메뉴 건너뛰기




Volumn 287, Issue 23, 2012, Pages 19429-19439

Role of conserved glycine in zinc-dependent medium chain dehydrogenase/reductase superfamily

Author keywords

[No Author keywords available]

Indexed keywords

BINDING GEOMETRIES; BOND ANGLE; COMPUTATIONAL ANALYSIS; DENSITY FUNCTIONALS; GLYCINE RESIDUES; ISOTHERMAL TITRATION CALORIMETRY; LARGE GROUPS; METAL BINDING AFFINITY; METAL-LIGAND BONDS; SCREENING STRATEGY; SITE DIRECTED MUTAGENESIS; SPECTROSCOPIC PROPERTY; WILD TYPES; ZINC BINDING; ZINC IONS;

EID: 84861722007     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.335752     Document Type: Article
Times cited : (31)

References (74)
  • 1
    • 58149109089 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families. The MDR superfamily
    • Persson, B., Hedlund, J., and Jörnvall, H. (2008) Medium- and short-chain dehydrogenase/reductase gene and protein families. The MDR superfamily. Cell. Mol. Life Sci. 65, 3879-3894
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3879-3894
    • Persson, B.1    Hedlund, J.2    Jörnvall, H.3
  • 2
    • 29244479504 scopus 로고    scopus 로고
    • Merging protein, gene and genomic data: The evolution of the MDR-ADH family
    • DOI 10.1038/sj.hdy.6800723, PII 6800723
    • Gonzàlez-Duarte, R., and Albalat, R. (2005) Merging protein, gene, and genomic data. The evolution of the MDR-ADH family. Heredity 95, 184-197 (Pubitemid 43102279)
    • (2005) Heredity , vol.95 , Issue.3 , pp. 184-197
    • Gonzalez-Duarte, R.1    Albalat, R.2
  • 3
    • 0019880506 scopus 로고
    • Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution
    • Eklund, H., Samma, J. P., Wallén, L., Brändén, C. I., Akeson, A., and Jones, T. A. (1981) Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution. J. Mol. Biol. 146, 561-587
    • (1981) J. Mol. Biol. , vol.146 , pp. 561-587
    • Eklund, H.1    Samma, J.P.2    Wallén, L.3    Brändén, C.I.4    Akeson, A.5    Jones, T.A.6
  • 4
    • 58149136238 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/ reductase gene and protein families. The role of zinc for alcohol dehydrogenase structure and function
    • Auld, D. S., and Bergman, T. (2008) Medium- and short-chain dehydrogenase/ reductase gene and protein families. The role of zinc for alcohol dehydrogenase structure and function. Cell. Mol. Life Sci. 65, 3961-3970
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3961-3970
    • Auld, D.S.1    Bergman, T.2
  • 5
    • 0018786675 scopus 로고
    • Structural differences between apoand holoenzyme of horse liver alcohol dehydrogenase
    • Eklund, H., and Brändén, C. I. (1979) Structural differences between apoand holoenzyme of horse liver alcohol dehydrogenase. J. Biol. Chem. 254, 3458-3461
    • (1979) J. Biol. Chem. , vol.254 , pp. 3458-3461
    • Eklund, H.1    Brändén, C.I.2
  • 6
    • 70350680995 scopus 로고    scopus 로고
    • Coordination dynamics of zinc in proteins
    • Maret, W., and Li, Y. (2009) Coordination dynamics of zinc in proteins. Chem. Rev. 109, 4682-4707
    • (2009) Chem. Rev. , vol.109 , pp. 4682-4707
    • Maret, W.1    Li, Y.2
  • 7
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb, W. N., and Sträter, N. (1996) Recent advances in zinc enzymology. Chem. Rev. 96, 2375-2434
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2434
    • Lipscomb, W.N.1    Sträter, N.2
  • 8
    • 0242500908 scopus 로고    scopus 로고
    • First-second shell interactions in metal binding sites in proteins: A PDB survey and DFT/CDM calculations
    • DOI 10.1021/ja0209722
