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Raman Spectroscopic Studies Of The Structures, Energetics, And Bond Distortions Of Substrates Bound To Enzymes.
H. Deng, R. Callender
Published 1999 · Chemistry, Medicine
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THEORETICAL ESTIMATION OF THE DIELECTRIC PROPERTIES OF AN ENZYME ACTIVE SITE
Younghee Kim (1997)
Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
J. Bolin (1982)
MOLECULAR STRUCTURE OF S-ETHYL THIOACRYLATE : COMBINED VIBRATIONAL SPECTROSCOPIC AND AB INITIO SCF-MO STUDY
P. Tonge (1997)
Internal chemical bonding in solutions of simple phosphates and vanadates.
W. Ray (1993)
Raman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase
H. Deng (1992)
Tyrosine hydrogen-bonding and environmental effects in proteins probed by ultraviolet resonance Raman spectroscopy.
P. G. Hildebrandt (1988)
Spectral and calorimetric studies of hydrogen bonding with pyrrole
R. S. Drago (1970)
Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH)+: a possible model for enzymatic phosphoryl transfer.
D. Herschlag (1990)
An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase.
A. Clarke (1988)
The lactate dehydrogenase catalyzed pyruvate adduct reaction: simultaneous general acid-base catalysis involving an enzyme and an external catalyst.
J. Burgner (1984)
Elucidation of the solution structure of the Escherichia coli aspartate aminotransferase-.alpha.-methyl-L-aspartate complex by isotope-edited Raman difference spectroscopy
H. Deng (1993)
A vibrational analysis of the catalytically important C4-H bonds of NADH bound to lactate or malate dehydrogenase: ground-state effects.
H. Deng (1992)
The binding of amide substrate analogues to phospholipase A2. Studies by 13C-nuclear-magnetic-resonance and infrared spectroscopy.
P. K. Slaich (1992)
Raman spectroscopic studies of NAD coenzymes bound to malate dehydrogenases by difference techniques.
H. Deng (1991)
pH-dependent conformational changes in Escherichia coli dihydrofolate reductase revealed by Raman difference spectroscopy.
Y. Chen (1997)
Correlation of the molecular electrostatic potential surface of an enzymatic transition state with novel transition-state inhibitors.
B. Horenstein (1993)
Hydrogen-bonding in enzyme catalysis. Fourier-transform infrared detection of ground-state electronic strain in acyl-chymotrypsins and analysis of the kinetic consequences.
A. White (1990)
An isotope edited classical Raman difference spectroscopic study of the interactions of guanine nucleotides with elongation factor Tu and H-ras p21.
D. Manor (1991)
Infrared and Raman studies of hydrogen bonded complexes involving acetone, acetophenone and benzophenone—I. Thermodynamic constants and frequency shifts of the νOH and νCO stretching vibrations
R. Thijs (1984)
Acceleration of the NAD cyanide adduct reaction by lactate dehydrogenase: the equilibrium binding effect as a measure of the activation of bound NAD.
J. Burgner (1984)
A new infrared electronic transition of the oxidized primary electron donor in bacterial reaction centers: a way to assess resonance interactions between the bacteriochlorophylls.
J. Breton (1992)
Resonance Raman and Fourier transform infrared spectroscopic studies of the acyl carbonyl group in [3-(5-methyl-2-thienyl)acryloyl]chymotrypsin: evidence for artifacts in the spectra obtained by both techniques.
P. Tonge (1991)
Characterization of vanadate-based transition-state-analogue complexes of phosphoglucomutase by spectral and NMR techniques.
W. Ray (1990)
Trypanosomal nucleoside hydrolase. Resonance Raman spectroscopy of a transition-state inhibitor complex.
H. Deng (1996)
Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state.
C. Bystroff (1990)
Isotope effects on binding of NAD+ to lactate dehydrogenase.
R. Lareau (1989)
Raman Difference Spectroscopy with the Rotating Cell
W. Kiefer (1973)
On the origin of the lactate dehydrogenase induced rate effect.
