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Richard V. Wolfenden - Publications

Affiliations: 
Biochemistry University of North Carolina, Chapel Hill, Chapel Hill, NC 
Area:
Kinetics of Enzymatic Reactions
Website:
http://www.med.unc.edu/biochem/wolfenden
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146 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Lewis CA, Wolfenden R. Ether Hydrolysis, Ether Thiolysis and the Catalytic Power of Etherases in the Disassembly of Lignin. Biochemistry. PMID 31657902 DOI: 10.1021/Acs.Biochem.9B00698  0.472
2019 Carter C, Wolfenden R, Caplow M, Lentz B, Pielak G, Watenpaugh K, Hu H, Puett D. Jan Hermans (1933-2018): Red-blooded biophysicists study hemoglobin. Proteins. 87: 171-173. PMID 30779407 DOI: 10.1002/Prot.25659  0.733
2018 Lewis CA, Wolfenden R. Sulfonium Ion Condensation: the Burden Borne by SAM Synthetase. Biochemistry. PMID 29787240 DOI: 10.1021/Acs.Biochem.8B00477  0.335
2017 Lewis CA, Shen L, Yang W, Wolfenden R. Three pyrimidine decarboxylations in the absence of a catalyst. Biochemistry. PMID 28225618 DOI: 10.1021/Acs.Biochem.7B00055  0.377
2016 Lewis CA, Crayle J, Zhou S, Swanstrom R, Wolfenden R. Cytosine deamination and the precipitous decline of spontaneous mutation during Earth's history. Proceedings of the National Academy of Sciences of the United States of America. PMID 27382162 DOI: 10.1073/Pnas.1607580113  0.325
2015 Wolfenden R, Lewis CA, Yuan Y, Carter CW. Temperature dependence of amino acid hydrophobicities. Proceedings of the National Academy of Sciences of the United States of America. 112: 7484-8. PMID 26034278 DOI: 10.1073/Pnas.1507565112  0.307
2014 Wolfenden R. Massive thermal acceleration of the emergence of primordial chemistry, the incidence of spontaneous mutation, and the evolution of enzymes. Journal of Biological Chemistry. 289: 30198-30204. PMID 25210030 DOI: 10.1074/Jbc.R114.567081  0.365
2014 Wolfenden R. Primordial chemistry and enzyme evolution in a hot environment Cellular and Molecular Life Sciences. 71: 2909-2915. PMID 24623557 DOI: 10.1007/S00018-014-1587-2  0.361
2014 Lewis CA, Wolfenden R. The nonenzymatic decomposition of guanidines and amidines. Journal of the American Chemical Society. 136: 130-6. PMID 24359273 DOI: 10.1021/Ja411927K  0.455
2013 Lohman DC, Edwards DR, Wolfenden R. Catalysis by desolvation: the catalytic prowess of SAM-dependent halide-alkylating enzymes. Journal of the American Chemical Society. 135: 14473-5. PMID 24041082 DOI: 10.1021/Ja406381B  0.434
2013 Zhou X, Chou TF, Aubol BE, Park CJ, Wolfenden R, Adams J, Wagner CR. Kinetic mechanism of human histidine triad nucleotide binding protein 1. Biochemistry. 52: 3588-600. PMID 23614568 DOI: 10.1021/Bi301616C  0.409
2012 Schroeder GK, Zhou L, Snider MJ, Chen X, Wolfenden R. Flight of a cytidine deaminase complex with an imperfect transition state analogue inhibitor: mass spectrometric evidence for the presence of a trapped water molecule. Biochemistry. 51: 6476-86. PMID 22775299 DOI: 10.1021/Bi300516U  0.79
2012 Edwards DR, Wolfenden R. Proton-in-flight mechanism for the spontaneous hydrolysis of N-methyl O-phenyl sulfamate: Implications for the design of steroid sulfatase inhibitors Journal of Organic Chemistry. 77: 4450-4453. PMID 22486328 DOI: 10.1021/Jo300386U  0.404
2012 Lohman DC, Wolfenden R, Edwards DR. Hydrolysis of N-alkyl sulfamates and the catalytic efficiency of an S-N cleaving sulfamidase. The Journal of Organic Chemistry. 77: 2907-10. PMID 22352783 DOI: 10.1021/Jo300198W  0.385
2012 Edwards DR, Lohman DC, Wolfenden R. Catalytic proficiency: the extreme case of S-O cleaving sulfatases. Journal of the American Chemical Society. 134: 525-31. PMID 22087808 DOI: 10.1021/Ja208827Q  0.384
2011 Wolfenden R, Yuan Y. The "neutral" hydrolysis of simple carboxylic esters in water and the rate enhancements produced by acetylcholinesterase and other carboxylic acid esterases Journal of the American Chemical Society. 133: 13821-13823. PMID 21793525 DOI: 10.1021/Ja204116A  0.424
2011 Lewis CA, Wolfenden R. Amide bonds to the nitrogen atoms of cysteine and serine as "weak points" in the backbones of proteins. Biochemistry. 50: 7259-64. PMID 21755938 DOI: 10.1021/Bi200813S  0.373
