메뉴 건너뛰기




Volumn 86, Issue , 2017, Pages 387-415

Electric fields and enzyme catalysis

Author keywords

Electric fields; Enzyme electrostatics; Infrared spectroscopy; Preorganization; Protein biophysics; Vibrational Stark effect

Indexed keywords

CARBONYL DERIVATIVE; ENZYME; ISOMERASE; OXOSTEROID; SOLVENT; 4-CHLOROBENZOYL COENZYME A DEHALOGENASE; BACTERIAL PROTEIN; HYDROLASE; STEROID DELTA ISOMERASE;

EID: 84987861629     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-061516-044432     Document Type: Review
Times cited : (335)

References (161)
  • 1
    • 0009369386 scopus 로고
    • Observation of the separation of spectral lines by an electric field
    • Stark J. (1913). Observation of the separation of spectral lines by an electric field. Nature 92(2301): 401
    • (1913) Nature , vol.92 , Issue.2301 , pp. 401
    • Stark, J.1
  • 2
    • 6344286862 scopus 로고
    • Lanalogo elettrico del fenomeno diZeeman e la costituzione dellatomo
    • Lo Surdo A. (1914). Lanalogo elettrico del fenomeno diZeeman e la costituzione dellatomo. Leletrotecnica 1: 624-34
    • (1914) Leletrotecnica , vol.1 , pp. 624-634
    • Lo Surdo, A.1
  • 3
    • 6344230203 scopus 로고    scopus 로고
    • A simultaneous discovery: The case of Johannes Stark and Antonino Lo Surdo
    • Leone M, Paoletti A, Robotti N. (2004). A simultaneous discovery: the case of Johannes Stark and Antonino Lo Surdo. Phys. Perspect. 6: 271-94
    • (2004) Phys. Perspect , vol.6 , pp. 271-294
    • Leone, M.1    Paoletti, A.2    Robotti, N.3
  • 4
    • 36149022808 scopus 로고
    • The Stark effect from the point of view of Schroedingers quantum theory
    • Epstein PS. (1926). The Stark effect from the point of view of Schroedingers quantum theory. Phys. Rev. 28: 695-710
    • (1926) Phys. Rev , vol.28 , pp. 695-710
    • Epstein, P.S.1
  • 5
    • 84981796364 scopus 로고
    • Electrochromism and solvatochromism
    • Liptay W. (1969). Electrochromism and solvatochromism. Angew. Chem. Int. Ed. 8(3): 177-88
    • (1969) Angew. Chem. Int. Ed , vol.8 , Issue.3 , pp. 177-188
    • Liptay, W.1
  • 6
    • 33947087821 scopus 로고
    • Electric field effects on oriented molecules and molecular crystals
    • Hochstrasser RM. (1973). Electric field effects on oriented molecules and molecular crystals. Acc. Chem. Res. 6: 263-69
    • (1973) Acc. Chem. Res , vol.6 , pp. 263-269
    • Hochstrasser, R.M.1
  • 7
    • 84858759425 scopus 로고
    • Experimental and theoretical studies on the excited state polarizabilities of benzene, naphthalene and anthracene
    • Mathies R, Albrecht AC. (1974). Experimental and theoretical studies on the excited state polarizabilities of benzene, naphthalene and anthracene. J. Chem. Phys. 60: 2500-8
    • (1974) J. Chem. Phys , vol.60 , pp. 2500-2508
    • Mathies, R.1    Albrecht, A.C.2
  • 8
    • 0001718556 scopus 로고
    • Retinal has a highly dipolar vertically excited singlet state: Implications for vision
    • Mathies R, Stryer L. (1976). Retinal has a highly dipolar vertically excited singlet state: implications for vision. PNAS 73(7): 2169-73
    • (1976) PNAS , vol.73 , Issue.7 , pp. 2169-2173
    • Mathies, R.1    Stryer, L.2
  • 9
    • 0000460141 scopus 로고
    • Magnitude and direction of the change in dipole moment associated with excitation of the primary electron donor in Rhodopseudomonas sphaeroides reaction centers
    • Lockhart DJ, Boxer SG. (1987). Magnitude and direction of the change in dipole moment associated with excitation of the primary electron donor in Rhodopseudomonas sphaeroides reaction centers. Biochemistry 26: 664-68
    • (1987) Biochemistry , vol.26 , pp. 664-668
    • Lockhart, D.J.1    Boxer, S.G.2
  • 10
    • 0025758270 scopus 로고
    • Large protein-induced dipoles for a symmetric carotenoid in a photosynthetic antenna complex
    • Gottfried DS, Steffen MA, Boxer SG. (1991). Large protein-induced dipoles for a symmetric carotenoid in a photosynthetic antenna complex. Science 251(4994): 662-65
    • (1991) Science , vol.251 , Issue.4994 , pp. 662-665
    • Gottfried, D.S.1    Steffen, M.A.2    Boxer, S.G.3
  • 11
    • 0004214524 scopus 로고
    • London: Longmans Green
    • Haldane JBS. (1930). Enzymes. London: Longmans Green
    • (1930) Enzymes
    • Haldane, J.B.S.1
  • 12
    • 84855649802 scopus 로고    scopus 로고
    • Catalytic proficiency: The extreme case of S-O cleaving sulfatases
    • Edwards DR, Lohman DC, Wolfenden R. (2012). Catalytic proficiency: the extreme case of S-O cleaving sulfatases. J. Am. Chem. Soc. 134: 525-31
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 525-531
    • Edwards, D.R.1    Lohman, D.C.2    Wolfenden, R.3
  • 13
    • 0038286174 scopus 로고    scopus 로고
    • The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases
    • Lad C, Williams N, Wolfenden R. (2003). The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases. PNAS 100: 5607-10
    • (2003) PNAS , vol.100 , pp. 5607-5610
    • Lad, C.1    Williams, N.2    Wolfenden, R.3
  • 14
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka A, Wolfenden R. (1995). A proficient enzyme. Science 267(5194): 90-93
    • (1995) Science , vol.267 , Issue.5194 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 16
    • 0346726109 scopus 로고    scopus 로고
    • How enzymes work: Analysis by modern rate theory and computer simulations
    • Garcia-Viloca M, Gao J, Karplus M, Truhlar DG. (2004). How enzymes work: analysis by modern rate theory and computer simulations. Science 303(5655): 186-95
    • (2004) Science , vol.303 , Issue.5655 , pp. 186-195
    • Garcia-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 17
    • 0034656302 scopus 로고    scopus 로고
    • So do we understand how enzymes work?
    • Blow D. (2000). So do we understand how enzymes work? Structure 8(4): R77-81
    • (2000) Structure , vol.8 , Issue.4 , pp. R77-R81
    • Blow, D.1
  • 18
    • 0024298964 scopus 로고
    • How do enzymes work?
