placental cells
    • Benachour N., Seralini G.-E. Glyphosate formulations induce apoptosis and necrosis in human umbilical, embryonic, and placental cells. Chem. Res. Toxicol. 2009, 22:97-105.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 97-105
    • Benachour, N.1    Seralini, G.-E.2
  • 16
    • 27644553925 scopus 로고    scopus 로고
    • Comparative effects of the roundup and glyphosate on mitochondrial oxidative phosphorylation
    • Peixoto F. Comparative effects of the roundup and glyphosate on mitochondrial oxidative phosphorylation. Chemosphere 2005, 61:1115-1122.
    • (2005) Chemosphere , vol.61 , pp. 1115-1122
    • Peixoto, F.1
  • 17
    • 0000796826 scopus 로고
    • Acid dissociation constants of arsenic acid, methylarsonic acid (MAA), Dimethylarsinic acid (Cacodylic Acid), and N-(Phosphonomethy1)glycine (Glyphosate)
    • Wauchope D.J. Acid dissociation constants of arsenic acid, methylarsonic acid (MAA), Dimethylarsinic acid (Cacodylic Acid), and N-(Phosphonomethy1)glycine (Glyphosate). Agric. Food Chem. 1978, 24:717-721.
    • (1978) Agric. Food Chem. , vol.24 , pp. 717-721
    • Wauchope, D.J.1
  • 20
    • 1542364465 scopus 로고    scopus 로고
    • The quaternary structure of the saccharomyces cerevisiae succinate dehydrogenase
    • Oyedotun K.S., Lemire B.D. The quaternary structure of the saccharomyces cerevisiae succinate dehydrogenase. J. Biol. Chem. 2004, 279:9424-9431.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9424-9431
    • Oyedotun, K.S.1    Lemire, B.D.2
  • 21
    • 0016861486 scopus 로고
    • The reaction of N-ethylmaleimide at the active site of succinate dehydrogenase
    • Kenney W.C. The reaction of N-ethylmaleimide at the active site of succinate dehydrogenase. J. Biol. Chem. 1975, 250:3089-3094.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3089-3094
    • Kenney, W.C.1
  • 22
    • 38749087624 scopus 로고    scopus 로고
    • High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates
    • Muller F.L., Liut Y., Abdul-Ghani M.A., Lustgarten M.S., Bhattacharya A., Jang Y.C., Van Remmen H. High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates. Biochem. J. 2008, 409:491-499.
    • (2008) Biochem. J. , vol.409 , pp. 491-499
    • Muller, F.L.1    Liut, Y.2    Abdul-Ghani, M.A.3    Lustgarten, M.S.4    Bhattacharya, A.5    Jang, Y.C.6    Van Remmen, H.7
  • 23
    • 79953908318 scopus 로고    scopus 로고
    • Succinate Dehydrogenase: Assembly, Regulation and Role in Human Disease
    • Hajjawi O.S. Succinate Dehydrogenase: Assembly, Regulation and Role in Human Disease. Eur. J. Sci. Res. 2011, 51:133-142.
    • (2011) Eur. J. Sci. Res. , vol.51 , pp. 133-142
    • Hajjawi, O.S.1
  • 25
    • 84962386907 scopus 로고    scopus 로고
    • ArgusLab 4.0, Planaria Software, LCC, Seattle, WA.
    • M.A. Thompson, ArgusLab 4.0, Planaria Software, LCC, Seattle, WA. http://www.arguslab.com/.
    • Thompson, M.A.1
  • 27
    • 34250681353 scopus 로고    scopus 로고
    • Detailed comparison of the protein-ligand docking efficiencies of GOLD, a commercial package and ArgusLab, a licensable freeware
    • Joy S., Nair P.S., Hariharan R., Pillai M.R. Detailed comparison of the protein-ligand docking efficiencies of GOLD, a commercial package and ArgusLab, a licensable freeware. Silico Biol. 2006, 6:601-605.
    • (2006) Silico Biol. , vol.6 , pp. 601-605
    • Joy, S.1    Nair, P.S.2    Hariharan, R.3    Pillai, M.R.4
  • 29
    • 35448937584 scopus 로고    scopus 로고
    • Optimization of parameters for semiempirical methods V: Modification of NDDO approximations and application to 70 elements
    • Stewart J.J.P. Optimization of parameters for semiempirical methods V: Modification of NDDO approximations and application to 70 elements. J. Mol. Model. 2007, 13:1173-1213.
