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Volumn 151, Issue 1-2, 2010, Pages 39-45

Individual contributions of the aromatic chromophores to the near-UV Circular Dichroism in class A c-lactamases: A comparative computational analysis

Author keywords

Aromatic chromophores; Class lactamase; Excited states; Matrix method; Rotational strength; Tyrosine and tryptophan chromophores

Indexed keywords

BETA LACTAMASE; BETA LACTAMASE CLASS A; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 77954757373     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.05.003     Document Type: Article
Times cited : (4)

References (48)
  • 1
    • 14844366787 scopus 로고    scopus 로고
    • Introduction: antibiotic resistance
    • Walsh C., Wright G. Introduction: antibiotic resistance. Chem. Rev. 2005, 105:391-393.
    • (2005) Chem. Rev. , vol.105 , pp. 391-393
    • Walsh, C.1    Wright, G.2
  • 3
    • 70349452283 scopus 로고    scopus 로고
    • Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase
    • Marciano D.C., Brown N.G., Palzkill T. Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase. Protein Sci. 2009, 18:2080-2089.
    • (2009) Protein Sci. , vol.18 , pp. 2080-2089
    • Marciano, D.C.1    Brown, N.G.2    Palzkill, T.3
  • 4
    • 43249098735 scopus 로고    scopus 로고
    • Relationship between chiroptical properties, structural changes and interactions in enzymes: a computational study on beta-lactamases from class A
    • Christov C., Karabencheva T., Lodola A. Relationship between chiroptical properties, structural changes and interactions in enzymes: a computational study on beta-lactamases from class A. Comput. Biol. Chem. 2008, 32:167-175.
    • (2008) Comput. Biol. Chem. , vol.32 , pp. 167-175
    • Christov, C.1    Karabencheva, T.2    Lodola, A.3
  • 5
    • 33645699595 scopus 로고    scopus 로고
    • Molecular mechanisms of antibiotic resistance: QM/MM modelling of deacylation in a class A beta-lactamase
    • Hermann J.C., Ridder L., Hotje H.D., Mulholland A.J. Molecular mechanisms of antibiotic resistance: QM/MM modelling of deacylation in a class A beta-lactamase. Org. Biomol. Chem. 2006, 4:206-210.
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 206-210
    • Hermann, J.C.1    Ridder, L.2    Hotje, H.D.3    Mulholland, A.J.4
  • 7
    • 0028802117 scopus 로고
    • Contribution of mutant analysis to the understanding of enzyme catalysis - the case of class-a beta-lactamases
    • Matagne A., Frere J.M. Contribution of mutant analysis to the understanding of enzyme catalysis - the case of class-a beta-lactamases. Biochim. Biophys. Acta-Protein Struct. Molecular Enzymol. 1995, 1246:109-127.
    • (1995) Biochim. Biophys. Acta-Protein Struct. Molecular Enzymol. , vol.1246 , pp. 109-127
    • Matagne, A.1    Frere, J.M.2
  • 9
    • 0018339835 scopus 로고
    • The interpretaion of near-ultraviolet circular dichroism
    • Kahn P.C. The interpretaion of near-ultraviolet circular dichroism. Meth. Enzymol. 1979, 61:339.
    • (1979) Meth. Enzymol. , vol.61 , pp. 339
    • Kahn, P.C.1
  • 11
    • 75649121834 scopus 로고    scopus 로고
    • Synthesis of enantiopure sulfonimidamides and elucidation of their absolute configuration by comparison of measured and calculated CD spectra and X-ray crystal structure determination
    • Worch C., Atodiresei I., Raabe G., Bolm C. Synthesis of enantiopure sulfonimidamides and elucidation of their absolute configuration by comparison of measured and calculated CD spectra and X-ray crystal structure determination. Chemistry 2009, 16:677-683.
    • (2009) Chemistry , vol.16 , pp. 677-683
    • Worch, C.1    Atodiresei, I.2    Raabe, G.3    Bolm, C.4
  • 12
    • 34250899133 scopus 로고    scopus 로고
    • Quantum-chemical calculations on the electronic circular dichroism of (-)-dibromophakellin and (-)-dibromophakellstatin
    • Atodiresei I., Zollinger M., Lindel T., Fleischhauer J., Raabe G. Quantum-chemical calculations on the electronic circular dichroism of (-)-dibromophakellin and (-)-dibromophakellstatin. Chirality 2007, 19:542-549.
    • (2007) Chirality , vol.19 , pp. 542-549
    • Atodiresei, I.1    Zollinger, M.2    Lindel, T.3    Fleischhauer, J.4    Raabe, G.5
  • 13
    • 34249686052 scopus 로고    scopus 로고
    • Application of electronic circular dichroism in configurational and conformational analysis of organic compounds