    • Kraut J. (1988). How do enzymes work? Science 242: 533-40
    • (1988) Science , vol.242 , pp. 533-540
    • Kraut, J.1
  • 19
    • 33947547892 scopus 로고
    • Molecular architecture and biological reactions
    • Pauling L. (1946). Molecular architecture and biological reactions. Chem. Eng. News 24(10): 1375-77
    • (1946) Chem. Eng. News , vol.24 , Issue.10 , pp. 1375-1377
    • Pauling, L.1
  • 20
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme: A three-dimensional Fourier synthesis at 2Å resolution
    • Blake CCF, Koenig DF, Mair GA, North ACT, Phillips DC, Sarma VR. (1965). Structure of hen egg-white lysozyme: a three-dimensional Fourier synthesis at 2Å resolution. Nature 206: 757-61
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 21
    • 0002102170 scopus 로고
    • On the nature of the binding of hexa-N-Acetyl glucosamine substrate to lysozyme
    • ed.ERBlout, FABovey, MGoodman, NLotan NewYork Wiley
    • Levitt M. (1974). On the nature of the binding of hexa-N-Acetyl glucosamine substrate to lysozyme. In Peptides, Polypeptides, and Proteins, ed.ERBlout, FABovey, MGoodman, NLotan, pp. 99-113.NewYork: Wiley
    • (1974) Peptides, Polypeptides, and Proteins , pp. 99-113
    • Levitt, M.1
  • 22
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzymic catalysis: The Circe effect
    • Jencks WP. (1975). Binding energy, specificity, and enzymic catalysis: the Circe effect. Adv. Enzymol. Relat. Areas Mol. Biol. 43: 219-410
    • (1975) Adv. Enzymol. Relat. Areas Mol. Biol , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 23
    • 84875636822 scopus 로고    scopus 로고
    • Specificity in transition state binding: The Pauling model revisited
    • Amyes TL, Richard JP. (2013). Specificity in transition state binding: the Pauling model revisited. Biochemistry 52(12): 2021-35
    • (2013) Biochemistry , vol.52 , Issue.12 , pp. 2021-2035
    • Amyes, T.L.1    Richard, J.P.2
  • 24
    • 43649086695 scopus 로고    scopus 로고
    • Phosphate binding energy and catalysis by small and large molecules
    • Morrow JR, Amyes TL, Richard JP. (2008). Phosphate binding energy and catalysis by small and large molecules. Acc. Chem. Res. 41(4): 539-48
    • (2008) Acc. Chem. Res , vol.41 , Issue.4 , pp. 539-548
    • Morrow, J.R.1    Amyes, T.L.2    Richard, J.P.3
  • 25
    • 79955438648 scopus 로고    scopus 로고
    • OMP decarboxylase: Phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate
    • Goryanova B, Amyes TL, Gerlt JA, Richard JP. (2011). OMP decarboxylase: phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate. J. Am. Chem. Soc. 133: 6545-48
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 6545-6548
    • Goryanova, B.1    Amyes, T.L.2    Gerlt, J.A.3    Richard, J.P.4
  • 26
    • 70149104037 scopus 로고    scopus 로고
    • Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase
    • Schwans JP, Kraut DA, Herschlag D. (2009). Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase. PNAS 106: 14271-75
    • (2009) PNAS , vol.106 , pp. 14271-14275
    • Schwans, J.P.1    Kraut, D.A.2    Herschlag, D.3
  • 27
    • 33947486528 scopus 로고
    • Transition state characterization for catalyzed reactions
    • Kurz JL. (1963). Transition state characterization for catalyzed reactions. J. Am. Chem. Soc. 85: 987-91
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 987-991
    • Kurz, J.L.1
  • 28
    • 0002903441 scopus 로고
    • Analog approaches to the structure of the transition state in enzyme reactions
    • Wolfenden R. (1972). Analog approaches to the structure of the transition state in enzyme reactions. Acc. Chem. Res. 5: 10-18
    • (1972) Acc. Chem. Res , vol.5 , pp. 10-18
    • Wolfenden, R.1
  • 29
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey P, Whitt S, Tobin J. (1994). A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science 264(5167): 1927-30
    • (1994) Science , vol.264 , Issue.5167 , pp. 1927-1930
    • Frey, P.1    Whitt, S.2    Tobin, J.3
  • 30
    • 0032475836 scopus 로고    scopus 로고
    • The low barrier hydrogen bond in enzymatic catalysis
    • Cleland WW, Frey PA, Gerlt JA. (1998). The low barrier hydrogen bond in enzymatic catalysis. J. Biol. Chem. 273: 25529-32
    • (1998) J. Biol. Chem , vol.273 , pp. 25529-25532
    • Cleland, W.W.1    Frey, P.A.2    Gerlt, J.A.3
  • 32
    • 0015497445 scopus 로고
    • Subtilisin Stereochemical mechanism involving transition-state stabilization
    • Robertus JD, Kraut J, Alden RA, Birktoft JJ. (1972). Subtilisin. Stereochemical mechanism involving transition-state stabilization. Biochemistry 11: 4293-303
    • (1972) Biochemistry , vol.11 , pp. 4293-4303
    • Robertus, J.D.1    Kraut, J.2    Alden, R.A.3    Birktoft, J.J.4
  • 34
    • 77957753971 scopus 로고    scopus 로고
    • Enzyme catalysis from improved packing in their transition-state structures
    • Williams D. (2010). Enzyme catalysis from improved packing in their transition-state structures. Curr. Opin. Chem. Biol. 14: 666-70
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 666-670
    • Williams, D.1
  • 35
    • 13644271603 scopus 로고    scopus 로고
    • Positional ordering of reacting groups contributes significantly to the efficiency of proton transfer at an antibody active site
    • Seebeck FP, Hilvert D. (2005). Positional ordering of reacting groups contributes significantly to the efficiency of proton transfer at an antibody active site. J. Am. Chem. Soc. 127: 1307-12
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1307-1312
    • Seebeck, F.P.1    Hilvert, D.2
  • 36
    • 0030917908 scopus 로고    scopus 로고
    • Loss of translational entropy in binding, folding, and catalysis
    • Amzel LM. (1998). Loss of translational entropy in binding, folding, and catalysis. Proteins 28: 144-49
    • (1998) Proteins , vol.28 , pp. 144-149
    • Amzel, L.M.1
  • 37
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page M, Jencks W. (1971). Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. PNAS 68: 1678-83
    • (1971) PNAS , vol.68 , pp. 1678-1683
    • Page, M.1    Jencks, W.2
  • 38
    • 85023100437 scopus 로고
    • The effect of geminal substitution ring size and rotamer distribution on the intramolecular nucleophilic catalysis of the hydrolysis of monophenyl esters of dibasic acids and the solvolysis of the intermediate anhydrides
    • Bruice TC, Pandit UK. (1960). The effect of geminal substitution ring size and rotamer distribution on the intramolecular nucleophilic catalysis of the hydrolysis of monophenyl esters of dibasic acids and the solvolysis of the intermediate anhydrides. J. Am. Chem. Soc. 82: 5858-65