    • (2007) J. Mol. Model. , vol.13 , pp. 1173-1213
    • Stewart, J.J.P.1
  • 30
  • 33
    • 33748263628 scopus 로고    scopus 로고
    • Quantum chemical modeling of enzyme active sites and reaction mechanisms
    • Himo F. Quantum chemical modeling of enzyme active sites and reaction mechanisms. Theor. Chem. Acc. 2006, 116:232-240.
    • (2006) Theor. Chem. Acc. , vol.116 , pp. 232-240
    • Himo, F.1
  • 34
    • 84946893847 scopus 로고
    • Electrostatic interaction of a solute with a continuum. A direct utilization of ab initio molecular potentials for the prevision of solvent effects
    • Miertus S., Scrocco E., Tomasi J. Electrostatic interaction of a solute with a continuum. A direct utilization of ab initio molecular potentials for the prevision of solvent effects. Chem. Phys. 1981, 55:117-129.
    • (1981) Chem. Phys. , vol.55 , pp. 117-129
    • Miertus, S.1    Scrocco, E.2    Tomasi, J.3
  • 35
    • 33751157732 scopus 로고
    • Ab Initio calculation of vibrational absorption and circular dichroism spectra using density functional force fields
    • Stephens P.J., Devlin F.J., Chabalowski C.F., Frisch M.J. Ab Initio calculation of vibrational absorption and circular dichroism spectra using density functional force fields. J. Phys. Chem. 1994, 98:11623-11627.
    • (1994) J. Phys. Chem. , vol.98 , pp. 11623-11627
    • Stephens, P.J.1    Devlin, F.J.2    Chabalowski, C.F.3    Frisch, M.J.4
  • 36
    • 80052604882 scopus 로고    scopus 로고
    • Theoretical study of the isomerization of maleic acid into fumaric acid
    • Ugarte R., Bustos C., Moreno-Villoslada I. Theoretical study of the isomerization of maleic acid into fumaric acid. J. Chil. Chem. Soc. 2011, 56:656-662.
    • (2011) J. Chil. Chem. Soc. , vol.56 , pp. 656-662
    • Ugarte, R.1    Bustos, C.2    Moreno-Villoslada, I.3
  • 37
    • 84890067171 scopus 로고    scopus 로고
    • Molecular recognition of aromatic rings by flavin: electrostatics and dispersion determine ring positioning above isoalloxazine
    • Koziol L., Kumar N., Wong S.E., Lightstone F.C. Molecular recognition of aromatic rings by flavin: electrostatics and dispersion determine ring positioning above isoalloxazine. J. Phys. Chem. A 2013, 117:12946-12952.
    • (2013) J. Phys. Chem. A , vol.117 , pp. 12946-12952
    • Koziol, L.1    Kumar, N.2    Wong, S.E.3    Lightstone, F.C.4
  • 38
    • 43049141516 scopus 로고    scopus 로고
    • The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: two new functionals and systematic testing of four M06-class functionals and 12 other functionals
    • Zhao Y., Truhlar D.G. The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: two new functionals and systematic testing of four M06-class functionals and 12 other functionals. Theor. Chem. Acc. 2008, 120:215-241.
    • (2008) Theor. Chem. Acc. , vol.120 , pp. 215-241
    • Zhao, Y.1    Truhlar, D.G.2
  • 39
    • 84889066017 scopus 로고    scopus 로고
    • Performance of M06, M06-2X, and M06-HF density functionals for conformationally flexible anionic clusters: M06 functionals perform better than B3LYP for a model system with dispersion and ionic hydrogen-bonding interactions
    • Walker M., Harvey A.J.A., Sen A., Dessent C.E.H. Performance of M06, M06-2X, and M06-HF density functionals for conformationally flexible anionic clusters: M06 functionals perform better than B3LYP for a model system with dispersion and ionic hydrogen-bonding interactions. J. Phys. Chem. A 2013, 117:12590-12600.
    • (2013) J. Phys. Chem. A , vol.117 , pp. 12590-12600
    • Walker, M.1    Harvey, A.J.A.2    Sen, A.3    Dessent, C.E.H.4
  • 40
    • 40149109196 scopus 로고    scopus 로고
    • Systematic optimization of long-range corrected hybrid density functionals
    • 084106:1-15
    • Chai J.-D., Head-Gordon M. Systematic optimization of long-range corrected hybrid density functionals. J. Chem. Phys. 2008, 128. 084106:1-15.
