-
1
-
-
0032475836
-
The low barrier hydrogen bond in enzymatic catalysis
-
Cleland WW, Frey PA, Gerlt JA. The low barrier hydrogen bond in enzymatic catalysis. J Biol Chem 1998;273:25529-25532.
-
(1998)
J Biol Chem
, vol.273
, pp. 25529-25532
-
-
Cleland, W.W.1
Frey, P.A.2
Gerlt, J.A.3
-
2
-
-
0032872140
-
NMR methods for the detection and study of low-barrier hydrogen bonds on enzymes
-
in press
-
Mildvan AS, Harris TK, Abeygunawardana C. NMR methods for the detection and study of low-barrier hydrogen bonds on enzymes. Methods Enzymol 1999;308; in press.
-
(1999)
Methods Enzymol
, pp. 308
-
-
Mildvan, A.S.1
Harris, T.K.2
Abeygunawardana, C.3
-
5
-
-
33746007568
-
Lengthening of the covalent O - H bond in O - H····O hydrogen bonds re-examined from low-temperature neutron diffraction data of organic compounds
-
Steiner Th, Saenger W. Lengthening of the covalent O - H bond in O - H····O hydrogen bonds re-examined from low-temperature neutron diffraction data of organic compounds. Acta Crystallogr 1994;B50:348-357.
-
(1994)
Acta Crystallogr
, vol.B50
, pp. 348-357
-
-
Steiner, Th.1
Saenger, W.2
-
7
-
-
0029815959
-
Calculation of the potential energy surface for intermolecular amide hydrogen bonds using semiempirical and ab initio methods
-
Adalsteinsson H, Maulitz AH, Bruice TC. Calculation of the potential energy surface for intermolecular amide hydrogen bonds using semiempirical and ab initio methods. J Am Chem Soc 1996;119:7689-7693.
-
(1996)
J Am Chem Soc
, vol.119
, pp. 7689-7693
-
-
Adalsteinsson, H.1
Maulitz, A.H.2
Bruice, T.C.3
-
8
-
-
84962476487
-
Characterization of low-barrier hydrogen bonds. 7. Relationship between strength and geometry of short-strong hydrogen bonds. The formic acid-formate anion model system. An ab initio and DFT investigation
-
Smallwood CJ, McAllister MA. Characterization of low-barrier hydrogen bonds. 7. Relationship between strength and geometry of short-strong hydrogen bonds. The formic acid-formate anion model system. An ab initio and DFT investigation. J Am Chem Soc 1997;119:11277-11281.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 11277-11281
-
-
Smallwood, C.J.1
McAllister, M.A.2
-
9
-
-
0029905014
-
The change in hydrogen bond strength accompanying charge rearrangement: Implications for enzymatic catalysis
-
Shan S, Herschlag D. The change in hydrogen bond strength accompanying charge rearrangement: implications for enzymatic catalysis. Proc Natl Acad Sci USA 1996;93:14474-14479.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 14474-14479
-
-
Shan, S.1
Herschlag, D.2
-
11
-
-
0004246255
-
-
Menlo Park, CA: Benjamin/ Cummings
-
Watson JD, Hopkins NH, Roberts JW, Steitz JA, Weiner AM. Molecular biology of the gene. Menlo Park, CA: Benjamin/ Cummings, 1987. p 132-138.
-
(1987)
Molecular Biology of the Gene
, pp. 132-138
-
-
Watson, J.D.1
Hopkins, N.H.2
Roberts, J.W.3
Steitz, J.A.4
Weiner, A.M.5
-
12
-
-
0029040169
-
On low-barrier hydrogen bonds and enzyme catalysis
-
Warshel A, Papazyan A, Kollman PA. On low-barrier hydrogen bonds and enzyme catalysis. Science 1995;269:102-104.
-
(1995)
Science
, vol.269
, pp. 102-104
-
-
Warshel, A.1
Papazyan, A.2
Kollman, P.A.3
-
13
-
-
0030462453
-
Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds
-
Warshel A., Papazyan A. Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds. Proc Natl Acad Sci USA 1996;93:13665-13670.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 13665-13670
-
-
Warshel, A.1
Papazyan, A.2
-
14
-
-
0030090490
-
Short strong hydrogen bonds: Can they explain enzymic catalysis?
-
Guthrie JP. Short strong hydrogen bonds: can they explain enzymic catalysis? Chem Biol 1996;3:163-170.