    • (1960) J. Am. Chem. Soc , vol.82 , pp. 5858-5865
    • Bruice, T.C.1    Pandit, U.K.2
  • 39
    • 0040362704 scopus 로고    scopus 로고
    • Chemical basis for enzyme catalysis
    • Bruice TC, Benkovic SJ. (2000). Chemical basis for enzyme catalysis. Biochemistry 39: 6267-74
    • (2000) Biochemistry , vol.39 , pp. 6267-6274
    • Bruice, T.C.1    Benkovic, S.J.2
  • 40
    • 0037433232 scopus 로고    scopus 로고
    • Enzymes do what is expected (chalcone isomerase versus chorismate mutase
    • Hur S, Bruice TC. (2003). Enzymes do what is expected (chalcone isomerase versus chorismate mutase). J. Am. Chem. Soc. 125: 1472-73
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1472-1473
    • Hur, S.1    Bruice, T.C.2
  • 41
  • 43
    • 0043141259 scopus 로고
    • An empirical valence bond approach for comparing reactions in solutions and in enzymes
    • Warshel A, Weiss RM. (1980). An empirical valence bond approach for comparing reactions in solutions and in enzymes. J. Am. Chem. Soc. 102: 6218-26
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 6218-6226
    • Warshel, A.1    Weiss, R.M.2
  • 44
    • 0000467270 scopus 로고
    • Electrostatic basis of structure-function correlation in proteins
    • Warshel A. (1981). Electrostatic basis of structure-function correlation in proteins. Acc. Chem. Res. 14: 284-90
    • (1981) Acc. Chem. Res , vol.14 , pp. 284-290
    • Warshel, A.1
  • 45
    • 4644373998 scopus 로고    scopus 로고
    • Enzymatic mechanisms for catalysis of enolization: Ketosteroid isomerase
    • Pollack RM. (2004). Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase. Bioorg. Chem. 32: 341-53
    • (2004) Bioorg. Chem , vol.32 , pp. 341-353
    • Pollack, R.M.1
  • 47
    • 0343791148 scopus 로고
    • Electric moments of molecules in liquids
    • Onsager L. (1936). Electric moments of molecules in liquids. J. Am. Chem. Soc. 58: 1486-93
    • (1936) J. Am. Chem. Soc , vol.58 , pp. 1486-1493
    • Onsager, L.1
  • 48
    • 0342394897 scopus 로고
    • The dielectric polarization of polar liquids
    • Kirkwood JG. (1939). The dielectric polarization of polar liquids. J. Chem. Phys. 7: 911-19
    • (1939) J. Chem. Phys , vol.7 , pp. 911-919
    • Kirkwood, J.G.1
  • 49
    • 0001229288 scopus 로고
    • Theory of the time development of the Stokes shift in polar media
    • Bagchi B, Oxtoby DW, Fleming GR. (1984). Theory of the time development of the Stokes shift in polar media. Chem. Phys. 86: 257-67
    • (1984) Chem. Phys , vol.86 , pp. 257-267
    • Bagchi, B.1    Oxtoby, D.W.2    Fleming, G.R.3
  • 50
    • 36549096336 scopus 로고
    • Femtosecond resolved solvation dynamics in polar solvents
    • Kahlow MA, Jarzeba W, Kang TJ, Barbara PF. (1989). Femtosecond resolved solvation dynamics in polar solvents. J. Chem. Phys. 90: 151-58
    • (1989) J. Chem. Phys , vol.90 , pp. 151-158
    • Kahlow, M.A.1    Jarzeba, W.2    Kang, T.J.3    Barbara, P.F.4
  • 51
    • 0542434939 scopus 로고
    • Inorganic oxidation-reduction reactions in solution electron transfers
    • Zwolinski B, Marcus R, Eyring H. (1955). Inorganic oxidation-reduction reactions in solution electron transfers. Chem. Rev. 55: 157-80
    • (1955) Chem. Rev , vol.55 , pp. 157-180
    • Zwolinski, B.1    Marcus, R.2    Eyring, H.3
  • 52
    • 0010884753 scopus 로고
    • On the theory of oxidation-reduction reactions involving electron transfer
    • Marcus R. (1956). On the theory of oxidation-reduction reactions involving electron transfer. J. Chem. Phys. 24: 966
    • (1956) J. Chem. Phys , vol.24 , pp. 966
    • Marcus, R.1
  • 53
    • 84928333221 scopus 로고    scopus 로고
    • Measuring electric fields and noncovalent interactions using the vibrational Stark effect
    • Fried SD, Boxer SG. (2015). Measuring electric fields and noncovalent interactions using the vibrational Stark effect. Acc. Chem. Res. 48: 998-1006
    • (2015) Acc. Chem. Res , vol.48 , pp. 998-1006
    • Fried, S.D.1    Boxer, S.G.2
  • 54
    • 84881071656 scopus 로고    scopus 로고
    • Measuring electrostatic fields in both hydrogen-bonding and nonhydrogen-bonding environments using carbonyl vibrational probes
    • Fried SD, Bagchi S, Boxer SG. (2013). Measuring electrostatic fields in both hydrogen-bonding and nonhydrogen-bonding environments using carbonyl vibrational probes. J. Am. Chem. Soc. 135: 11181-92
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 11181-11192
    • Fried, S.D.1    Bagchi, S.2    Boxer, S.G.3
  • 55
    • 80055014555 scopus 로고    scopus 로고
    • Direct measurements of electric fields in weak OH p hydrogen bonds
    • Saggu M, Levinson NM, Boxer SG. (2011). Direct measurements of electric fields in weak OH p hydrogen bonds. J. Am. Chem. Soc. 133: 17414-19
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 17414-17419
    • Saggu, M.1    Levinson, N.M.2    Boxer, S.G.3
  • 57
    • 37049142631 scopus 로고
    • Substitution at saturated carbon Part XIV Solvent effects on the free energies of ions, ion-pairs, non-electrolytes, and transition states in some SN and SE reactions
    • Abraham MH. (1972). Substitution at saturated carbon. Part XIV. Solvent effects on the free energies of ions, ion-pairs, non-electrolytes, and transition states in some SN and SE reactions. J. Chem. Soc. Perkin Trans. 2 10: 1343-57
    • (1972) J. Chem. Soc. Perkin Trans , vol.2 , Issue.10 , pp. 1343-1357
    • Abraham, M.H.1
  • 58
    • 0000230329 scopus 로고
    • Energetics of enzyme catalysis
    • Warshel A. (1978). Energetics of enzyme catalysis. PNAS 75: 5250-54
    • (1978) PNAS , vol.75 , pp. 5250-5254
    • Warshel, A.1
  • 59
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel A, Levitt M. (1976). Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103: 227-49
    • (1976) J. Mol. Biol , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 60
    • 0019889036 scopus 로고
    • Calculations of enzymic reactions: Calculations of pKa, proton transfer reactions, and general acid catalysis reactions in enzymes
    • Warshel A. (1981). Calculations of enzymic reactions: calculations of pKa, proton transfer reactions, and general acid catalysis reactions in enzymes. Biochemistry 20: 3167-77
    • (1981) Biochemistry , vol.20 , pp. 3167-3177
    • Warshel, A.1
  • 61
    • 0037207102 scopus 로고    scopus 로고
    • The catalytic power of ketosteroid isomerase investigated by computer simulation
    • Feierberg I, Aqvist J. (2002). The catalytic power of ketosteroid isomerase investigated by computer simulation. Biochemistry 41: 15728-35
    • (2002) Biochemistry , vol.41 , pp. 15728-15735
    • Feierberg, I.1    Aqvist, J.2
  • 62
    • 34547940340 scopus 로고    scopus 로고