    • Dudev, T., Lin, Y. L., Dudev, M., and Lim, C. (2003) First-second shell interactions in metal binding sites in proteins. A PDB survey and DFT/CDM calculations. J. Am. Chem. Soc. 125, 3168-3180 (Pubitemid 36512542)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.10 , pp. 3168-3180
    • Dudev, T.1    Lin, Y.-L.2    Dudev, M.3    Lim, C.4
  • 9
    • 0034669246 scopus 로고    scopus 로고
    • Tetrahedral versus octahedral zinc complexes with ligands of biological interest.ADFT/CDMstudy
    • Dudev, T., and Lim, C. (2000) Tetrahedral versus octahedral zinc complexes with ligands of biological interest.ADFT/CDMstudy. J. Am. Chem. Soc. 122, 11146-11153
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11146-11153
    • Dudev, T.1    Lim, C.2
  • 10
    • 0033603838 scopus 로고    scopus 로고
    • Competitive binding in magnesium coordination chemistry. Water versus ligands of biological interest
    • Dudev, T., Cowan, J. A., and Lim, C. (1999) Competitive binding in magnesium coordination chemistry. Water versus ligands of biological interest. J. Am. Chem. Soc. 121, 7665-7673
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7665-7673
    • Dudev, T.1    Cowan, J.A.2    Lim, C.3
  • 11
    • 0032708644 scopus 로고    scopus 로고
    • Carboxylate binding modes in zinc proteins. A theoretical study
    • Ryde, U. (1999) Carboxylate binding modes in zinc proteins. A theoretical study. Biophys. J. 77, 2777-2787
    • (1999) Biophys. J. , vol.77 , pp. 2777-2787
    • Ryde, U.1
  • 12
    • 0035857417 scopus 로고    scopus 로고
    • Reactivity of zinc finger cores: Analysis of protein packing and electrostatic screening
    • DOI 10.1021/ja0011616
    • Maynard, A. T., and Covell, D. G. (2001) Reactivity of zinc finger cores. Analysis of protein packing and electrostatic screening. J. Am. Chem. Soc. 123, 1047-1058 (Pubitemid 32148172)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.6 , pp. 1047-1058
    • Maynard, A.T.1    Covell, D.G.2
  • 13
    • 0037067059 scopus 로고    scopus 로고
    • Factors governing the protonation state of cysteines in proteins: An ab initio/CDM study
    • DOI 10.1021/ja012620l
    • Dudev, T., and Lim, C. (2002) Factors governing the protonation state of cysteines in proteins. An ab initio/CDM study. J. Am. Chem. Soc. 124, 6759-6766 (Pubitemid 34602669)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.23 , pp. 6759-6766
    • Dudev, T.1    Lim, C.2
  • 14
    • 0028873117 scopus 로고
    • Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
    • Kiefer, L. L., Paterno, S. A., and Fierke, C. A. (1995) Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency. J. Am. Chem. Soc. 117, 6831-6837
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 15
    • 0028796822 scopus 로고
    • X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
    • Lesburg, C. A., and Christianson, D. W. (1995) X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site. J. Am. Chem. Soc. 117, 6838-6844
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6838-6844
    • Lesburg, C.A.1    Christianson, D.W.2
  • 16
    • 0030881845 scopus 로고    scopus 로고
    • Kinetic and spectroscopic analyses of mutants of a conserved histidine in the metallophosphatases calcineurin and λ protein phosphatase
    • DOI 10.1074/jbc.272.34.21296
    • Mertz, P., Yu, L., Sikkink, R., and Rusnak, F. (1997) Kinetic and spectroscopic analyses of mutants of a conserved histidine in the metallophosphatases calcineurin and λ-protein phosphatase. J. Biol. Chem. 272, 21296-21302 (Pubitemid 27373996)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.34 , pp. 21296-21302