-
(1996)
Chem Biol
, vol.3
, pp. 163-170
-
-
Guthrie, J.P.1
-
15
-
-
0028854341
-
The nonexistence of specially stabilized hydrogen bonds in enzymes
-
Scheiner S, Kar T. The nonexistence of specially stabilized hydrogen bonds in enzymes. J Am Chem Soc 1995;117:6970-6975.
-
(1995)
J Am Chem Soc
, vol.117
, pp. 6970-6975
-
-
Scheiner, S.1
Kar, T.2
-
16
-
-
0028030684
-
Low-barrier hydrogen bonds and enzymatic catalysis
-
Cleland WW, Kreevoy MM. Low-barrier hydrogen bonds and enzymatic catalysis. Science 1994;264:1887-1890.
-
(1994)
Science
, vol.264
, pp. 1887-1890
-
-
Cleland, W.W.1
Kreevoy, M.M.2
-
17
-
-
0016148924
-
High-resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" system
-
Robillard G, Shulman RG. High-resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" system. J Mol Biol 1972;71:519-540.
-
(1972)
J Mol Biol
, vol.71
, pp. 519-540
-
-
Robillard, G.1
Shulman, R.G.2
-
19
-
-
0028040716
-
A low-barrier hydrogen bond in the catalytic triad of serine proteases
-
Frey PA, Whitt SA, Tobin JB. A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science 1994;264:1927-1930.
-
(1994)
Science
, vol.264
, pp. 1927-1930
-
-
Frey, P.A.1
Whitt, S.A.2
Tobin, J.B.3
-
20
-
-
0030937806
-
A new concept for the mechanism of action of chymotrypsin: The role of the low-barrier hydrogen bond
-
Cassidy CS, Lin J, Frey PA. A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond. Biochemistry 1997;36:4576-4584.
-
(1997)
Biochemistry
, vol.36
, pp. 4576-4584
-
-
Cassidy, C.S.1
Lin, J.2
Frey, P.A.3
-
21
-
-
0018068795
-
Zymogen activation in serine proteases: Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and α-chymotrypsin
-
Markley J, Ibanez IB. Zymogen activation in serine proteases: proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and α-chymotrypsin. Biochemistry 1978;17:4637-4640.
-
(1978)
Biochemistry
, vol.17
, pp. 4637-4640
-
-
Markley, J.1
Ibanez, I.B.2
-
22
-
-
0023463943
-
Complex of α-chymotrypsin and N-acetyl-L-leucyl-L-phenylalanyltrifluoromethyl ketone: Structural studies with NMR spectroscopy
-
Liang T-C, Abeles RH. Complex of α-chymotrypsin and N-acetyl-L-leucyl-L-phenylalanyltrifluoromethyl ketone: structural studies with NMR spectroscopy. Biochemistry 1987;26:7603-7608.
-
(1987)
Biochemistry
, vol.26
, pp. 7603-7608
-
-
Liang, T.-C.1
Abeles, R.H.2
-
23
-
-
0029758171
-
Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: Bovine chymotrypsinogen A
-
Markley JL, Westler WM. Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: bovine chymotrypsinogen A. Biochemistry 1996;35: 11092-11097.
-
(1996)
Biochemistry
, vol.35
, pp. 11092-11097
-
-
Markley, J.L.1
Westler, W.M.2
-
24
-
-
0032438194
-
Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin
-
Lin J, Westler WM, Cleland WW, Markley JL, Frey PA. Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin. Proc Natl Acad Sci USA 1998;95: 14664-14668.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 14664-14668
-
-
Lin, J.1
Westler, W.M.2
Cleland, W.W.3
Markley, J.L.4
Frey, P.A.5
-
25
-
-
0025952945
-
NMR observation of exchangeable protons of pyridoxal phosphate and histidine residues in cytosolic aspartate aminotransferase
-
Kintanar A, Metzler CM, Metzler DE, Scott RD. NMR observation of exchangeable protons of pyridoxal phosphate and histidine residues in cytosolic aspartate aminotransferase. J Biol Chem 1991;266:17222-17229.
-
(1991)
J Biol Chem
, vol.266
, pp. 17222-17229
-
-
Kintanar, A.1
Metzler, C.M.2
Metzler, D.E.3
Scott, R.D.4
-
29
-
-
0030734269
-
NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase
-
Harris TK, Abeygunawardana C, Mildvan AS. NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase. Biochemistry 1997;36:14661-14675.