2011 Wolfenden R. Benchmark reaction rates, the stability of biological molecules in water, and the evolution of catalytic power in enzymes Annual Review of Biochemistry. 80: 645-667. PMID 21495848 DOI: 10.1146/Annurev-Biochem-060409-093051  0.443
2011 Stockbridge RB, Wolfenden R. Enhancement of the rate of pyrophosphate hydrolysis by nonenzymatic catalysts and by inorganic pyrophosphatase. The Journal of Biological Chemistry. 286: 18538-46. PMID 21460215 DOI: 10.1074/Jbc.M110.214510  0.697
2011 Wolfenden R, Lewis CA, Yuan Y. Kinetic challenges facing oxalate, malonate, acetoacetate, and oxaloacetate decarboxylases. Journal of the American Chemical Society. 133: 5683-5. PMID 21434608 DOI: 10.1021/Ja111457H  0.405
2010 Stockbridge RB, Lewis CA, Yuan Y, Wolfenden R. Impact of temperature on the time required for the establishment of primordial biochemistry, and for the evolution of enzymes. Proceedings of the National Academy of Sciences of the United States of America. 107: 22102-5. PMID 21123742 DOI: 10.1073/Pnas.1013647107  0.69
2010 Stockbridge RB, Schroeder GK, Wolfenden R. The rate of spontaneous cleavage of the glycosidic bond of adenosine. Bioorganic Chemistry. 38: 224-8. PMID 20580404 DOI: 10.1016/J.Bioorg.2010.05.003  0.786
2010 Stockbridge RB, Wolfenden R. The hydrolysis of phosphate diesters in cyclohexane and acetone. Chemical Communications (Cambridge, England). 46: 4306-8. PMID 20448876 DOI: 10.1039/C0Cc00229A  0.698
2009 Marquez VE, Schroeder GK, Ludek OR, Siddiqui MA, Ezzitouni A, Wolfenden R. Contrasting behavior of conformationally locked carbocyclic nucleosides of adenosine and cytidine as substrates for deaminases. Nucleosides, Nucleotides & Nucleic Acids. 28: 614-32. PMID 20183605 DOI: 10.1080/15257770903091904  0.755
2009 Stockbridge RB, Wolfenden R. Phosphate monoester hydrolysis in cyclohexane. Journal of the American Chemical Society. 131: 18248-9. PMID 20028146 DOI: 10.1021/Ja907967Y  0.719
2009 Lewis CA, Wolfenden R. Orotic acid decarboxylation in water and nonpolar solvents: a potential role for desolvation in the action of OMP decarboxylase. Biochemistry. 48: 8738-45. PMID 19678695 DOI: 10.1021/Bi901085M  0.423
2009 Ludek OR, Schroeder GK, Liao C, Russ PL, Wolfenden R, Marquez VE. Synthesis and conformational analysis of locked carbocyclic analogues of 1,3-diazepinone riboside, a high-affinity cytidine deaminase inhibitor. The Journal of Organic Chemistry. 74: 6212-23. PMID 19618900 DOI: 10.1021/Jo901127A  0.77
2009 Stockbridge RB, Wolfenden R. The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine: a thermodynamic analysis. The Journal of Biological Chemistry. 284: 22747-57. PMID 19531469 DOI: 10.1074/Jbc.M109.017806  0.699
2008 Lewis CA, Wolfenden R. Uroporphyrinogen decarboxylation as a benchmark for the catalytic proficiency of enzymes. Proceedings of the National Academy of Sciences of the United States of America. 105: 17328-33. PMID 18988736 DOI: 10.1073/Pnas.0809838105  0.468
2008 Ludek OR, Schroeder GK, Wolfenden R, Marquez VE. Synthesis of conformationally locked carbocyclic 1,3-diazepinone nucleosides as inhibitors of cytidine deaminase. Nucleic Acids Symposium Series (2004). 659-60. PMID 18776552 DOI: 10.1093/nass/nrn333  0.719
2008 Ouvry-Patat SA, Torres MP, Quek HH, Gelfand CA, O'Mullan P, Nissum M, Schroeder GK, Han J, Elliott M, Dryhurst D, Ausio J, Wolfenden R, Borchers CH. Free-flow electrophoresis for top-down proteomics by Fourier transform ion cyclotron resonance mass spectrometry. Proteomics. 8: 2798-808. PMID 18655049 DOI: 10.1002/Pmic.200800079  0.72
2008 Wolfenden R, Yuan Y. Rates of spontaneous cleavage of glucose, fructose, sucrose, and trehalose in water, and the catalytic proficiencies of invertase and trehalas Journal of the American Chemical Society. 130: 7548-7549. PMID 18505259 DOI: 10.1021/Ja802206S  0.418
2007 Schroeder GK, Wolfenden R. Rates of spontaneous disintegration of DNA and the rate enhancements produced by DNA glycosylases and deaminases. Biochemistry. 46: 13638-47. PMID 17973496 DOI: 10.1021/Bi701480F  0.748