    • Mertz, P.1    Yu, L.2    Sikkink, R.3    Rusnak, F.4
  • 17
    • 0032479421 scopus 로고    scopus 로고
    • Mutations at nonliganding residues Tyr-85 and Glu-83 in the N-lobe of human serum transferrin: Functional second shell effects
    • DOI 10.1074/jbc.273.27.17018
    • He, Q. Y., Mason, A. B., Woodworth, R. C., Tam, B. M., MacGillivray, R. T., Grady, J. K., and Chasteen, N. D. (1998) Mutations at nonliganding residues Tyr-85 and Glu-83 in the N-lobe of human serum transferrin. Functional second shell effects. J. Biol. Chem. 273, 17018-17024 (Pubitemid 28311735)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.27 , pp. 17018-17024
    • He, Q.-Y.1    Mason, A.B.2    Woodworth, R.C.3    Tam, B.M.4    MacGillivray, R.T.A.5    Grady, J.K.6    Chasteen, N.D.7
  • 18
    • 0030053257 scopus 로고    scopus 로고
    • An isoleucine to leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese
    • DOI 10.1021/bi9523926
    • Vipond, I. B., Moon, B. J., and Halford, S. E. (1996) An isoleucine to leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese. Biochemistry 35, 1712-1721 (Pubitemid 26062619)
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 1712-1721
    • Vipond, I.B.1    Moon, B.-J.2    Halford, S.E.3
  • 19
    • 0033200372 scopus 로고    scopus 로고
    • Secondary ligands enhance affinity at a designed metal-binding site
    • DOI 10.1016/S1074-5521(99)80116-1
    • Marino, S. F., and Regan, L. (1999) Secondary ligands enhance affinity at a designed metal-binding site. Chem. Biol. 6, 649-655 (Pubitemid 29427380)
    • (1999) Chemistry and Biology , vol.6 , Issue.9 , pp. 649-655
    • Marino, S.F.1    Regan, L.2
  • 20
    • 0035471138 scopus 로고    scopus 로고
    • Engineering novel metalloproteins: Design of metal-binding sites into native protein scaffolds
    • DOI 10.1021/cr0000574
    • Lu, Y., Berry, S. M., and Pfister, T. D. (2001) Engineering novel metalloproteins. Design of metal-binding sites into native protein scaffolds. Chem. Rev. 101, 3047-3080 (Pubitemid 35401385)
    • (2001) Chemical Reviews , vol.101 , Issue.10 , pp. 3047-3080
    • Lu, Y.1    Berry, S.M.2    Pfister, T.D.3
  • 21
    • 29844437516 scopus 로고    scopus 로고
    • Site-selective metal binding by designed α-helical peptides
    • DOI 10.1021/ja055433m
    • Matzapetakis, M., and Pecoraro, V. L. (2005) Site-selective metal binding by designed α-helical peptides. J. Am. Chem. Soc. 127, 18229-18233 (Pubitemid 43038485)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.51 , pp. 18229-18233
    • Matzapetakis, M.1    Pecoraro, V.L.2
  • 23
    • 77951978627 scopus 로고    scopus 로고
    • Molecular modeling studies of L-arabinitol 4-dehydrogenase of Hypocrea jecorina. Its binding interactions with substrate and cofactor
    • Tiwari, M., and Lee, J. K. (2010) Molecular modeling studies of L-arabinitol 4-dehydrogenase of Hypocrea jecorina. Its binding interactions with substrate and cofactor. J. Mol. Graph. Model. 28, 707-713
    • (2010) J. Mol. Graph. Model. , vol.28 , pp. 707-713
    • Tiwari, M.1    Lee, J.K.2
  • 24
    • 36348946321 scopus 로고    scopus 로고
    • Cloning, characterization, and mutational analysis of a highly active and stable L-arabinitol 4-dehydrogenase from Neurospora crassa
    • DOI 10.1007/s00253-007-1225-0
    • Sullivan, R., and Zhao, H. (2007) Cloning, characterization, and mutational analysis of a highly active and stable L-arabinitol 4-dehydrogenase from Neurospora crassa. Appl. Microbiol. Biotechnol. 77, 845-852 (Pubitemid 350159872)