    • Quantum chemical analysis of reaction paths in chorismate mutase: Conformational effects and electrostatic stabilization
    • Szefczyk B, Claeyssens F, Mulholland AJ, Sokalski WA. (2007). Quantum chemical analysis of reaction paths in chorismate mutase: conformational effects and electrostatic stabilization. Int. J. Quantum Chem. 107: 2274-85
    • (2007) Int. J. Quantum Chem , vol.107 , pp. 2274-2285
    • Szefczyk, B.1    Claeyssens, F.2    Mulholland, A.J.3    Sokalski, W.A.4
  • 63
    • 0023280069 scopus 로고
    • Calculation of electrostatic potentials in an enzyme active site
    • Gilson M, Honig B. (1987). Calculation of electrostatic potentials in an enzyme active site. Nature 330: 84-86
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.1    Honig, B.2
  • 64
    • 0024706282 scopus 로고
    • Electrostatic fields in the active sites of lysozymes
    • Sun D, Liao D, Remington S. (1989). Electrostatic fields in the active sites of lysozymes. PNAS 86: 5361-65
    • (1989) PNAS , vol.86 , pp. 5361-5365
    • Sun, D.1    Liao, D.2    Remington, S.3
  • 66
    • 0036001159 scopus 로고    scopus 로고
    • Structural basis of perturbed pKa values of catalytic groups in enzyme active sites
    • Harris TK, Turner GJ. (2002). Structural basis of perturbed pKa values of catalytic groups in enzyme active sites. IUBMB Life 53: 85-98
    • (2002) IUBMB Life , vol.53 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 67
    • 79955092337 scopus 로고    scopus 로고
    • Large shifts in pKa values of lysine residues buried inside a protein
    • Isom DG, Casta ñeda CA, Cannon BR, Garćia-Moreno B. (2011). Large shifts in pKa values of lysine residues buried inside a protein. PNAS 108: 5260-65
    • (2011) PNAS , vol.108 , pp. 5260-5265
    • Isom, D.G.1    Casta Ñeda, C.A.2    Cannon, B.R.3    Garćia-Moreno, B.4
  • 68
    • 0024594073 scopus 로고
    • Electrostatic interactions in wild-Type and mutant recombinant human myoglobins
    • Varadarajan R, Lambright DG, Boxer SG. (1989). Electrostatic interactions in wild-Type and mutant recombinant human myoglobins. Biochemistry 28: 3771-81
    • (1989) Biochemistry , vol.28 , pp. 3771-3781
    • Varadarajan, R.1    Lambright, D.G.2    Boxer, S.G.3
  • 69
    • 0041972670 scopus 로고    scopus 로고
    • How cytochromes with different folds control heme redox potentials
    • Mao J, Hauser K, Gunner MR. (2003). How cytochromes with different folds control heme redox potentials. Biochemistry 42: 9829-40
    • (2003) Biochemistry , vol.42 , pp. 9829-9840
    • Mao, J.1    Hauser, K.2    Gunner, M.R.3
  • 70
    • 0024495355 scopus 로고
    • Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin
    • Varadarajan R, Zewert TE, Gray HB, Boxer SG. (1989). Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin. Science 243: 69-72
    • (1989) Science , vol.243 , pp. 69-72
    • Varadarajan, R.1    Zewert, T.E.2    Gray, H.B.3    Boxer, S.G.4
  • 71
    • 33646262869 scopus 로고    scopus 로고
    • Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole
    • Kraut DA, Sigala PA, Pybus B, Liu CW, Ringe D, et al. (2006). Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion hole. PLOS Biol. 4(4): e99
    • (2006) PLOS Biol , vol.4 , Issue.4 , pp. e99
    • Kraut, D.A.1    Sigala, P.A.2    Pybus, B.3    Liu, C.W.4    Ringe, D.5
  • 73
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian JT, Callis PR. (2001). Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80: 2093-109
    • (2001) Biophys. J , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 74
    • 0001465616 scopus 로고
    • Chemical shifts in proteins: A shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein
    • Pearson J, Oldfield E, Lee F, Warshel A. (1993). Chemical shifts in proteins: a shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein. J. Am. Chem. Soc. 115: 6851-62
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 6851-6862
    • Pearson, J.1    Oldfield, E.2    Lee, F.3    Warshel, A.4
  • 75
    • 0009423608 scopus 로고
    • Correlation of fluorine-19 chemical shielding and chemical shift nonequivalence
    • Augspurger J, Dykstra C. (1993). Correlation of fluorine-19 chemical shielding and chemical shift nonequivalence. J. Am. Chem. Soc. 115: 12016-19
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 12016-12019
    • Augspurger, J.1    Dykstra, C.2
  • 76
    • 0000435803 scopus 로고
    • Correlation of carbon-13 and oxygen-17 chemical shifts and the vibrational frequency of electrically perturbed carbon monoxide
    • Augspurger J, Dykstra C, Oldfield E. (1991). Correlation of carbon-13 and oxygen-17 chemical shifts and the vibrational frequency of electrically perturbed carbon monoxide. J. Am. Chem. Soc. 113: 2447-51
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 2447-2451
    • Augspurger, J.1    Dykstra, C.2    Oldfield, E.3
  • 77
    • 0000103150 scopus 로고
    • Chemical shifts in the NMR spectra of molecules containing polar groups
    • Buckingham AD. (1960). Chemical shifts in the NMR spectra of molecules containing polar groups. Can. J. Chem. 38: 300-7
    • (1960) Can. J. Chem , vol.38 , pp. 300-307
    • Buckingham, A.D.1
  • 78
    • 80051673221 scopus 로고    scopus 로고
    • SHIFTX2: Significantly improved protein chemical shift prediction
    • Han B, Liu Y, Ginzinger SW, Wishart DS. (2011). SHIFTX2: significantly improved protein chemical shift prediction. J. Biomol. NMR 50: 43-57
    • (2011) J. Biomol. NMR , vol.50 , pp. 43-57
    • Han, B.1    Liu, Y.2    Ginzinger, S.W.3    Wishart, D.S.4
  • 79
    • 80054955089 scopus 로고    scopus 로고
    • Site-specific spectroscopic reporters of the local electric field, hydration, structure, and dynamics of biomolecules
    • Waegele MM, Culik RM, Gai F. (2011). Site-specific spectroscopic reporters of the local electric field, hydration, structure, and dynamics of biomolecules. J. Phys. Chem. Lett. 2: 2598-609
    • (2011) J. Phys. Chem. Lett , vol.2 , pp. 2598-2609
    • Waegele, M.M.1    Culik, R.M.2    Gai, F.3
  • 80
    • 84881082892 scopus 로고    scopus 로고
    • Infrared probes for studying the structure and dynamics of biomolecules
    • Kim H, Cho M. (2013). Infrared probes for studying the structure and dynamics of biomolecules. Chem. Rev. 113: 5817-47
    • (2013) Chem. Rev , vol.113 , pp. 5817-5847
    • Kim, H.1    Cho, M.2
  • 81
    • 84857125236 scopus 로고    scopus 로고
    • Quantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase
    • Fafarman AT, Sigala PA, Schwans JP, Fenn TD, Herschlag D, Boxer SG. (2012). Quantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase. PNAS 109(6): E299-308