J. Burgner (1984)
Studies in physical and theoretical chemistry : Vol. 55, semiconductor electrodes. H.O. Finklea (Editor). Elsevier, Amsterdam, 1988, xxii + 520 pp., Dfl.340.00, US$179.00
P. Bartlett (1988)
Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms.
W. Maentele (1993)
Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules.
R. Callender (1994)
FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model
K. Rothschild (1992)
Comparison of vibrational frequencies of critical bonds in ground-state complexes and in a vanadate-based transition-state analog complex of muscle phosphoglucomutase. Mechanistic implications.
H. Deng (1993)
Raman difference spectroscopy in measurements of molecules and molecular groups inside proteins
K. T. Yue (1989)
Biological applications of Raman spectroscopy
T. Spiro (1987)
Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy.
J. M. Goldberg (1993)
Infrared and Raman study of the interaction between methyl acetate and phenol derivatives
L. Vanderheyden (1983)
Biochemical Applications of Raman and Resonance Raman Spectroscopies
P. Carey (1982)
Mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrate.
J. F. Morrison (1988)
Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopy.
J. Baenziger (1992)
The Handbook of Infrared and Raman Characteristic Frequencies of Organic Molecules
D. Lin-Vien (1991)
Structure of the Dimeric Ethylene Glycol-Vanadate Complex and Other 1,2-Diol-Vanadate Complexes in Aqueous Solution: Vanadate-Derived Transition-State Analog Complexes of Phosphotransferases
W. Ray (1995)
UNLOCKING THE SECRETS OF ENZYME POWER USING RAMAN SPECTROSCOPY
P. Carey (1995)
Computational studies on pterins and speculations on the mechanism of action of dihydrofolate reductase.
T. Uchimaru (1989)
Source of catalysis in the lactate dehydrogenase system. Ground-state interactions in the enzyme-substrate complex.
H. Deng (1994)
The oxyvanadium constellation in transition-state-analogue complexes of phosphoglucomutase and ribonuclease. Structural deductions from electron-transfer spectra.
W. Ray (1990)
Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis
A. R. Clarke (1986)
Thermodynamic studies of binary and ternary complexes of pig heart lactate dehydrogenase.
F. Schmid (1976)
Determination of vanadium-oxygen bond distances and bond orders by Raman spectroscopy
F. D. Hardcastle (1991)
Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications.
Y. Chen (1994)
Electronic nature of the transition state for nucleoside hydrolase. A blueprint for inhibitor design.
B. Horenstein (1993)
Analysis and elimination of protein perturbation in infrared difference spectra of acyl-chymotrypsin ester carbonyl groups by using 13C isotopic substitution.
A. White (1992)
Lactic dehydrogenase. V. Inhibition by oxamate and by oxalate.
W. B. Novoa (1959)
Infrared studies of amine complexes. IV. The N-H-O hydrogen bond in aromatic amine complexes of ethers ketones, esters, and amides
J. H. Lady (1967)
Hydrogen bonding and reaction specificity in lactate dehydrogenase studied by Raman spectroscopy
H. Deng (1989)
4 Lactate Dehydrogenase
J. Holbrook (1975)
Relation between O-H stretching frequency and hydrogen bond energy: re-examination of the Badger-Bauer rule
C. Rao (1975)
Biochemical applications of Raman and resonance Raman spectroscopy : by P.R. Carey, Academic Press, 1982. £22.60/US$34.00 (xi + 262 pages) ISBN 0 12 159650 8
H. Ishida (1984)
Correlation between interaction energy and shift of the carbonyl stretching frequency
Z. Latajka (1990)
Raman difference spectroscopy as a probe of biological molecules
D. Rousseau (1981)
Transition-state analysis of nucleoside hydrolase from Crithidia fasciculata.