    • (2007) Applied Microbiology and Biotechnology , vol.77 , Issue.4 , pp. 845-852
    • Sullivan, R.1    Zhao, H.2
  • 25
    • 77956172696 scopus 로고    scopus 로고
    • Structure and engineering of L-arabinitol 4-dehydrogenase from Neurospora crassa
    • Bae, B., Sullivan, R. P., Zhao, H., and Nair, S. K. (2010) Structure and engineering of L-arabinitol 4-dehydrogenase from Neurospora crassa. J. Mol. Biol. 402, 230-240
    • (2010) J. Mol. Biol. , vol.402 , pp. 230-240
    • Bae, B.1    Sullivan, R.P.2    Zhao, H.3    Nair, S.K.4
  • 26
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao, S. T., and Rossmann, M. G. (1973) Comparison of super-secondary structures in proteins. J. Mol. Biol. 76, 241-256
    • (1973) J. Mol. Biol. , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 27
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins
    • Harding, M. M. (1999) The geometry of metal-ligand interactions relevant to proteins. Acta Crystallogr. D Biol. Crystallogr. 55, 1432-1443
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1432-1443
    • Harding, M.M.1
  • 28
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • DOI 10.1006/jmbi.1994.1334
    • McDonald, I. K., and Thornton, J. M. (1994) Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793 (Pubitemid 24168633)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.5 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 29
    • 84861741421 scopus 로고    scopus 로고
    • Inverse tuning of metal binding affinity and protein stability by altering charged coordination residues in designed calcium binding proteins
    • Maniccia, A. W., Yang, W., Johnson, J. A., Li, S., Tjong, H., Zhou, H. X., Shaket, L. A., and Yang, J. J. (2009) Inverse tuning of metal binding affinity and protein stability by altering charged coordination residues in designed calcium binding proteins. PMC Biophys. 2, 11
    • (2009) PMC Biophys. , vol.2 , pp. 11
    • Maniccia, A.W.1    Yang, W.2    Johnson, J.A.3    Li, S.4    Tjong, H.5    Zhou, H.X.6    Shaket, L.A.7    Yang, J.J.8
  • 30
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 31
    • 77249140467 scopus 로고    scopus 로고
    • Accelrys Inc. San Diego, CA
    • Accelrys Materials Studio (2006) Accelrys Inc. San Diego, CA
    • (2006) Accelrys Materials Studio
  • 32
    • 34447260582 scopus 로고
    • An all-electron numerical method for solving the local density functional for polyatomic molecules
    • Delley, B. (1990) An all-electron numerical method for solving the local density functional for polyatomic molecules. J. Chem. Phys. 92, 508-517
    • (1990) J. Chem. Phys. , vol.92 , pp. 508-517
    • Delley, B.1
  • 33
    • 76049122968 scopus 로고    scopus 로고
    • Quantum chemical modeling of methanol oxidation mechanisms by methanol dehydrogenase enzyme. Effect of substitution of calcium by barium in the active site
    • Idupulapati, N. B., and Mainardi, D. S. (2010) Quantum chemical modeling of methanol oxidation mechanisms by methanol dehydrogenase enzyme. Effect of substitution of calcium by barium in the active site. J. Phys. Chem. A 114, 1887-1896
    • (2010) J. Phys. Chem. A , vol.114 , pp. 1887-1896
    • Idupulapati, N.B.1    Mainardi, D.S.2
  • 34
    • 33645898818 scopus 로고
    • Accurate and simple analytic representation of the electron-gas correlation energy
    • Perdew, J. P., and Wang, Y. (1992) Accurate and simple analytic representation of the electron-gas correlation energy. Phys. Rev. B Condens. Matter 45, 13244-13249