    • (2012) PNAS , vol.109 , Issue.6 , pp. E299-E308
    • Fafarman, A.T.1    Sigala, P.A.2    Schwans, J.P.3    Fenn, T.D.4    Herschlag, D.5    Boxer, S.G.6
  • 82
    • 0034499168 scopus 로고    scopus 로고
    • Vibrational Stark effects of nitriles i Methods and experimental results
    • Andrews SS, Boxer SG. (2000). Vibrational Stark effects of nitriles I. Methods and experimental results. J. Phys. Chem. A 104: 11853-63
    • (2000) J. Phys. Chem , vol.A104 , pp. 11853-11863
    • Andrews, S.S.1    Boxer, S.G.2
  • 83
    • 0001300576 scopus 로고
    • Vibrational Stark effect spectroscopy
    • Chattopadhyay A, Boxer SG. (1995). Vibrational Stark effect spectroscopy. J. Am. Chem. Soc. 117: 1449-50
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 1449-1450
    • Chattopadhyay, A.1    Boxer, S.G.2
  • 84
    • 0030624708 scopus 로고    scopus 로고
    • Stark spectroscopy: Applications in chemistry, biology, and materials science
    • Bublitz GU, Boxer SG. (1997). Stark spectroscopy: applications in chemistry, biology, and materials science. Annu. Rev. Phys. Chem. 48: 213-42
    • (1997) Annu. Rev. Phys. Chem , vol.48 , pp. 213-242
    • Bublitz, G.U.1    Boxer, S.G.2
  • 85
    • 65249172623 scopus 로고    scopus 로고
    • Stark realities
    • Boxer SG. (2009). Stark realities. J. Phys. Chem. B. 113: 2972-83
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2972-2983
    • Boxer, S.G.1
  • 87
    • 0037030845 scopus 로고    scopus 로고
    • Origins of the sensitivity of molecular vibrations to electric fields: Carbonyl and nitrosyl stretches in model compounds and proteins
    • New York: Springer. 3rd ed. 87. Park ES, Boxer SG. (2002). Origins of the sensitivity of molecular vibrations to electric fields: carbonyl and nitrosyl stretches in model compounds and proteins. J. Phys. Chem. B 106: 5800-6
    • (2002) J. Phys. Chem. B , vol.106 , pp. 5800-5806
    • Park, E.S.1    Boxer, S.G.2
  • 88
    • 0001257322 scopus 로고    scopus 로고
    • Vibrational Stark spectroscopy in proteins: A probe and calibration for electrostatic fields
    • Park ES, Andrews SS, Hu RB, Boxer SG. (1999). Vibrational Stark spectroscopy in proteins: a probe and calibration for electrostatic fields. J. Phys. Chem. B. 103: 9813-17
    • (1999) J. Phys. Chem. B , vol.103 , pp. 9813-9817
    • Park, E.S.1    Andrews, S.S.2    Hu, R.B.3    Boxer, S.G.4
  • 89
    • 33746017658 scopus 로고    scopus 로고
    • Electric fields at the active site of an enzyme: Direct comparison of experiment with theory
    • Suydam IT, Snow CD, Pande VS, Boxer SG. (2006). Electric fields at the active site of an enzyme: direct comparison of experiment with theory. Science 313: 200-4
    • (2006) Science , vol.313 , pp. 200-204
    • Suydam, I.T.1    Snow, C.D.2    Pande, V.S.3    Boxer, S.G.4
  • 90
    • 84863492163 scopus 로고    scopus 로고
    • A solvatochromic model calibrates nitriles vibrational frequencies to electrostatic fields
    • Bagchi S, Fried SD, Boxer SG. (2012). A solvatochromic model calibrates nitriles vibrational frequencies to electrostatic fields. J. Am. Chem. Soc. 134: 10373-76
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 10373-10376
    • Bagchi, S.1    Fried, S.D.2    Boxer, S.G.3
  • 92
    • 77958474269 scopus 로고    scopus 로고
    • Nitrile bonds as infrared probes of electrostatics in ribonuclease S
    • Fafarman AT, Boxer SG. (2010). Nitrile bonds as infrared probes of electrostatics in ribonuclease S. J. Phys. Chem. B 114: 13536-44
    • (2010) J. Phys. Chem , vol.B114 , pp. 13536-13544
    • Fafarman, A.T.1    Boxer, S.G.2
  • 93
    • 79952751750 scopus 로고    scopus 로고
    • Dynamics of the folded and unfolded villin headpiece (HP35) measured with ultrafast 2D IR vibrational echo spectroscopy
    • Chung JK, Thielges MC, Fayer MD. (2011). Dynamics of the folded and unfolded villin headpiece (HP35) measured with ultrafast 2D IR vibrational echo spectroscopy. PNAS 108: 3578-83
    • (2011) PNAS , vol.108 , pp. 3578-3583
    • Chung, J.K.1    Thielges, M.C.2    Fayer, M.D.3
  • 94
    • 84904878087 scopus 로고    scopus 로고
    • Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase
    • Liu CT, Layfield JP, Stewart RJ III, French JB, Hanoian P, et al. (2014). Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase. J. Am. Chem. Soc. 136: 10349-60
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 10349-10360
    • Liu, C.T.1    Layfield, J.P.2    Stewart, R.J.3    French, J.B.4    Hanoian, P.5
  • 95
    • 70349303948 scopus 로고    scopus 로고
    • Nitrile groups as vibrational probes of biomolecular structure and dynamics: An overview
    • Lindquist BA, Furse KE, Corcelli SA. (2009). Nitrile groups as vibrational probes of biomolecular structure and dynamics: an overview. Phys. Chem. Chem. Phys. 11: 8119-32
    • (2009) Phys. Chem. Chem. Phys , vol.11 , pp. 8119-8132
    • Lindquist, B.A.1    Furse, K.E.2    Corcelli, S.A.3
  • 97
    • 84897114242 scopus 로고    scopus 로고
    • A conserved water-mediated hydrogen bond network defines bosutinibs kinase selectivity
    • Levinson NM, Boxer SG. (2013). A conserved water-mediated hydrogen bond network defines bosutinibs kinase selectivity. Nat. Chem. Biol. 10: 127-32
    • (2013) Nat. Chem. Biol , vol.10 , pp. 127-132
    • Levinson, N.M.1    Boxer, S.G.2
  • 98
    • 79961229861 scopus 로고    scopus 로고
    • Direct measurement of the membrane dipole field in bicelles using vibrational Stark effect spectroscopy
    • Hu W, Webb LJ. (2011). Direct measurement of the membrane dipole field in bicelles using vibrational Stark effect spectroscopy. J. Phys. Chem. Lett. 2: 1925-30
    • (2011) J. Phys. Chem. Lett , vol.2 , pp. 1925-1930
    • Hu, W.1    Webb, L.J.2
  • 99
    • 70349273994 scopus 로고    scopus 로고
    • Probing hydrogen bonding environments: Solvatochromic effects on the CN vibration of benzonitrile
    • Aschaffenburg D, Moog R. (2009). Probing hydrogen bonding environments: solvatochromic effects on the CN vibration of benzonitrile. J. Phys. Chem. B 113: 12736-43
    • (2009) J. Phys. Chem , vol.B113 , pp. 12736-12743
    • Aschaffenburg, D.1    Moog, R.2
  • 100
    • 77956634583 scopus 로고    scopus 로고
    • Decomposition of vibrational shifts of nitriles into electrostatic and hydrogen-bonding effects
    • Fafarman A, Sigala P, Herschlag D, Boxer S. (2010). Decomposition of vibrational shifts of nitriles into electrostatic and hydrogen-bonding effects. J. Am. Chem. Soc. 132: 12811-13
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 12811-12813
    • Fafarman, A.1    Sigala, P.2    Herschlag, D.3    Boxer, S.4
  • 101
    • 84969504494 scopus 로고    scopus 로고