-
(1997)
Biochemistry
, vol.36
, pp. 14661-14675
-
-
Harris, T.K.1
Abeygunawardana, C.2
Mildvan, A.S.3
-
30
-
-
0002623288
-
Proton chemical shift measurements in biological solids
-
Sussex, UK: Wiley
-
McDermott A, Ridenour CF. Proton chemical shift measurements in biological solids. In: Encyclopedia of NMR. Sussex, UK: Wiley, 1996:3820-3825.
-
Encyclopedia of NMR
, vol.1996
, pp. 3820-3825
-
-
McDermott, A.1
Ridenour, C.F.2
-
32
-
-
0020346954
-
Solvent isotope effects on enzyme systems
-
Schowen KB, Schowen RL. Solvent isotope effects on enzyme systems. Methods Enzymol 1982;87:551-606.
-
(1982)
Methods Enzymol
, vol.87
, pp. 551-606
-
-
Schowen, K.B.1
Schowen, R.L.2
-
33
-
-
0001467975
-
The exposition of isotope effects on rates and equilibria
-
Kreevoy MM. The exposition of isotope effects on rates and equilibria. J Chem Educ 1964;41:636-638.
-
(1964)
J Chem Educ
, vol.41
, pp. 636-638
-
-
Kreevoy, M.M.1
-
34
-
-
0027982960
-
Hydrogen bonding in proteins as studied by amide hydrogen D/H fractionation factors: Application to staphylococcal nuclease
-
Loh SN, Markley JL. Hydrogen bonding in proteins as studied by amide hydrogen D/H fractionation factors: application to staphylococcal nuclease. Biochemistry 1994;33:1029-1036.
-
(1994)
Biochemistry
, vol.33
, pp. 1029-1036
-
-
Loh, S.N.1
Markley, J.L.2
-
35
-
-
0030469181
-
15N labeled human ubiquitin by triple resonance NMR
-
15N labeled human ubiquitin by triple resonance NMR. J Am Chem Soc 1996;118:12864-12865.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 12864-12865
-
-
LiWang, A.C.1
Bax, A.2
-
36
-
-
0031182921
-
Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings
-
LiWang AC, Bax A. Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings. J Magn Reson 1997;127:54-64.
-
(1997)
J Magn Reson
, vol.127
, pp. 54-64
-
-
LiWang, A.C.1
Bax, A.2
-
37
-
-
0025882959
-
Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: An analogue of the intermediate on the reaction pathway
-
Davenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D. Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway. Biochemistry 1991;30:5821-5826.
-
(1991)
Biochemistry
, vol.30
, pp. 5821-5826
-
-
Davenport, R.C.1
Bash, P.A.2
Seaton, B.A.3
Karplus, M.4
Petsko, G.A.5
Ringe, D.6
-
38
-
-
0024282745
-
Triosephosphate isomerase: Removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism
-
Nickbarg EB, Davenport RC, Petsko GA, Knowles JR. Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. Biochemistry 1988;27:5948-5960.
-
(1988)
Biochemistry
, vol.27
, pp. 5948-5960
-
-
Nickbarg, E.B.1
Davenport, R.C.2
Petsko, G.A.3
Knowles, J.R.4
-
39
-
-
0032564378
-
Proton transfer in the mechanism of triosephosphate isomerase
-
Harris TK, Cole RN, Comer FI, Mildvan AS. Proton transfer in the mechanism of triosephosphate isomerase. Biochemistry 1998;37: 16828-16838.
-
(1998)
Biochemistry
, vol.37
, pp. 16828-16838
-
-
Harris, T.K.1
Cole, R.N.2
Comer, F.I.3
Mildvan, A.S.4
-
42
-
-
0026356563
-
5-3-ketosteroid isomerase by kinetic deuterium isotope effects
-
5-3-ketosteroid isomerase by kinetic deuterium isotope effects. Biochemistry 1991;30:10858-10865.
-
(1991)
Biochemistry
, vol.30
, pp. 10858-10865
-
-
Xue, L.1
Talalay, P.2
Mildvan, A.S.3
-
43
-
-
0001305507
-
5-3-ketosteroid isomerase with and without a reaction intermediate analogue
-
5-3-ketosteroid isomerase with and without a reaction intermediate analogue. Biochemistry 1997;36:14030-14036.
