G. H. Reed

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Refrigeration: A Practical Manual for Apprentices

G. H. Reed, 1969 .

Refrigeration : a practical manual for mechanics

G. H. Reed, 1981 .

The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids.

G. H. Reed, P. Babbitt, D. Ringe, 1996, Biochemistry.

Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII--enzyme complex from yeast at 1.9 A resolution.

G. H. Reed, J. Wedekind, I. Rayment, 1995, Biochemistry.

Octahedral Coordination at the High-Affinity Metal Site in Enolase: Crystallographic Analysis of the Mg"-Enzyme Complex from Yeast at 1.9

G. H. Reed, J. Wedekind, I. Rayment, 2001 .

Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution.

G. H. Reed, J. Wedekind, I. Rayment, 1994, Biochemistry.

Structural changes induced by substrates and anions at the active site of creatine kinase. Electron paramagnetic resonance and nuclear magnetic relaxation rate studies of the manganous complexes.

G. H. Reed, M. Cohn, 1972, The Journal of biological chemistry.

Nuclear Magnetic Resonance Investigation of Ligand Exchange Kinetics in the Calcium(II)-EDTA System.

G. H. Reed, R. J. Kula, 1966 .

Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases.

G. H. Reed, P. Frey, 2011, Biochimica et biophysica acta.

EPR spectroscopic and computational characterization of the hydroxyethylidene-thiamine pyrophosphate radical intermediate of pyruvate:ferredoxin oxidoreductase.

G. H. Reed, S. Ragsdale, T. Begley, 2006, Biochemistry.

Characterization of a succinyl-CoA radical-cob(II)alamin spin triplet intermediate in the reaction catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase.

G. H. Reed, R. Banerjee, S. O. Mansoorabadi, 2005, Biochemistry.

The catalytic Mn2+ sites in the enolase-inhibitor complex: crystallography, single-crystal EPR, and DFT calculations.

G. H. Reed, F. Neese, D. Goldfarb, 2007, Journal of the American Chemical Society.

The ubiquity of iron.

G. H. Reed, P. Frey, 2012, ACS chemical biology.

Properties of Intermediates in the Catalytic Cycle of Oxalate Oxidoreductase and Its Suicide Inactivation by Pyruvate

G. H. Reed, S. Ragsdale, Elizabeth Pierce, 2017, Biochemistry.

Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase.

G. H. Reed, P. Frey, K. Tang, 2009, Biochemistry.

Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases.

G. H. Reed, P. Frey, E. Behshad, 2006, Biochemistry.

Metal cofactors of lysine-2,3-aminomutase.

G. H. Reed, P. Frey, R. Petrovich, 1991, The Journal of biological chemistry.

Inhibition of lysine 2,3-aminomutase by the alternative substrate 4-thialysine and characterization of the 4-thialysyl radical intermediate.

G. H. Reed, P. Frey, V. Bandarian, 2001, Archives of biochemistry and biophysics.

Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase.

G. H. Reed, P. Frey, M. Ballinger, 1992, Biochemistry.

Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism.

G. H. Reed, P. Frey, V. Bandarian, 2000, Biochemistry.

Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: a radical centered on the beta-carbon of the alternative substrate, 4-thia-L-lysine.

G. H. Reed, P. Frey, W. Wu, 1995, Biochemistry.

Characterization of an allylic analogue of the 5'-deoxyadenosyl radical: an intermediate in the reaction of lysine 2,3-aminomutase.

G. H. Reed, P. Frey, O. Magnusson, 2001, Biochemistry.

Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy.

G. H. Reed, P. Frey, R. Petrovich, 1992, Biochemistry.

Kinetic and magnetic resonance studies of the interaction of oxalate with pyruvate kinase.

G. H. Reed, S. Morgan, 1974, Biochemistry.

EPR properties of the electron carrier intermediate between the reaction center bacteriochlorophylls and the primary acceptor in Chromatium vinosum

G. H. Reed, P. Dutton, R. Prince, 1976, FEBS letters.

S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance.

G. H. Reed, P. Frey, H. Beinert, 1998, Biochemistry.

Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement.