    • (1992) Phys. Rev. B Condens. Matter , vol.45 , pp. 13244-13249
    • Perdew, J.P.1    Wang, Y.2
  • 35
    • 78449238512 scopus 로고    scopus 로고
    • Density functional theory study of lithium and fluoride doped boron nitride sheet
    • Anota, E. C., Villanueva, M. S., and Cocoletzi, H. H. (2010) Density functional theory study of lithium and fluoride doped boron nitride sheet. physica. status solidi (c) 7, 2559-2561
    • (2010) Physica. Status Solidi (C) , vol.7 , pp. 2559-2561
    • Anota, E.C.1    Villanueva, M.S.2    Cocoletzi, H.H.3
  • 36
    • 61449172290 scopus 로고    scopus 로고
    • Computational methods for calculation of ligand binding affinity
    • de Azevedo, W. F., Jr., and Dias, R. (2008) Computational methods for calculation of ligand binding affinity. Curr. Drug Targets 9, 1031-1039
    • (2008) Curr. Drug Targets , vol.9 , pp. 1031-1039
    • De Azevedo Jr., W.F.1    Dias, R.2
  • 37
    • 0029994972 scopus 로고    scopus 로고
    • Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei. Enzyme purification, characterization, and N-terminal sequence
    • Bonete, M. J., Pire, C., LLorca, F. I., and Camacho, M. L. (1996) Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei. Enzyme purification, characterization, and N-terminal sequence. FEBS Lett. 383, 227-229
    • (1996) FEBS Lett. , vol.383 , pp. 227-229
    • Bonete, M.J.1    Pire, C.2    LLorca, F.I.3    Camacho, M.L.4
  • 38
    • 0035948221 scopus 로고    scopus 로고
    • Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/reductase family
    • DOI 10.1016/S0378-1097(01)00216-6, PII S0378109701002166
    • Pire, C., Esclapez, J., Ferrer, J., and Bonete, M. J. (2001) Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/ reductase family. FEMS Microbiol. Lett. 200, 221-227 (Pubitemid 32566366)
    • (2001) FEMS Microbiology Letters , vol.200 , Issue.2 , pp. 221-227
    • Pire, C.1    Esclapez, J.2    Ferrer, J.3    Bonete, M.-J.4
  • 39
    • 77953082532 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable xylitol dehydrogenase from Rhizobium etli CFN42
    • Tiwari, M. K., Moon, H. J., Jeya, M., and Lee, J. K. (2010) Cloning and characterization of a thermostable xylitol dehydrogenase from Rhizobium etli CFN42. Appl. Microbiol. Biotechnol. 87, 571-581
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 571-581
    • Tiwari, M.K.1    Moon, H.J.2    Jeya, M.3    Lee, J.K.4
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0014670773 scopus 로고
    • Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases
    • Hoagstrom, C. W., Iweibo, I., and Weiner, H. (1969) Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases. J. Biol. Chem. 244, 5967-5971
    • (1969) J. Biol. Chem. , vol.244 , pp. 5967-5971
    • Hoagstrom, C.W.1    Iweibo, I.2    Weiner, H.3
  • 42
    • 0023856594 scopus 로고
    • Purification and characterization of human liver sorbitol dehydrogenase
    • Maret, W., and Auld, D. S. (1988) Purification and characterization of human liver sorbitol dehydrogenase. Biochemistry 27, 1622-1628 (Pubitemid 18077455)
    • (1988) Biochemistry , vol.27 , Issue.5 , pp. 1622-1628
    • Maret, W.1    Auld, D.S.2
  • 43
    • 40949108071 scopus 로고    scopus 로고
    • Thionein/metallothionein control Zn(II) availability and the activity of enzymes
    • Krezel, A., and Maret, W. (2008) Thionein/metallothionein control Zn(II) availability and the activity of enzymes. J. Biol. Inorg. Chem. 13, 401-409
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 401-409