    • Correlating nitrile IR frequencies to local electrostatics quantifies noncovalent interactions of peptides and proteins
    • Deb P, Haldar T, Kashid SM, Banerjee S, Chakrabarty S, Bagchi S. (2016). Correlating nitrile IR frequencies to local electrostatics quantifies noncovalent interactions of peptides and proteins. J. Phys. Chem. B 120: 4034-46
    • (2016) J. Phys. Chem , vol.B120 , pp. 4034-4046
    • Deb, P.1    Haldar, T.2    Kashid, S.M.3    Banerjee, S.4    Chakrabarty, S.5    Bagchi, S.6
  • 102
    • 79955398126 scopus 로고    scopus 로고
    • Vibrational solvatochromism and electrochromism of infrared probe molecules containing C=O, C=N, C==O, or C-F vibrational chromophore
    • Choi J-H, Cho M. (2011). Vibrational solvatochromism and electrochromism of infrared probe molecules containing C=O, C=N, C==O, or C-F vibrational chromophore. J. Chem. Phys. 134: 154513
    • (2011) J. Chem. Phys , vol.134 , pp. 154513
    • Choi, J.-H.1    Cho, M.2
  • 103
    • 0019316936 scopus 로고
    • Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy
    • Belasco JG, Knowles JR. (1980). Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy. Biochemistry 19(3): 472-77
    • (1980) Biochemistry , vol.19 , Issue.3 , pp. 472-477
    • Belasco, J.G.1    Knowles, J.R.2
  • 104
    • 9744257006 scopus 로고    scopus 로고
    • Quantifying energetic contributions to ground state destabilization
    • Anderson VE. (2005). Quantifying energetic contributions to ground state destabilization. Arch. Biochem. Biophys. 433: 27-33
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 27-33
    • Anderson, V.E.1
  • 105
    • 33748632360 scopus 로고    scopus 로고
    • Spectroscopic characterization of distortion in enzyme complexes
    • Carey PR. (2006). Spectroscopic characterization of distortion in enzyme complexes. Chem. Rev. 106: 3043-54
    • (2006) Chem. Rev , vol.106 , pp. 3043-3054
    • Carey, P.R.1
  • 106
    • 0026788194 scopus 로고
    • Forces, bond lengths, and reactivity: Fundamental insight into themechanism of enzyme catalysis
    • Tonge PJ, Carey PR. (1992). Forces, bond lengths, and reactivity: fundamental insight into themechanism of enzyme catalysis. Biochemistry 31: 9122-25
    • (1992) Biochemistry , vol.31 , pp. 9122-9125
    • Tonge, P.J.1    Carey, P.R.2
  • 107
    • 84922796655 scopus 로고    scopus 로고
    • Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopy
    • Reddish MJ, Peng H-L, Deng H, Panwar KS, Callener R, Dyer RB. (2014). Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopy. J. Phys. Chem. B 118: 10854-62
    • (2014) J. Phys. Chem , vol.B118 , pp. 10854-10862
    • Reddish, M.J.1    Peng, H.-L.2    Deng, H.3    Panwar, K.S.4    Callener, R.5    Dyer, R.B.6
  • 108
    • 84987897228 scopus 로고    scopus 로고
    • Vibrational Stark effects of carbonyl probes applied to re-interpret IR and Raman data for enzyme inhibitors in terms of electric fields at the active site
    • Schneider SH, Boxer SG. (2016). Vibrational Stark effects of carbonyl probes applied to re-interpret IR and Raman data for enzyme inhibitors in terms of electric fields at the active site. J. Phys. Chem. B 120: 9672-84
    • (2016) J. Phys. Chem , vol.B120 , pp. 9672-9684
    • Schneider, S.H.1    Boxer, S.G.2
  • 109
    • 84978732960 scopus 로고    scopus 로고
    • Conformational heterogeneity in the Michaelis complex of lactate dehydrogenase: An analysis of vibrational spectroscopy usingMarkov and hiddenMarkov models
    • Pan X, Schwartz SD. (2016). Conformational heterogeneity in the Michaelis complex of lactate dehydrogenase: an analysis of vibrational spectroscopy usingMarkov and hiddenMarkov models. J. Phys. Chem. B 120: 6612-20
    • (2016) J. Phys. Chem , vol.B120 , pp. 6612-6620
    • Pan, X.1    Schwartz, S.D.2
  • 110
    • 50449136029 scopus 로고
    • Enzymic isomerization of 5-3-ketosteroids
    • Talalay P, Wang VS. (1955). Enzymic isomerization of 5-3-ketosteroids. Biochim. Biophys. Acta 18: 300-1
    • (1955) Biochim. Biophys. Acta , vol.18 , pp. 300-301
    • Talalay, P.1    Wang, V.S.2
  • 111
    • 0001078277 scopus 로고
    • Oxidative degradation of testosterone by adaptive enzymes
    • Talalay P, Dobson MM, Tapley DF. (1952). Oxidative degradation of testosterone by adaptive enzymes. Nature 170: 620-21
    • (1952) Nature , vol.170 , pp. 620-621
    • Talalay, P.1    Dobson, M.M.2    Tapley, D.F.3
  • 112
    • 0001138955 scopus 로고
    • The mechanism of the5-3-ketosteroid isomerase reaction: Absorption and fluorescence spectra of enzyme-steroid complexes
    • Wang S, Kawahara F, Talalay P. (1963). The mechanism of the5-3-ketosteroid isomerase reaction: absorption and fluorescence spectra of enzyme-steroid complexes. J. Biol. Chem. 238: 576-85
    • (1963) J. Biol. Chem , vol.238 , pp. 576-585
    • Wang, S.1    Kawahara, F.2    Talalay, P.3
  • 113
    • 0026598557 scopus 로고
    • Nature of the intermediate in the 3-oxo-5-steroid isomerase reaction
    • Zeng B, Bounds P, Steiner R, Pollack R. (1992). Nature of the intermediate in the 3-oxo-5-steroid isomerase reaction. Biochemistry 31: 1521-28
    • (1992) Biochemistry , vol.31 , pp. 1521-1528
    • Zeng, B.1    Bounds, P.2    Steiner, R.3    Pollack, R.4
  • 114
    • 0024585879 scopus 로고
    • Kinetic and ultraviolet spectroscopic studies of active-site mutants of5-3-ketosteroid isomerase
    • Kuliopulos A, Mildvan A, Shortle D, Talalay P. (1989). Kinetic and ultraviolet spectroscopic studies of active-site mutants of5-3-ketosteroid isomerase. Biochemistry 28: 149-59
    • (1989) Biochemistry , vol.28 , pp. 149-159
    • Kuliopulos, A.1    Mildvan, A.2    Shortle, D.3    Talalay, P.4
  • 115
    • 0025912705 scopus 로고
    • Microscopic rate constants for the acetate ion catalyzed isomerization of 5-Androstene-3, 17-dione to 4-Androstene-3, 17-dione: A model for steroid isomerase
    • Zeng B, Pollack RM. (1991). Microscopic rate constants for the acetate ion catalyzed isomerization of 5-Androstene-3, 17-dione to 4-Androstene-3, 17-dione: a model for steroid isomerase. J. Am. Chem. Soc. 113: 3838-42
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 3838-3842
    • Zeng, B.1    Pollack, R.M.2
  • 116
    • 84981516779 scopus 로고    scopus 로고
    • Evaluation of the catalytic contribution of a positioned general base in ketosteroid isomerase
    • Lamba V, Yabukarski F, Pinney M, Herschlag D. (2016). Evaluation of the catalytic contribution of a positioned general base in ketosteroid isomerase. J. Am. Chem. Soc. 138: 9902-9
    • (2016) J. Am. Chem. Soc , vol.138 , pp. 9902-9909
    • Lamba, V.1    Yabukarski, F.2    Pinney, M.3    Herschlag, D.4