G. H. Reed, P. Frey, M. Ballinger, 1995, Biochemistry.

Electron paramagnetic resonance spectra of manganese (II)-protein complexes. Manganese (II)-concanavalin A.

G. H. Reed, M. Cohn, 1970, The Journal of biological chemistry.

Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases.

G. H. Reed, S. Ragsdale, S. O. Mansoorabadi, 2012, Biochimica et biophysica acta.

Crystallization and preliminary analysis of enzyme‐substrate complexes of pyruvate kinase from rabbit muscle

G. H. Reed, I. Rayment, K. Schmidt-Bäse, 1991, Proteins.

Magnetic resonance studies of active sites in enzymic complexes.

G. H. Reed, M. Cohn, 1982, Annual review of biochemistry.

Investigations of equilibrium complexes of myoxin subfragment 1 with the manganous ion and adenosine diphosphate using magnetic resonance techniques.

G. H. Reed, C. R. Bagshow, 1976, The Journal of biological chemistry.

Mapping active sites of phosphoryl-transferring enzymes by magnetic resonance methods.

G. H. Reed, M. Cohn, J. Leigh, 1972, Cold Spring Harbor symposia on quantitative biology.

Reverse protonation is the key to general acid-base catalysis in enolase.

G. H. Reed, W. Cleland, P. Sims, 2003, Biochemistry.

Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin.

G. H. Reed, J. Markley, H. Cheng, 1994, Biochemistry.

Magnetic resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinase.

G. H. Reed, N. C. Price, M. Cohn, 1973, Biochemistry.

Reaction of AdoMet with ThiC generates a backbone free radical.

G. H. Reed, D. Downs, R. Poyner, 2009, Biochemistry.

Hydrazine cation radical in the active site of ethanolamine ammonia-lyase: mechanism-based inactivation by hydroxyethylhydrazine.

G. H. Reed, V. Bandarian, 1999, Biochemistry.

Reactions of phosphorothioate compounds catalyzed by adenylosuccinate synthetase. Steady state and pre-steady state kinetic studies.

G. H. Reed, G. D. Markham, 1978, The Journal of biological chemistry.

Electron paramagnetic resonance studies of manganese (II) coordination in the phosphoglucomutase system.

G. H. Reed, W. Ray, 1971, Biochemistry.

Method for the enzymatic synthesis of 2-phospho-D-glycerate from adenosine 5'-triphosphate and D-glycerate via D-glycerate-2-kinase

G. H. Reed, P. Sims, 2005 .

Spectroscopic Evidence for the Participation of an Allylic Analogue of the 5‘-Deoxyadenosyl Radical in the Reaction of Lysine 2,3-Aminomutase

G. H. Reed, P. Frey, O. Magnusson, 1999 .

Substrate activity of synthetic formyl phosphate in the reaction catalyzed by formyltetrahydrofolate synthetase.

G. H. Reed, R. Himes, J. Kofron, 1987, Biochemistry.

Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanism.

G. H. Reed, R. Himes, D. H. Buttlaire, 1976, The Journal of biological chemistry.

Magnetic resonance studies on manganese-nucleotide complexes of phosphoglycerate kinase.

G. H. Reed, W. O'Sullivan, R. Scopes, 1977, Biochemistry.

Application of physical methods to the study of enzymes containing bound manganese: problems and prospects.

G. H. Reed, A. Mildvan, M. Scrutton, 1973, Advances in experimental medicine and biology.

Note on the Distinction between Transverse and Longitudinal Electron Relaxation Times Obtained from Nuclear Relaxation Studies

G. H. Reed, J. Reuben, M. Cohn, 1970 .

Electron Paramagnetic Relaxation and EPR Line Shapes of Manganous Ion Complexes in Aqueous Solutions. Frequency and Ligand Dependence

G. H. Reed, J. Pearson, J. Leigh, 1971 .

An organic radical in the lysine 2,3-aminomutase reaction.