    • Krezel, A.1    Maret, W.2
  • 44
    • 0343580454 scopus 로고    scopus 로고
    • Perturbations to the active site of phosphotriesterase
    • DOI 10.1021/bi962099l
    • Kuo, J. M., Chae, M. Y., and Raushel, F. M. (1997) Perturbations to the active site of phosphotriesterase. Biochemistry 36, 1982-1988 (Pubitemid 27104687)
    • (1997) Biochemistry , vol.36 , Issue.8 , pp. 1982-1988
    • Kuo, J.M.1    Chae, M.Y.2    Raushel, F.M.3
  • 45
    • 0035826614 scopus 로고    scopus 로고
    • Thermodynamics of metal ion binding. 1. Metal ion binding by wild-type carbonic anhydrase
    • DOI 10.1021/bi001731e
    • DiTusa, C. A., Christensen, T., McCall, K. A., Fierke, C. A., and Toone, E. J. (2001) Thermodynamics of metal ion binding. 1. Metal ion binding by wild-type carbonic anhydrase. Biochemistry 40, 5338-5344 (Pubitemid 32458233)
    • (2001) Biochemistry , vol.40 , Issue.18 , pp. 5338-5344
    • DiTusa, C.A.1    Christensen, T.2    McCall, K.A.3    Fierke, C.A.4    Toone, E.J.5
  • 46
    • 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. G. (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B Condens. Matter 37, 785-789
    • (1988) Phys. Rev. B Condens. Matter , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 47
    • 84861735979 scopus 로고    scopus 로고
    • Accelrys Inc., San Diego, CA
    • DMol3 User Guide, S. D. (2003) Accelrys Inc., San Diego, CA
    • (2003) DMol3 User Guide, S. D.
  • 48
    • 0043049887 scopus 로고
    • A multicenter numerical integration scheme for polyatomic molecules
    • Becke, A. D. (1988) A multicenter numerical integration scheme for polyatomic molecules. J. Chem. Phys. 88, 2547-2553
    • (1988) J. Chem. Phys. , vol.88 , pp. 2547-2553
    • Becke, A.D.1
  • 49
    • 77950635312 scopus 로고    scopus 로고
    • Density functional modeling of the local structure of kaolinite subjected to thermal dehydroxylation
    • White, C. E., Provis, J. L., Proffen, T., Riley, D. P., and van Deventer, J. S. (2010) Density functional modeling of the local structure of kaolinite subjected to thermal dehydroxylation. J. Phys. Chem. A 114, 4988-4996
    • (2010) J. Phys. Chem. A , vol.114 , pp. 4988-4996
    • White, C.E.1    Provis, J.L.2    Proffen, T.3    Riley, D.P.4    Van Deventer, J.S.5
  • 50
    • 33751157086 scopus 로고
    • Conductor-like screening model for real solvents. A new approach to the quantitative calculation of solvation phenomena
    • Klamt, A. (1995) Conductor-like screening model for real solvents. A new approach to the quantitative calculation of solvation phenomena. J. Phys. Chem. A 99, 2224-2235
    • (1995) J. Phys. Chem. A , vol.99 , pp. 2224-2235
    • Klamt, A.1
  • 51
    • 0001446453 scopus 로고
    • Absolute electronegativity and hardness correlated with molecular orbital theory
    • Pearson, R. G. (1986) Absolute electronegativity and hardness correlated with molecular orbital theory. Proc. Natl. Acad. Sci. U.S.A. 83, 8440-8441
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8440-8441
    • Pearson, R.G.1
  • 52
    • 0038281434 scopus 로고    scopus 로고
    • Ionization potential, electron affinity, electronegativity, hardness, and electron excitation energy. Molecular properties from density functional theory orbital energies
    • Zhan, C.-G., Nichols, J. A., and Dixon, D. A. (2003) Ionization potential, electron affinity, electronegativity, hardness, and electron excitation energy. Molecular properties from density functional theory orbital energies. J. Phys. Chem. A 107, 4184-4195