    • (2008) J. Chem. Phys. , vol.128
    • Chai, J.-D.1    Head-Gordon, M.2
  • 41
    • 55849117399 scopus 로고    scopus 로고
    • Long-range corrected hybrid density functionals with damped atom-atom dispersion corrections
    • Chai J.-D., Head-Gordon M. Long-range corrected hybrid density functionals with damped atom-atom dispersion corrections. Phys. Chem. Chem. Phys. 2008, 10:6615-6620.
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 6615-6620
    • Chai, J.-D.1    Head-Gordon, M.2
  • 42
    • 11644266970 scopus 로고
    • Electronic population analysis on LCAO-MO molecular wave functions. I
    • Mulliken R.S. Electronic population analysis on LCAO-MO molecular wave functions. I. J. Chem. Phys. 1955, 23:1833-1840.
    • (1955) J. Chem. Phys. , vol.23 , pp. 1833-1840
    • Mulliken, R.S.1
  • 43
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarity
    • Fersht A.R. Catalysis, binding and enzyme-substrate complementarity. Proc. R. Soc. Lond. B 1974, 187:397-407.
    • (1974) Proc. R. Soc. Lond. B , vol.187 , pp. 397-407
    • Fersht, A.R.1
  • 45
    • 0024086838 scopus 로고
    • A theoretical study of the dielectric constant of protein
    • Nakamura H., Sakamoto T., Wada A. A theoretical study of the dielectric constant of protein. Protein Eng. 1988, 2:177-183.
    • (1988) Protein Eng. , vol.2 , pp. 177-183
    • Nakamura, H.1    Sakamoto, T.2    Wada, A.3
  • 46
    • 0031577320 scopus 로고    scopus 로고
    • Calculation of the dielectric properties of a protein and its solvent: theory and a case study
    • Löffler G., Schreiber H., Steinhauser O. Calculation of the dielectric properties of a protein and its solvent: theory and a case study. J. Mol. Biol. 1997, 270:520-534.
    • (1997) J. Mol. Biol. , vol.270 , pp. 520-534
    • Löffler, G.1    Schreiber, H.2    Steinhauser, O.3
  • 47
    • 0032534765 scopus 로고    scopus 로고
    • Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2Å resolution crystal structure of Azotobacter vinelandii ModA
    • Lawson D.M., Williams C.E.M., Mitchenall L.A., Pau R.N. Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2Å resolution crystal structure of Azotobacter vinelandii ModA. Structure 1998, 6:1529-1539.
    • (1998) Structure , vol.6 , pp. 1529-1539
    • Lawson, D.M.1    Williams, C.E.M.2    Mitchenall, L.A.3    Pau, R.N.4
  • 48
    • 1842411345 scopus 로고    scopus 로고
    • Energetic and entropic factors determining binding affinity in protein-ligand complexes
    • Klebe G., Bohm H.-J. Energetic and entropic factors determining binding affinity in protein-ligand complexes. J. Recep. Sig. Trans. Res. 1997, 17:459-473.
    • (1997) J. Recep. Sig. Trans. Res. , vol.17 , pp. 459-473
    • Klebe, G.1    Bohm, H.-J.2
  • 49
    • 84877768087 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: role and ramifications in biomolecular ligand recognition and design
    • Chodera J.D., Mobley D.L. Entropy-enthalpy compensation: role and ramifications in biomolecular ligand recognition and design. Annu. Rev. Biophys. 2013, 42:121-142.
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 121-142
    • Chodera, J.D.1    Mobley, D.L.2
  • 50
    • 84878812901 scopus 로고    scopus 로고
    • A quantum chemical view of enthalpy-entropy compensation
    • Korth M. A quantum chemical view of enthalpy-entropy compensation. Med. Chem. Commun. 2013, 4:1025-1033.
    • (2013) Med. Chem. Commun. , vol.4 , pp. 1025-1033
    • Korth, M.1
  • 51
    • 84870179636 scopus 로고    scopus 로고
    • Comparison of some dispersion-corrected and traditional functionals with CCSD(T) and MP2 ab initio methods: Dispersion, induction, and basis set superposition error
    • 134109:1-12
    • Roy D., Marianski M., Maitra N.T., Dannenberg J.J. Comparison of some dispersion-corrected and traditional functionals with CCSD(T) and MP2 ab initio methods: Dispersion, induction, and basis set superposition error. J. Chem. Phys. 2012, 137. 134109:1-12.
    • (2012) J. Chem. Phys. , vol.137
    • Roy, D.1    Marianski, M.2    Maitra, N.T.3    Dannenberg, J.J.4


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