G. H. Reed, P. Frey, M. Ballinger, 1992, Biochemistry.

Characterization of a unique coenzyme B6 radical in the ascarylose biosynthetic pathway [14]

G. H. Reed, Hung‐wen Liu, V. Bandarian, 2000 .

Kinetic characterization of an organic radical in the ascarylose biosynthetic pathway.

G. H. Reed, D. Johnson, D. Ballou, 1996, Biochemistry.

ATP-dependent phosphorylation of α-substituted carboxylic acids catalyzed by pyruvate kinase

G. H. Reed, P. Goodhart, D. Ash, 1984 .

Nuclear Magnetic Resonance Technique for Determining Hydration Numbers

G. H. Reed, D. Rabenstein, R. J. Kula, 1965 .

The stereochemical course of phospho transfer catalyzed by adenylosuccinate synthetase. A reaction pathway via a phosphorylated intermediate with net inversion.

G. H. Reed, F. Rudolph, M. Webb, 1984, The Journal of biological chemistry.

Free radical mechanisms in enzymology.

G. H. Reed, P. Frey, A. Hegeman, 2006, Chemical reviews.

Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine.

G. H. Reed, P. Frey, 2006, Advances in enzymology and related areas of molecular biology.

Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes.

G. H. Reed, T. Yonetani, H. Yamamoto, 1972, The Journal of biological chemistry.

Structure of the bis divalent cation complex with phosphonoacetohydroxamate at the active site of enolase.

G. H. Reed, R. Poyner, 1992, Biochemistry.

Electromagnetic properties of hemoproteins. 3. Electron paramagnetic resonance characteristics of iron (III) and manganese (II) protoporphyrins IX and their apohemoprotein complexes in high spin states.

G. H. Reed, M. Waterman, T. Yonetani, 1970, The Journal of biological chemistry.

EPR of Mn(II) Complexes with Enzymes and Other Proteins

G. H. Reed, G. D. Markham, 1984 .

Analysis of the Cob(II)alamin-5'-deoxy-3',4'-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase.

G. H. Reed, P. Frey, O. Magnusson, 2006, Biochemistry.

The positions of radical intermediates in the active sites of adenosylcobalamin-dependent enzymes.

G. H. Reed, S. O. Mansoorabadi, S. Mansoorabadi, 2003, Current opinion in structural biology.

Analysis of EPR powder pattern lineshapes for Mn(II) including third-order perturbation corrections. Applications to Mn(II) complexes with enzymes

G. H. Reed, G. D. Markham, B. Rao, 1979 .

Nuclear magnetic resonance studies of the aggregation of dihexanoyllecithin and of diheptanolyllecithin in aqueous solutions.

G. H. Reed, A. J. Slotboom, G. H. Haas, 1976, Biochimica et biophysica acta.

Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants.

G. H. Reed, J. Markley, V. Bandarian, 1996, Biochemistry.

Structure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations.

G. H. Reed, D. T. Lodato, 1987, Biochemistry.

Electron nuclear double resonance study of the Mn2+ environs in the oxalate-ATP complex of pyruvate kinase.

G. H. Reed, C. Scholes, R. Poyner, 1993, Biochemistry.

Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase.

G. H. Reed, P. Frey, V. Bandarian, 2000, Biochemistry.

Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: electron paramagnetic resonance studies with oxygen-17-labeled ligands.

G. H. Reed, G. L. Kenyon, T. Leyh, 1985, Biochemistry.

Identification of the six ligands to manganese(II) in transition-state-analogue complexes of creatine kinase: oxygen-17 superhyperfine coupling from selectively labeled ligands.

G. H. Reed, T. Leyh, 1980, Biochemistry.

Conformationally restricted creatine analogues and substrate specificity of rabbit muscle creatine kinase.

G. H. Reed, G. L. Kenyon, T. Leyh, 1980, Biochemistry.

Electron paramagnetic resonance studies of a ras p21-MnIIGDP complex in solution.

G. H. Reed, M. Poe, J. Leigh, 1992, Biochemistry.

Synthesis of oxalyl phosphate and processing of the acyl phosphate by phosphoenolpyruvate-dependent enzymes.