    • (2003) J. Phys. Chem. A , vol.107 , pp. 4184-4195
    • Zhan, C.-G.1    Nichols, J.A.2    Dixon, D.A.3
  • 53
    • 0000976633 scopus 로고
    • Electronic structures of molecules XI. Electroaffinity, molecular orbitals, and dipole moments
    • Mulliken, R. (1935) Electronic structures of molecules XI. Electroaffinity, molecular orbitals, and dipole moments. J. Chem. Phys. 3,
    • (1935) J. Chem. Phys. , vol.3
    • Mulliken, R.1
  • 54
    • 0347291894 scopus 로고
    • Absolute hardness: Companion parameter to absolute electronegativity
    • Parr, R. G., and Pearson, R. G. (1983) Absolute hardness: companion parameter to absolute electronegativity. J. Am. Chem. Soc. 105, 7512-7516
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 7512-7516
    • Parr, R.G.1    Pearson, R.G.2
  • 55
    • 0020756718 scopus 로고
    • Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase
    • Makinen, M. W., Maret, W., and Yim, M. B. (1983) Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 80, 2584-2588
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 2584-2588
    • Makinen, M.W.1    Maret, W.2    Yim, M.B.3
  • 58
    • 34548164849 scopus 로고    scopus 로고
    • Phenotypic classification of mutants: A tool for understanding ligand binding and activation of muscarinic acetylcholine receptors
    • Hulme, E. C., Bee, M. S., and Goodwin, J. A. (2007) Phenotypic classification of mutants. A tool for understanding ligand binding and activation of muscarinic acetylcholine receptors. Biochem. Soc. Trans. 35, 742-745 (Pubitemid 47310358)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.4 , pp. 742-745
    • Hulme, E.C.1    Bee, M.S.2    Goodwin, J.A.3
  • 59
    • 79954561773 scopus 로고    scopus 로고
    • First principles-based calculations of free energy of binding. Application to ligand binding in a self-assembling superstructure
    • Fox, S., Wallnoefer, H. G., Fox, T., Tautermann, C. S., and Skylaris, C.-K. (2011) First principles-based calculations of free energy of binding. Application to ligand binding in a self-assembling superstructure. J. Chem. Theory Comput. 7, 1102-1108
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 1102-1108
    • Fox, S.1    Wallnoefer, H.G.2    Fox, T.3    Tautermann, C.S.4    Skylaris, C.-K.5
  • 60
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts, I. L., Nadassy, K., and Wodak, S. J. (1998) Analysis of zinc binding sites in protein crystal structures. Protein Sci. 7, 1700-1716 (Pubitemid 29133175)
    • (1998) Protein Science , vol.7 , Issue.8 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 61
    • 0037366128 scopus 로고    scopus 로고
    • 2+, and zinc binding and selectivity in proteins
    • 2+, and zinc binding and selectivity in proteins. Chem. Rev. 103, 773-788
    • (2003) Chem. Rev. , vol.103 , pp. 773-788
    • Dudev, T.1    Lim, C.2
  • 62
    • 33750368382 scopus 로고    scopus 로고
    • Estimation of electronegativity values of elements in different valence states
    • DOI 10.1021/jp062886k
    • Li, K., and Xue, D. (2006) Estimation of electronegativity values of elements in different valence states. J. Phys. Chem. A 110, 11332-11337 (Pubitemid 44626505)
    • (2006) Journal of Physical Chemistry A , vol.110 , Issue.39 , pp. 11332-11337
    • Li, K.1    Xue, D.2
  • 63
    • 0000819172 scopus 로고    scopus 로고
    • Trigonal-planar zinc(II) and cadmium(II) Tris(phenoxide) Complexes
    • Darensbourg, D. J., Niezgoda, S. A., Draper, J. D., and Reibenspies, J. H. (1999) Trigonal-planar zinc(II) and cadmium(II) Tris(phenoxide) Complexes. Inorg. Chem. 38, 1356-1359