  • 117
    • 84899463140 scopus 로고    scopus 로고
    • Experimental and computational mutagenesis to investigate the positioning of a general base within an enzyme active site
    • Schwans JP, Hanoian P, Lengerich BJ, Sunden F, Gonzalez A, et al. (2014). Experimental and computational mutagenesis to investigate the positioning of a general base within an enzyme active site. Biochemistry 53(15): 2541-55
    • (2014) Biochemistry , vol.53 , Issue.15 , pp. 2541-2555
    • Schwans, J.P.1    Hanoian, P.2    Lengerich, B.J.3    Sunden, F.4    Gonzalez, A.5
  • 118
    • 84919430407 scopus 로고    scopus 로고
    • Extreme electric fields power catalysis in the active site of ketosteroid isomerase
    • Fried SD, Bagchi S, Boxer SG. (2014). Extreme electric fields power catalysis in the active site of ketosteroid isomerase. Science 346: 1510-14
    • (2014) Science , vol.346 , pp. 1510-1514
    • Fried, S.D.1    Bagchi, S.2    Boxer, S.G.3
  • 119
    • 84987811206 scopus 로고    scopus 로고
    • A critical test of the electrostatic contribution to catalysis with non-canonical amino acids in ketosteroid isomerase
    • Wu Y, Boxer SG. (2016). A critical test of the electrostatic contribution to catalysis with non-canonical amino acids in ketosteroid isomerase. J. Am. Chem. Soc. 138: 11890-95
    • (2016) J. Am. Chem. Soc , vol.138 , pp. 11890-11895
    • Wu, Y.1    Boxer, S.G.2
  • 120
    • 84901705960 scopus 로고    scopus 로고
    • Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site
    • Natarajan A, Schwans JP, Herschlag D. (2014). Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site. J. Am. Chem. Soc. 136: 7643-54
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 7643-7654
    • Natarajan, A.1    Schwans, J.P.2    Herschlag, D.3
  • 121
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L. (2002). Serine protease mechanism and specificity. Chem. Rev. 102: 4501-24
    • (2002) Chem. Rev , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 122
    • 0025005004 scopus 로고
    • Mechanistic studies of peptide prolyl cis-Trans isomerase: Evidence for catalysis by distortion
    • Harrison RK, Stein RL. (1990). Mechanistic studies of peptide prolyl cis-Trans isomerase: evidence for catalysis by distortion. Biochemistry 29: 1684-89
    • (1990) Biochemistry , vol.29 , pp. 1684-1689
    • Harrison, R.K.1    Stein, R.L.2
  • 123
    • 0027742843 scopus 로고
    • A mechanism for rotamase catalysis by the FK506 binding protein
    • Fischer S, Michnick S, Karplus M. (1993). A mechanism for rotamase catalysis by the FK506 binding protein. Biochemistry 32: 13830-37
    • (1993) Biochemistry , vol.32 , pp. 13830-13837
    • Fischer, S.1    Michnick, S.2    Karplus, M.3
  • 124
    • 84904329758 scopus 로고    scopus 로고
    • Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism
    • Camilloni C, Sahakyan AB, Holliday MJ, Isern NG, Zhang F, et al. (2014). Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism. PNAS 111: 10203-8
    • (2014) PNAS , vol.111 , pp. 10203-10208
    • Camilloni, C.1    Sahakyan, A.B.2    Holliday, M.J.3    Isern, N.G.4    Zhang, F.5
  • 125
    • 0029639694 scopus 로고
    • Exploration of possible mechanisms for 4-chlorobenzoyl CoA dehalogenase: Evidence for an aryl-enzyme intermediate
    • Crooks GP, Xu L, Barkley RM, Copley SD. (1995). Exploration of possible mechanisms for 4-chlorobenzoyl CoA dehalogenase: evidence for an aryl-enzyme intermediate. J. Am. Chem. Soc. 117: 10791
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 10791
    • Crooks, G.P.1    Xu, L.2    Barkley, R.M.3    Copley, S.D.4
  • 126
    • 0030921325 scopus 로고    scopus 로고
    • On the dehalogenation mechanism of 4-chlorobenzyl CoA by 4-chlorobenzyl CoA dehalogenase
    • Zheng Y-J, Bruice TC. (1997). On the dehalogenation mechanism of 4-chlorobenzyl CoA by 4-chlorobenzyl CoA dehalogenase. J. Am. Chem. Soc. 119: 3868-77
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 3868-3877
    • Zheng, Y.-J.1    Bruice, T.C.2
  • 127
    • 30144432502 scopus 로고    scopus 로고
    • Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: A combined theoretical and experimental study
    • Wu J, Xu D, Lu X, Wang C, Guo H, Dunaway-Mariano D. (2006). Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and experimental study. Biochemistry 45: 102-12
    • (2006) Biochemistry , vol.45 , pp. 102-112
    • Wu, J.1    Xu, D.2    Lu, X.3    Wang, C.4    Guo, H.5    Dunaway-Mariano, D.6
  • 128
    • 0000707160 scopus 로고
    • An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin
    • Corey DR, Craik CS. (1992). An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin. J. Am. Chem. Soc. 114: 1784-90
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 1784-1790
    • Corey, D.R.1    Craik, C.S.2
  • 129
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow DM, Birktoft JJ, Hartley BS. (1969). Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221: 337-40
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 130
    • 0014945734 scopus 로고
    • Structure of crystalline α-chymotrypsin: IV the structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme
    • Henderson R. (1970). Structure of crystalline α-chymotrypsin: IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J. Mol. Biol. 54: 341-54
    • (1970) J. Mol. Biol , vol.54 , pp. 341-354
    • Henderson, R.1
  • 132
    • 0034102419 scopus 로고    scopus 로고
    • Electrostatic stress in catalysis: Structure and mechanism of the enzyme orotidine monophosphate decarboxylase
    • Wu N, Mo Y, Gao J, Pai EF. (2000). Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase. PNAS 97: 2017-22
    • (2000) PNAS , vol.97 , pp. 2017-2022
    • Wu, N.1    Mo, Y.2    Gao, J.3    Pai, E.F.4
  • 133
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • Stec B, Holtz KM, Kantrowitz ER. (2000). A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J. Mol. Biol. 299: 1303-11
    • (2000) J. Mol. Biol , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 134
    • 84908499924 scopus 로고    scopus 로고
    • Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: Comparative analysis of alkaline phosphatase and protein tyrosine phosphatases
    • Andrews LD, Zalatan JG, Herschlag D. (2014). Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: comparative analysis of alkaline phosphatase and protein tyrosine phosphatases. Biochemistry 53: 6811-19
    • (2014) Biochemistry , vol.53 , pp. 6811-6819
    • Andrews, L.D.1    Zalatan, J.G.2    Herschlag, D.3
  • 135
    • 33748585807 scopus 로고    scopus 로고
    • Pericyclic reactions in biological systems-Does nature know about the Diels-Alder reaction?