G. H. Reed, J. Kofron, 1990, Archives of biochemistry and biophysics.

Electron paramagnetic resonance studies of the coordination schemes and site selectivities for divalent metal ions in complexes with pyruvate kinase.

G. H. Reed, J. Buchbinder, 1990, Biochemistry.

Vanadyl(IV)-thallium(I)-205,203 superhyperfine coupling in complexes with pyruvate kinase

G. H. Reed, K. A. Lord, 1987 .

Observation of manganese(II)-ligand superhyperfine couplings in complexes with proteins by electron spin-echo spectroscopy.

G. H. Reed, W. Orme-Johnson, R. Lobrutto, 1986, Biochemistry.

Electron paramagnetic resonance studies in frozen aqueous solutions. Elimination of freezing artifacts

G. H. Reed, J. Leigh, 1971 .

Pyruvate carboxylase from chicken liver. Magnetic resonance studies of the effect of substrates and inhibitors on the environment of the bound manganese.

G. H. Reed, M. Scrutton, 1974, The Journal of biological chemistry.

Electron paramagnetic resonance studies of manganese (II)-pyruvate kinase-substrate complexes.

G. H. Reed, M. Cohn, 1973, The Journal of biological chemistry.

Studies of manganous nucleotide complexes with uridine diphosphate-glucose pyrophosphorylase, formyltetrahydrofolate synthetase, and creatine kinase. Mechanism of water proton magnetic relaxation from frequency dependent measurements.

G. H. Reed, M. Cohn, H. Diefenbach, 1972, The Journal of biological chemistry.

Magnetic resonance and kinetic studies of pyruvate, phosphate dikinase. Interaction of oxalate with the phosphorylated form of the enzyme.

G. H. Reed, Y. Milner, G. Michaels, 1975, Biochemistry.

Vanadyl(IV) complexes with pyruvate kinase: activation of the enzyme and electron paramagnetic resonance properties of ternary complexes with the protein.

G. H. Reed, K. A. Lord, 1990, Archives of biochemistry and biophysics.

Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit.

G. H. Reed, P. Sims, S. O. Mansoorabadi, 2006, Journal of molecular biology.

Magnetic resonance studies of three forms of creatine kinase. Comparison of the properties of native, CH-S-blocked, and H2NCOCH-blocked enzymes.

G. H. Reed, G. D. Markham, 1977, The Journal of biological chemistry.

Investigations of anion binding sites in transition state analogue complexes of creatine kinase by infrared spectroscopy.

G. H. Reed, C. Barlow, R. Burns, 1978, The Journal of biological chemistry.

Scalar coupling between 31P and spin-1/2 metal nuclides in 31P NMR of complexes with a ligand containing phosphonate donor groups.

G. H. Reed, J. Bock, 1979, Biochemical and biophysical research communications.

5'-Deoxyadenosine contacts the substrate radical intermediate in the active site of ethanolamine ammonia-lyase: 2H and 13C electron nuclear double resonance studies.

G. H. Reed, O. Magnusson, V. Schramm, 2001, Biochemistry.

Radical mechanisms in adenosylmethionine- and adenosylcobalamin-dependent enzymatic reactions.

G. H. Reed, P. Frey, 2000, Archives of biochemistry and biophysics.

Identification of the substrate radical intermediate derived from ethanolamine during catalysis by ethanolamine ammonia-lyase.

G. H. Reed, G. Bender, R. Poyner, 2008, Biochemistry.

Radical mechanisms in adenosylcobalamin-dependent enzymes.

G. H. Reed, 2004, Current opinion in chemical biology.

Probing interactions from solvent‐exchangeable protons and monovalent cations with the 1,2‐propanediol‐1‐yl radical intermediate in the reaction of dioldehydrase

G. H. Reed, P. Frey, Phillip A. Schwartz, 2007, Protein science : a publication of the Protein Society.

Reaction of adenosylcobalamin-dependent glutamate mutase with 2-thiolglutarate.

G. H. Reed, Chunhua Qiao, E. Marsh, 2006, Biochemistry.

Adenylosuccinate synthetase from Azotobacter vinelandii: purification, properties and steady-state kinetics.