    • Berova N., Di Bari L., Pescitelli G. Application of electronic circular dichroism in configurational and conformational analysis of organic compounds. Chem. Soc. Rev. 2007, 36:914-931.
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 914-931
    • Berova, N.1    Di Bari, L.2    Pescitelli, G.3
  • 14
    • 0242696058 scopus 로고    scopus 로고
    • Individual tyrosine side-chain contributions to circular dichroism of ribonuclease
    • Woody A.Y.M., Woody R.W. Individual tyrosine side-chain contributions to circular dichroism of ribonuclease. Biopolymers 2003, 72:500-513.
    • (2003) Biopolymers , vol.72 , pp. 500-513
    • Woody, A.Y.M.1    Woody, R.W.2
  • 16
    • 77954762345 scopus 로고    scopus 로고
    • C Christov: PhD Thesis, PhD, Bulgarian Academy of Sciences, Sofia
    • C Christov: PhD Thesis, PhD, Bulgarian Academy of Sciences, Sofia, 2002.
    • (2002)
  • 17
    • 0039894210 scopus 로고    scopus 로고
    • Calculation of the CD spectrum of class A beta-lactamase from Escherichia coli (TEM-1)
    • Christov C., Gabriel S., Atanasov B., Fleischhauer J. Calculation of the CD spectrum of class A beta-lactamase from Escherichia coli (TEM-1). Z. Naturforsch. A 2001, 56:757-760.
    • (2001) Z. Naturforsch. A , vol.56 , pp. 757-760
    • Christov, C.1    Gabriel, S.2    Atanasov, B.3    Fleischhauer, J.4
  • 18
    • 10344237532 scopus 로고    scopus 로고
    • Mechanisms of generation of the rotational strengths in TEM-1 ß-lactamase part II: theoretical study of the effects of the electrostatic interactions in the near-UV
    • Christov C., Kantardjiev A., Karabencheva T., Tielens F. Mechanisms of generation of the rotational strengths in TEM-1 ß-lactamase part II: theoretical study of the effects of the electrostatic interactions in the near-UV. Chem. Phys. Lett. 2004, 400:524-530.
    • (2004) Chem. Phys. Lett. , vol.400 , pp. 524-530
    • Christov, C.1    Kantardjiev, A.2    Karabencheva, T.3    Tielens, F.4
  • 19
    • 7044256879 scopus 로고    scopus 로고
    • Mechanisms of generation of rotational strengths in TEM-1 beta-lactamase. Part I: theoretical analysis of the influences of conformational changes in the near-UV
    • Christov C., Karabencheva T. Mechanisms of generation of rotational strengths in TEM-1 beta-lactamase. Part I: theoretical analysis of the influences of conformational changes in the near-UV. Chem. Phys. Lett. 2004, 396:282-287.
    • (2004) Chem. Phys. Lett. , vol.396 , pp. 282-287
    • Christov, C.1    Karabencheva, T.2
  • 20
    • 33644776777 scopus 로고    scopus 로고
    • Modeling study of the influences of the aromatic transitions and the local environment on the far-UV rotational strengths in TEM-1 beta-lactamase
    • Christov C., Tielens F., Mirazchiiski M. Modeling study of the influences of the aromatic transitions and the local environment on the far-UV rotational strengths in TEM-1 beta-lactamase. J. Mol. Model. 2006, 12:411-416.
    • (2006) J. Mol. Model. , vol.12 , pp. 411-416
    • Christov, C.1    Tielens, F.2    Mirazchiiski, M.3
  • 21
    • 41749089998 scopus 로고    scopus 로고
    • Aromatic interactions and rotational strengths within protein environment: an electronic structural study on beta-lactamases from class A
    • Christov C., Karabencheva T., Lodola A. Aromatic interactions and rotational strengths within protein environment: an electronic structural study on beta-lactamases from class A. Chem. Phys. Lett. 2008, 456:89-95.
    • (2008) Chem. Phys. Lett. , vol.456 , pp. 89-95
    • Christov, C.1    Karabencheva, T.2    Lodola, A.3
  • 22
    • 0031923940 scopus 로고    scopus 로고
    • Beta-lactamases as models for protein-folding studies
    • Vanhove M., Lejeune A., Pain R.H. Beta-lactamases as models for protein-folding studies. Cell. Mol. Life Sci. 1998, 54:372-377.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 372-377
    • Vanhove, M.1    Lejeune, A.2    Pain, R.H.3
  • 23
    • 7044272784 scopus 로고    scopus 로고
    • Comparative theoretical study of the mechanisms of generation of rotational strengths in the near-UV in beta-lactamases from class A
    • Karabencheva T., Christov C. Comparative theoretical study of the mechanisms of generation of rotational strengths in the near-UV in beta-lactamases from class A. Chem. Phys. Lett. 2004, 398:511-516.