B. Horenstein (1991)
Combination of theoretical ab initio and experimental information to obtain reliable harmonic force constants. Scaled quantum mechanical (QM) force fields for glyoxal, acrolein, butadiene, formaldehyde, and ethylene
P. Pulay (1983)
Empirical parameters for calculating cation–oxygen bond valences
I. Brown (1976)
Classical Raman spectroscopic studies of NADH and NAD+ bound to liver alcohol dehydrogenase by difference techniques.
D. Chen (1987)
Fourier transform infrared techniques for probing membrane protein structure.
M. Braiman (1988)
This paper is referenced by
Verhinderung hitze- und säureinduzierter Proteindenaturierung durch einige niedrig- und hochmolekulare protektive Substanzen, gemessen an der Beeinträchtigung des aktiven Zentrums des Lactatdehydrogenase-Modellenzyms
Stephanie Lina Meeß (2006)
Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers.
Alasdair F. Bell (2002)
Whatvibrations tell us aboutproteins
A. Barth (2002)
Mapping Interactions between the Ca2+-ATPase and Its Substrate ATP with Infrared Spectroscopy*
Man Liu (2003)
Enzyme active site interactions by Raman/FTIR, NMR, and ab initio calculations.
H. Deng (2013)
Tracking Reactive Water and Hydrogen-Bonding Networks in Photosynthetic Oxygen Evolution.
B. Barry (2017)
Correlations between the structure and the vibrational spectrum of the phosphate group. Implications for the analysis of an important functional group in phosphoproteins
P. Pettersson (2020)
The Acceptor Quinones of Purple Photosynthetic Bacteria— Structure and Spectroscopy
C. A. Wraight (2009)
Production of chromium-chelating peptides after hydrolysis of silk fibroin protein with elastase
Hu Changlia (2011)
Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.
I. Lopez-Peña (2015)
Conformational Dynamics Measured with Proteins in Solution
J. Fitter (2006)
Multidisciplinary Experimental Approaches to Characterizing Biomolecular Dynamics
F. Romesberg (2003)
Calcium and the Hydrogen-Bonded Water Network in the Photosynthetic Oxygen-Evolving Complex.
Brandon C. Polander (2013)
Solution structure of ligands involved in purine salvage pathway.
Vishakha Karnawat (2015)
Quantifying energetic contributions to ground state destabilization.
V. Anderson (2005)
Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin
Saqer M. Darwish (2017)
Raman crystallography and other biochemical applications of Raman microscopy.
P. Carey (2006)
Conformational properties and aggregation of homo‐oligomeric β3(R)‐valine peptides in organic solvents
B. Vasantha (2017)
Quantifying bond distortions in transient enzyme species by a combination of density functional theory calculations and time-resolved infrared difference spectroscopy. Implications for the mechanism of dephosphorylation of the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a).
A. Barth (2015)
Raman Scattering and Other Multi-photon Processes
W. Parson (2015)
Raman Crystallographic Studies of Inhibitor Reactions in Class A β-Lactamases
Matthew D. Kalp (2009)
What vibrations tell us about proteins.
A. Barth (2002)
Real-time Raman microspectroscopy scanning of the single live sperm bound to human zona pellucida.
F. Liu (2013)
Two sides of the same coin : How enzymes distort substrates and vice versa. An infrared spectroscopic view on pyruvate kinase and Ca2+-ATPase
A. Barth (2016)
Exquisite Modulation of the Active Site of Methanocaldococcus jannaschii Adenylosuccinate Synthetase in Forward Reaction Complexes.
Vishakha Karnawat (2016)
Optical Spectroscopy in Photosynthetic Antennas
W. Parson (2003)
Terahertz mechanical vibrations in lysozyme: Raman spectroscopy vs modal analysis
A. Carpinteri (2017)
Infrared spectroscopy of proteins.
A. Barth (2007)
Fourier transform infrared (FTIR) spectroscopy
C. Berthomieu (2009)
An extremely low-frequency magnetic field can affect CREB protein conformation which may have a role in neuronal activities including memory
Saqer M. Darwish (2020)