    • Laschat S. (1996). Pericyclic reactions in biological systems-Does nature know about the Diels-Alder reaction? Angew. Chem. Int. Ed. 35: 289-91
    • (1996) Angew. Chem. Int. Ed , vol.35 , pp. 289-291
    • Laschat, S.1
  • 136
    • 84962109823 scopus 로고    scopus 로고
    • Dynamically complex [6+4] and [4+2] cycloadditions in the biosynthesis of spinosyn A
    • Patel A, Chen Z, Yang Z, Gutíerrez O, Liu H-w, et al. (2016). Dynamically complex [6+4] and [4+2] cycloadditions in the biosynthesis of spinosyn A. J. Am. Chem. Soc. 138: 3631-34
    • (2016) J. Am. Chem. Soc , vol.138 , pp. 3631-3634
    • Patel, A.1    Chen, Z.2    Yang, Z.3    Gutíerrez, O.4    Liu, H.-W.5
  • 138
    • 77954811495 scopus 로고    scopus 로고
    • Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction
    • Siegel JB, Zanghellini A, Lovick HM, Kiss G, Lambert AR, et al. (2010). Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction. Science 329: 309-13
    • (2010) Science , vol.329 , pp. 309-313
    • Siegel, J.B.1    Zanghellini, A.2    Lovick, H.M.3    Kiss, G.4    Lambert, A.R.5
  • 139
    • 67549086082 scopus 로고    scopus 로고
    • Understanding the functional roles of amino acid residues in enzyme catalysis
    • Holliday GL, Mitchell JBO, Thornton JM. (2009). Understanding the functional roles of amino acid residues in enzyme catalysis. J. Mol. Biol. 390: 560-77
    • (2009) J. Mol. Biol , vol.390 , pp. 560-577
    • Holliday, G.L.1    Mitchell, J.B.O.2    Thornton, J.M.3
  • 140
    • 80053616941 scopus 로고    scopus 로고
    • Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis
    • Holliday GL, Fischer JD, Mitchell JBO, Thornton JM. (2011). Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis. FEBS J. 278: 3835-45
    • (2011) FEBS J , vol.278 , pp. 3835-3845
    • Holliday, G.L.1    Fischer, J.D.2    Mitchell, J.B.O.3    Thornton, J.M.4
  • 143
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky O, Tawfik DS. (2010). Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79: 471-505
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 144
    • 57049143713 scopus 로고    scopus 로고
    • Promiscuous sulfatase activity and thio-effects in a phosphodiesterase of the alkaline phosphatase superfamily
    • Lassila JK, Herschlag D. (2008). Promiscuous sulfatase activity and thio-effects in a phosphodiesterase of the alkaline phosphatase superfamily. Biochemistry 47: 12853-59
    • (2008) Biochemistry , vol.47 , pp. 12853-12859
    • Lassila, J.K.1    Herschlag, D.2
  • 145
    • 0028896311 scopus 로고
    • A relationship between protein stability and protein function
    • Shoichet BK, Baase WA, Kuroki R, Matthews BW. (1995). A relationship between protein stability and protein function. PNAS 92: 452-56
    • (1995) PNAS , vol.92 , pp. 452-456
    • Shoichet, B.K.1    Baase, W.A.2    Kuroki, R.3    Matthews, B.W.4
  • 146
    • 84879549646 scopus 로고    scopus 로고
    • What makes a protein fold amenable to functional innovation? Fold polarity and stability trade-offs
    • Dellus-Gur E, Toth-Petroczy A, Elias M, Tawfik DS. (2013). What makes a protein fold amenable to functional innovation? Fold polarity and stability trade-offs. J. Mol. Biol. 425: 2609-21
    • (2013) J. Mol. Biol , vol.425 , pp. 2609-2621
    • Dellus-Gur, E.1    Toth-Petroczy, A.2    Elias, M.3    Tawfik, D.S.4
  • 148
    • 80054974028 scopus 로고    scopus 로고
    • A tale of two isomerases: Compact versus extended active sites in ketosteroid isomerase and phosphoglucose isomerase
    • Somarowthu S, Brodkin HR, DAquino JA, Ringe D, Ondrechen MJ, Beuning PJ. (2011). A tale of two isomerases: compact versus extended active sites in ketosteroid isomerase and phosphoglucose isomerase. Biochemistry 50: 4923-35
    • (2011) Biochemistry , vol.50 , pp. 4923-4935
    • Somarowthu, S.1    Brodkin, H.R.2    D'Aquino, J.A.3    Ringe, D.4    Ondrechen, M.J.5    Beuning, P.J.6
  • 149
    • 0001305507 scopus 로고    scopus 로고
    • High-resolution crystal structures of 5-3-ketosteroid isomerase with and without a reaction intermediate analogue
    • Kim SW, Cha SS, Cho HS, Kim JS, Ha NC, et al. (1997). High-resolution crystal structures of 5-3-ketosteroid isomerase with and without a reaction intermediate analogue. Biochemistry 36: 14030-36
    • (1997) Biochemistry , vol.36 , pp. 14030-14036
    • Kim, S.W.1    Cha, S.S.2    Cho, H.S.3    Kim, J.S.4    Ha, N.C.5
  • 150
    • 84940495083 scopus 로고    scopus 로고
    • Response to comments on Extreme electric fields power catalysis in the active site of ketosteroid isomerase
    • Fried SD, Boxer SG. (2015). Response to comments on Extreme electric fields power catalysis in the active site of ketosteroid isomerase. Science 349: 936
    • (2015) Science , vol.349 , pp. 936
    • Fried, S.D.1    Boxer, S.G.2
  • 151
    • 83755181406 scopus 로고    scopus 로고
    • Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase
    • Schwans JP, Sunden F, Gonzalez A, Tsai Y, Herschlag D. (2011). Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase. J. Am. Chem. Soc. 133: 20052-55
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 20052-20055
    • Schwans, J.P.1    Sunden, F.2    Gonzalez, A.3    Tsai, Y.4    Herschlag, D.5
  • 152
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarity
    • Fersht AR. (1974). Catalysis, binding and enzyme-substrate complementarity. Proc. R. Soc. B 187: 397-407
    • (1974) Proc. R. Soc , vol.B187 , pp. 397-407
    • Fersht, A.R.1
  • 153
    • 53849096731 scopus 로고    scopus 로고
    • Testing geometrical discrimination within an enzyme active site: Constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole
    • Sigala PA, Kraut DA, Caaveiro JMM, Pybus B, Ruben EA, et al. (2008). Testing geometrical discrimination within an enzyme active site: constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole. J. Am. Chem. Soc. 130: 13696-708
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 13696-13708
    • Sigala, P.A.1    Kraut, D.A.2    Caaveiro, J.M.M.3    Pybus, B.4    Ruben, E.A.5
  • 154
    • 82455219011 scopus 로고    scopus 로고
    • Flexibility, diversity, and cooperativity: Pillars of enzyme catalysis
    • Hammes GG, Benkovic SJ, Hammes-Schiffer S. (2011). Flexibility, diversity, and cooperativity: pillars of enzyme catalysis. Biochemistry 50: 10422-30
    • (2011) Biochemistry , vol.50 , pp. 10422-10430
    • Hammes, G.G.1    Benkovic, S.J.2    Hammes-Schiffer, S.3
  • 155
    • 84923078953 scopus 로고    scopus 로고
    • Role of dynamics in enzyme catalysis: Substantial versus semantic controversies
    • Kohen A. (2015). Role of dynamics in enzyme catalysis: substantial versus semantic controversies. Acc. Chem. Res. 48: 466-73
    • (2015) Acc. Chem. Res , vol.48 , pp. 466-473
    • Kohen, A.1
  • 156
    • 77951226274 scopus 로고    scopus 로고
    • At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?
    • Kamerlin SCL, Warshel A. (2010). At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins 78: 1339-75
    • (2010) Proteins , vol.78 , pp. 1339-1375
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 157
    • 84971264954 scopus 로고    scopus 로고
    • Defining and quantifying the role of dynamics in enzyme catalysis
    • Warshel A, Bora RP. (2016). Defining and quantifying the role of dynamics in enzyme catalysis. J. Chem. Phys. 144: 180901
    • (2016) J. Chem. Phys , vol.144 , pp. 180901
    • Warshel, A.1    Bora, R.P.2
  • 158
    • 80053641898 scopus 로고    scopus 로고
    • Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase
    • Jha SK, Ji M, Gaffney KJ, Boxer SG. (2011). Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase. PNAS 108: 16612-17
    • (2011) PNAS , vol.108 , pp. 16612-16617
    • Jha, S.K.1    Ji, M.2    Gaffney, K.J.3    Boxer, S.G.4
  • 160
    • 84858758329 scopus 로고    scopus 로고
    • Evidence that a dynamic knockout in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis
    • Loveridge EJ, Behiry EM, Guo J, Allemann RK. (2012). Evidence that a dynamic knockout in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis. Nat. Chem. 4: 292-97
    • (2012) Nat. Chem , vol.4 , pp. 292-297
    • Loveridge, E.J.1    Behiry, E.M.2    Guo, J.3    Allemann, R.K.4
  • 161
    • 84976333816 scopus 로고    scopus 로고
    • Correction to Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase
    • Schwans JP, Sunden F, Gonzalez A, Tsai Y, Herschlag D. (2016). Correction to Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase. J. Am. Chem. Soc. 138: 7801-2
    • (2016) J. Am. Chem. Soc , vol.138 , pp. 7801-7802
    • Schwans, J.P.1    Sunden, F.2    Gonzalez, A.3    Tsai, Y.4    Herschlag, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.