G. H. Reed, G. D. Markham, 1977, Archives of biochemistry and biophysics.

Synergistic inhibition of adenylosuccinate synthetase by nitrate and GDP

G. H. Reed, G. D. Markham, 1975, FEBS letters.

Ethanolamine ammonia-lyase has a "base-on" binding mode for coenzyme B(12).

G. H. Reed, V. Bandarian, J Rétey, 1999, Archives of biochemistry and biophysics.

Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: determination of the number of exchangeable hydrogens in the enzyme-cofactor complex.

G. H. Reed, V. Bandarian, 2000, Biochemistry.

Characterization of a radical intermediate in the lysine 2,3-aminomutase reaction.

G. H. Reed, M. Ballinger, George H. Reed, 1995, Methods in enzymology.

Kinetic characterization of transient free radical intermediates in reaction of lysine 2,3-aminomutase by EPR lineshape analysis.

G. H. Reed, Christopher H. Chang, P. Frey, 2002, Methods in enzymology.

How Active Is Actin? Propagated Conformational Changes in the Actin Filament

G. H. Reed, J. Loscalzo, A. Weber, 1977 .

Fourier Deconvolution Methods for Resolution Enhancement in Continuous-Wave EPR Spectroscopy.

G. H. Reed, R. Poyner, 2015, Methods in enzymology.

The significance of the slow dissociation of divalent metal ions from myosin ‘regulatory’ light chains

G. H. Reed, Clive R. Bagshaw, 1977, FEBS letters.

Adsorption of Methyl Orange and Ethyl Orange on Tailored Silica Gels.

G. H. Reed, L. Rogers, 1965 .

Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.

G. H. Reed, I. Rayment, M. Benning, 1998, Biochemistry.

A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution.

G. H. Reed, J. Wedekind, I. Rayment, 1996, Biochemistry.

Structural and mechanistic studies of enolase.

G. H. Reed, J. Wedekind, I. Rayment, 1996, Current opinion in structural biology.

Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.

G. H. Reed, I. Rayment, M. Benning, 1997, Archives of biochemistry and biophysics.

Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate.

G. H. Reed, I. Rayment, H. Holden, 1994, Biochemistry.

Electron paramagnetic resonance and water proton relaxation rate studies of formyltetrahydrofolate synthetase-manganous ion complexes. Evidence for involvement of substrates in the promotion of a catalytically competent active site.

G. H. Reed, R. Himes, D. H. Buttlaire, 1975, The Journal of biological chemistry.

Equilibrium and water proton relaxation rate enhancement properties of formyltetrahydrofolate synthetase-manganous ion-substrate complexes.

G. H. Reed, R. Himes, D. H. Buttlaire, 1975, The Journal of biological chemistry.

Stereochemical control over manganese(II)-thio versus manganese(II)-oxy coordination in adenosine 5'-O-(1-thiodiphosphate) complexes at the active site of creatine kinase

G. H. Reed, R. Lobrutto, G. Smithers, 1989 .

Coordination of manganous ion at the active site of pyruvate, phosphate dikinase: the complex of oxalate with the phosphorylated enzyme.

G. H. Reed, J. Kofron, D. Ash, 1988, Biochemistry.

Analysis of the electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B(12)-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol.

G. H. Reed, V. Bandarian, 2002, Biochemistry.

Coordination scheme and stereochemical configuration of manganese(II) adenosine 5'-diphosphate at the active site of 3-phosphoglycerate kinase.

G. H. Reed, J. Moore, 1985, Biochemistry.

Analysis of equilibrium data from proton magnetic relaxation rates of water for manganese-nucleotide-kinase ternary complexes.

G. H. Reed, W. O'Sullivan, M. Cohn, 1970, The Journal of biological chemistry.

The Role of S‐Adenosylmethionine as a Poor Man's Adenosylcobalamin in the Reaction of Lysine 2,3‐Aminomutase

G. H. Reed, Christopher H. Chang, P. Frey, 2007 .

Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase.