    • (1999) Inorg. Chem. , vol.38 , pp. 1356-1359
    • Darensbourg, D.J.1    Niezgoda, S.A.2    Draper, J.D.3    Reibenspies, J.H.4
  • 64
    • 0024848116 scopus 로고
    • - complex. A possible new coordination mode for zinc-cysteine centers
    • DOI 10.1021/ja00205a052
    • Gruff, E. S., and Koch, S. A. (1989) Trigonal planar [Zn(SR)3]1-complex. A possible new coordination mode for zinc-cysteine centers.J. Am. Chem. Soc. 111, 8762-8763 (Pubitemid 20021846)
    • (1989) Journal of the American Chemical Society , vol.111 , Issue.23 , pp. 8762-8763
    • Gruff, E.S.1    Koch, S.A.2
  • 65
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites. Biometals 14, 271-313
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 66
    • 43449131553 scopus 로고    scopus 로고
    • Physical basis of structural and catalytic zinc-binding sites in proteins
    • Lee, Y. M., and Lim, C. (2008) Physical basis of structural and catalytic zinc-binding sites in proteins. J. Mol. Biol. 379, 545-553
    • (2008) J. Mol. Biol. , vol.379 , pp. 545-553
    • Lee, Y.M.1    Lim, C.2
  • 67
    • 0345114077 scopus 로고
    • Hard and soft acids and bases
    • Pearson, R. G. (1963) Hard and soft acids and bases. J. Am. Chem. Soc. 85, 3533-3539
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 3533-3539
    • Pearson, R.G.1
  • 68
    • 78249281661 scopus 로고    scopus 로고
    • Discrimination between hard metals with soft ligand donor atoms. An on-fluorescence probe for manganese (II)
    • Liang, J., and Canary, J. W. (2010) Discrimination between hard metals with soft ligand donor atoms. An on-fluorescence probe for manganese (II). Angew. Chem. Int. Ed. 49, 7710-7713
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 7710-7713
    • Liang, J.1    Canary, J.W.2
  • 69
    • 0026409452 scopus 로고
    • Structural biology of zinc
    • Christianson, D. W. (1991) Structural biology of zinc. Adv. Protein. Chem. 42, 281-355
    • (1991) Adv. Protein. Chem. , vol.42 , pp. 281-355
    • Christianson, D.W.1
  • 70
    • 0029069437 scopus 로고
    • The effect of salt and site-directed mutations on the iron(III)-binding site of human serum transferrin as probed by EPR spectroscopy
    • Grady, J. K., Mason, A. B., Woodworth, R. C., and Chasteen, N. D. (1995) The effect of salt and site-directed mutations on the iron(III)-binding site of human serum transferrin as probed by EPR spectroscopy. Biochem. J. 309, 403-410
    • (1995) Biochem. J. , vol.309 , pp. 403-410
    • Grady, J.K.1    Mason, A.B.2    Woodworth, R.C.3    Chasteen, N.D.4
  • 71
    • 0035979330 scopus 로고    scopus 로고
    • 2+ binding site of bacteriophage λphosphoprotein phosphatase. Effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities
    • 2+ binding site of bacteriophage λphosphoprotein phosphatase. Effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities. Biochemistry 40, 8918-8929
    • (2001) Biochemistry , vol.40 , pp. 8918-8929
    • White, D.J.1    Reiter, N.J.2    Sikkink, R.A.3    Yu, L.4    Rusnak, F.5
  • 73
    • 0000390128 scopus 로고    scopus 로고
    • Glycine residues provide flexibility for enzyme active sites
    • DOI 10.1074/jbc.272.6.3190
    • Yan, B. X., and Sun, Y. Q. (1997) Glycine residues provide flexibility for enzyme active sites. J. Biol. Chem. 272, 3190-3194 (Pubitemid 27066807)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3190-3194
    • Yan, B.X.1    Sun, Q.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.