    • (2004) Chem. Phys. Lett. , vol.398 , pp. 511-516
    • Karabencheva, T.1    Christov, C.2
  • 26
    • 79251623123 scopus 로고    scopus 로고
    • Atomistic Insight in Protein Circular Dichroism: Computational Dissection of Contributions of Individual Chromophores in TEM-1 ß-Lactamase. Submited for publication Theor Chem Acc, doi:10.1007/s00214-010-0744-4
    • C Christov, T Karabencehva: Atomistic Insight in Protein Circular Dichroism: Computational Dissection of Contributions of Individual Chromophores in TEM-1 ß-Lactamase. Submited for publication Theor Chem Acc. (2010), doi:10.1007/s00214-010-0744-4.
    • (2010)
    • Christov, C.1    Karabencehva, T.2
  • 33
    • 36849127374 scopus 로고
    • Theory of one-electron rotatory power
    • Condon E.U. Theory of one-electron rotatory power. J. Chem. Phys. 1937, 5:753.
    • (1937) J. Chem. Phys. , vol.5 , pp. 753
    • Condon, E.U.1
  • 34
    • 37049170445 scopus 로고
    • The physical significance of optical rotatory power
    • Kuhn W. The physical significance of optical rotatory power. Trans. Faraday Soc. 1930, 46:293-308.
    • (1930) Trans. Faraday Soc. , vol.46 , pp. 293-308
    • Kuhn, W.1
  • 35
    • 36849120258 scopus 로고
    • On the theory of optical rotatory power
    • Kirkwood J.G. On the theory of optical rotatory power. J. Chem. Phys. 1937, 5:479-491.
    • (1937) J. Chem. Phys. , vol.5 , pp. 479-491
    • Kirkwood, J.G.1
  • 37
    • 33947321475 scopus 로고
    • Symmetry rules for optical rotation
    • Schellman J. Symmetry rules for optical rotation. Acc. Chem. Res. 1968, 1:144-151.
    • (1968) Acc. Chem. Res. , vol.1 , pp. 144-151
    • Schellman, J.1
  • 38
    • 0014448179 scopus 로고
    • Rotatory properties of molecules containing two peptide groups: theory
    • Bayley P.M., Nielsen E.B., Schellman J.A. Rotatory properties of molecules containing two peptide groups: theory. J. Phys. Chem. 1969, 73:228-243.
    • (1969) J. Phys. Chem. , vol.73 , pp. 228-243
    • Bayley, P.M.1    Nielsen, E.B.2    Schellman, J.A.3
  • 40
    • 0000291490 scopus 로고
    • Chiroptical properties of proteins. 1. Near-ultraviolet circular-dichroism of ribonuclease-S
    • Goux W.J., Hooker T.M. Chiroptical properties of proteins. 1. Near-ultraviolet circular-dichroism of ribonuclease-S. J. Am. Chem. Soc. 1980, 102:7080-7087.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7080-7087
    • Goux, W.J.1    Hooker, T.M.2
  • 41
    • 77954763237 scopus 로고    scopus 로고
    • B Kramer: Ph.D. thesis, RWTH Aachen, 1991.
    • B Kramer: Ph.D. thesis, RWTH Aachen, 1991.
  • 42
    • 0033578401 scopus 로고    scopus 로고
    • Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor
    • Sreerama N., Manning M.C., Powers M.E., Zhang J.X., Goldenberg D.P., Woody R.W. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor. Biochemistry 1999, 38:10814-10822.
    • (1999) Biochemistry , vol.38 , pp. 10814-10822
    • Sreerama, N.1    Manning, M.C.2    Powers, M.E.3    Zhang, J.X.4    Goldenberg, D.P.5    Woody, R.W.6
  • 44
    • 0032748895 scopus 로고    scopus 로고
    • Theoretical studies toward quantitative protein circular dichroism calculations
    • Besley N.A., Hirst J.D. Theoretical studies toward quantitative protein circular dichroism calculations. J. Am. Chem. Soc. 1999, 121:9636-9644.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9636-9644
    • Besley, N.A.1    Hirst, J.D.2
  • 45
    • 0042287851 scopus 로고    scopus 로고
    • Influence of tyrosine on the electronic circular dichroism of helical peptides
    • Bhattacharjee S., Toth G., Lovas S., Hirst J.D. Influence of tyrosine on the electronic circular dichroism of helical peptides. J. Phys. Chem. B 2003, 107:8682-8688.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 8682-8688
    • Bhattacharjee, S.1    Toth, G.2    Lovas, S.3    Hirst, J.D.4
  • 46
    • 33646400824 scopus 로고    scopus 로고
    • First-principles calculations of protein circular dichroism in the far-ultraviolet and beyond
    • Oakley M.T., Bulheller B.M., Hirst J.D. First-principles calculations of protein circular dichroism in the far-ultraviolet and beyond. Chirality 2006, 18:340-347.
    • (2006) Chirality , vol.18 , pp. 340-347
    • Oakley, M.T.1    Bulheller, B.M.2    Hirst, J.D.3


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