G. H. Reed, P. Frey, J. Buchbinder, 1993, Biochemistry.

The stereochemical configuration of Mn(II) . ADP at the active site of creatine kinase elucidated by electron paramagnetic resonance with Rp [alpha-17O]ADP and Sp [alpha-17O]ADP.

G. H. Reed, P. Frey, T. Leyh, 1982, The Journal of biological chemistry.

S-adenosylmethionine: a 'poor man's coenzyme B12' in the reaction of lysine 2,3-aminomutase.

G. H. Reed, P. Frey, M. Ballinger, 1998, Biochemical Society transactions.

Lysine 2,3-aminomutase: rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate.

G. H. Reed, P. Frey, C. Chang, 1996, Biochemistry.

Spectroscopic studies of actin-metal-nucleotide complexes.

G. H. Reed, J. Loscalzo, 1976, Biochemistry.

Analysis of powder and single-crystal electron paramagnetic resonance spectra for manganese(II) protoporphyrin IX myoglobin at various microwave frequencies

G. H. Reed, M. Ikeda-Saito, T. Yonetani, 1984 .

Chapter 17 – Manganese: An Overview of Chemical Properties1

G. H. Reed, 1986 .

Nuclear magnetic resonance and infrared spectral studies of structural and kinetic properties of amino polycarboxylate chelates of divalent lead, zinc, cadmium, and mercury in acidic aqueous solutions

G. H. Reed, R. J. Kula, 1971 .

Electron paramagnetic resonance studies of MN(II) complexes with myosin subfragment 1 and oxygen 17-labeled ligands.

G. H. Reed, T. Leyh, D. Trentham, 1982, The Journal of biological chemistry.

The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117.

G. H. Reed, L. Laughlin, 1997, Archives of biochemistry and biophysics.

STRUCTURAL STUDIES OF TRANSITION STATE ANALOG COMPLEXES OF CREATINE KINASE *

G. H. Reed, A. McLaughlin, 1973, Annals of the New York Academy of Sciences.

Pulsed electron paramagnetic resonance experiments identify the paramagnetic intermediates in the pyruvate ferredoxin oxidoreductase catalytic cycle.

G. H. Reed, S. Ragsdale, A. Astashkin, 2006, Journal of the American Chemical Society.

Temperature dependent conformational changes at the active site of pyruvate kinase. A li nuclear magnetic resonance study.

G. H. Reed, F. Kayne, D. Ash, 1978, Archives of biochemistry and biophysics.

Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.

G. H. Reed, R. Poyner, T. M. Larsen, 2002, Archives of biochemistry and biophysics.

An electron paramagnetic resonance study of bovine α-lactalbumin-metal ion complexes

G. H. Reed, L. Berliner, G. Musci, 1986 .

Phospholipase A2 complexes with gadolinium (III) and interaction of the enzyme-metal ion complex with monomeric and micellar alkylphosphorylcholines. Water proton nuclear magnetic relaxation studies.

G. H. Reed, A. J. Slotboom, R. Hershberg, 1976, Biochemistry.

Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme.

G. H. Reed, W. Cleland, R. Poyner, 2001, Biochemistry.

Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants.

G. H. Reed, R. Poyner, G. Sowa, 1996, Biochemistry.

Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase.

G. H. Reed, P. Frey, K. Tang, 2009, Biochemistry.

Solution electron paramagnetic resonance spectra of hemoproteins at room temperature.

G. H. Reed, J. Leigh, T. Asakura, 1972, Biochemistry.

Conformational change and cooperativity in actin filaments free of tropomyosin.

G. H. Reed, J. Loscalzo, A. Weber, 1975, Proceedings of the National Academy of Sciences of the United States of America.

Interaction of Mn2+ and MnATP2- with the allosteric sites of AMP nucleosidase.

G. H. Reed, V. Schramm, 1980, The Journal of biological chemistry.

Electron paramagnetic resonance measurements of the hydration of Mn(II) in ternary complexes with GDP and ras p21 proteins.

G. H. Reed, M. Poe, G. Smithers, 1990, Archives of biochemistry and biophysics.