-
(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
Cho, M.-J.6
Joo, S.7
Kim, K.K.8
Choi, K.Y.9
Oh, B.-H.10
-
45
-
-
0030955066
-
5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids
-
5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids. Biochemistry 1997;36:3458-3472.
-
(1997)
Biochemistry
, vol.36
, pp. 3458-3472
-
-
Zhao, Q.1
Abeygunawardana, C.2
Mildvan, A.S.3
-
46
-
-
0032578355
-
The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin
-
Kuhn P, Knapp M, Soltis SM, Granshaw G, Thoene M, Bott R. The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin. Biochemistry 1998;37:13446-13452.
-
(1998)
Biochemistry
, vol.37
, pp. 13446-13452
-
-
Kuhn, P.1
Knapp, M.2
Soltis, S.M.3
Granshaw, G.4
Thoene, M.5
Bott, R.6
-
47
-
-
0024280501
-
Dissecting the catalytic triad of a serine protease
-
Carter P, Wells J. Dissecting the catalytic triad of a serine protease. Nature 1988;332:564-568.
-
(1988)
Nature
, vol.332
, pp. 564-568
-
-
Carter, P.1
Wells, J.2
-
48
-
-
0021930156
-
Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8-Å resolution
-
Wang D, Bode W, Huber R J. Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8-Å resolution. J Mol Biol 1985;185:595-624.
-
(1985)
J Mol Biol
, vol.185
, pp. 595-624
-
-
Wang, D.1
Bode, W.2
Huber, R.J.3
-
49
-
-
0033583716
-
Distinguished hydrogen bonding to active-site histidine in peptidyl boronic acid inhibitor complexes of chymotrypsin and subtilisin: Proton magnetic resonance assignments and H/D fractionation
-
in press
-
Bao D, Kettner C, Huskey WP, Jordan F. Distinguished hydrogen bonding to active-site histidine in peptidyl boronic acid inhibitor complexes of chymotrypsin and subtilisin: proton magnetic resonance assignments and H/D fractionation. J Am Chem Soc 1999; in press.
-
(1999)
J Am Chem Soc
-
-
Bao, D.1
Kettner, C.2
Huskey, W.P.3
Jordan, F.4
-
50
-
-
0021809359
-
Structure of α-chymotrypsin refined at 1.68-Å resolution
-
Tsukada H, Blow DM. Structure of α-chymotrypsin refined at 1.68-Å resolution. J Mol Biol 1985;184:703-711.
-
(1985)
J Mol Biol
, vol.184
, pp. 703-711
-
-
Tsukada, H.1
Blow, D.M.2
-
51
-
-
0023645043
-
Structure of a tetrahedral transition state complex of α-chymotrypsin dimer at 1.8-Å resolution
-
Tulinsky A, Blevins RA. Structure of a tetrahedral transition state complex of α-chymotrypsin dimer at 1.8-Å resolution. J Biol Chem 1987;262:7737-7743.
-
(1987)
J Biol Chem
, vol.262
, pp. 7737-7743
-
-
Tulinsky, A.1
Blevins, R.A.2
-
52
-
-
0025002985
-
Structure of chymotrypsintrifluoromethyl ketone inhibitor complexes: Comparison of slowly and rapidly equilibrating inhibitors
-
Brady K, Wei A, Ringe D, Abeles RH. Structure of chymotrypsintrifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Biochemistry 1990;29:7600-7607.
-
(1990)
Biochemistry
, vol.29
, pp. 7600-7607
-
-
Brady, K.1
Wei, A.2
Ringe, D.3
Abeles, R.H.4
-
53
-
-
0032512422
-
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: Crystal structures of γ-chymotrypsin and subtilisin carlsberg complexes
-
Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF. Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of γ-chymotrypsin and subtilisin carlsberg complexes. Biochemistry 1998; 37:451-462.
-
(1998)
Biochemistry
, vol.37
, pp. 451-462
-
-
Stoll, V.S.1
Eger, B.T.2
Hynes, R.C.3
Martichonok, V.4
Jones, J.B.5
Pai, E.F.6
-
54
-
-
0023705796
-
Triosephosphate isomerase: Energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli
-
Nickbarg EB, Knowles JR. Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli. 1988;Biochemistry 27:5939-5947.
-
(1988)
Biochemistry
, vol.27
, pp. 5939-5947
-
-
Nickbarg, E.B.1
Knowles, J.R.2
|