2007 Lewis CA, Wolfenden R. Indiscriminate binding by orotidine 5'-phosphate decarboxylase of uridine 5'-phosphate derivatives with bulky anionic c6 substituents. Biochemistry. 46: 13331-43. PMID 17967036 DOI: 10.1021/Bi700796T  0.431
2007 Schroeder GK, Wolfenden R. The rate enhancement produced by the ribosome: an improved model. Biochemistry. 46: 4037-44. PMID 17352494 DOI: 10.1021/Bi602600P  0.767
2007 Wolfenden R, Yuan Y. Monoalkyl sulfates as alkylating agents in water, alkylsulfatase rate enhancements, and the "energy-rich" nature of sulfate half-esters Proceedings of the National Academy of Sciences of the United States of America. 104: 83-86. PMID 17182738 DOI: 10.1073/Pnas.0609644104  0.401
2007 Richard JP, Wolfenden RV. The ACS Division of Biological Chemistry Iubmb Life. 59: 224-225. DOI: 10.1080/15216540601187829  0.405
2006 Jencks WP, Wolfenden RV. Fritz Albert Lipmann: June 12, 1899-July 24, 1986. Biographical Memoirs. National Academy of Sciences (U.S.). 88: 246-66. PMID 18543445  0.513
2006 Wolfenden R. Degrees of difficulty of water-consuming reactions in the absence of enzymes Chemical Reviews. 106: 3379-3396. PMID 16895333 DOI: 10.1021/Cr050311Y  0.391
2006 Huang DT, Kaplan J, Menz RI, Katis VL, Wake RG, Zhao F, Wolfenden R, Christopherson RI. Thermodynamic analysis of catalysis by the dihydroorotases from hamster and Bacillus caldolyticus, as compared with the uncatalyzed reaction Biochemistry. 45: 8275-8283. PMID 16819826 DOI: 10.1021/Bi060595W  0.428
2006 Callahan BP, Lomino JV, Wolfenden R. Nanomolar inhibition of the enterobactin biosynthesis enzyme, EntE: synthesis, substituent effects, and additivity. Bioorganic & Medicinal Chemistry Letters. 16: 3802-5. PMID 16678412 DOI: 10.1016/J.Bmcl.2006.04.024  0.713
2006 Schroeder GK, Lad C, Wyman P, Williams NH, Wolfenden R. The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA. Proceedings of the National Academy of Sciences of the United States of America. 103: 4052-5. PMID 16537483 DOI: 10.1073/Pnas.0510879103  0.755
2006 Callahan BP, Bell AF, Tonge PJ, Wolfenden R. A Raman-active competitive inhibitor of OMP decarboxylase. Bioorganic Chemistry. 34: 59-65. PMID 16457871 DOI: 10.1016/J.Bioorg.2005.12.001  0.692
2005 Horvat CM, Wolfenden RV. A persistent pesticide residue and the unusual catalytic proficiency of a dehalogenating enzyme. Proceedings of the National Academy of Sciences of the United States of America. 102: 16199-202. PMID 16260733 DOI: 10.1073/Pnas.0508176102  0.45
2005 Callahan BP, Yuan Y, Wolfenden R. The burden borne by urease. Journal of the American Chemical Society. 127: 10828-9. PMID 16076178 DOI: 10.1021/Ja0525399  0.719
2005 Sievers A, Wolfenden R. The effective molarity of the substrate phosphoryl group in the transition state for yeast OMP decarboxylase. Bioorganic Chemistry. 33: 45-52. PMID 15668182 DOI: 10.1016/J.Bioorg.2004.08.005  0.638
2005 Callahan BP, Wolfenden R. Orotidine Monophosphate Decarboxylase: A Mechanistic Dialogue. Topics in Current Chemistry, 238 Edited by Jeehiun K. Lee (Rutgers University) and Dean J. Tantillo (University of California, Davis). Springer-Verlag: Berlin, Heidelberg, New York. 2004. x + 152 pp. $139.00. ISBN 3-540-20566-7. Journal of the American Chemical Society. 127: 4541-4541. DOI: 10.1021/Ja040982Y  0.637
2004 Callahan BP, Wolfenden R. OMP decarboxylase: an experimental test of electrostatic destabilization of the enzyme-substrate complex. Journal of the American Chemical Society. 126: 14698-9. PMID 15535676 DOI: 10.1021/Ja0450049  0.727
2004 Borchers CH, Marquez VE, Schroeder GK, Short SA, Snider MJ, Speir JP, Wolfenden R. Fourier transform ion cyclotron resonance MS reveals the presence of a water molecule in an enzyme transition-state analogue complex. Proceedings of the National Academy of Sciences of the United States of America. 101: 15341-5. PMID 15494437 DOI: 10.1073/Pnas.0406781101  0.798
2004 Wolfenden R, Zhao F. Lithium-catalyzed hydroxide attack at the carbon atom of methyl phosphate Journal of the American Chemical Society. 126: 8646-8647. PMID 15250705 DOI: 10.1021/Ja0473586  0.351
2004 Sievers A, Beringer M, Rodnina MV, Wolfenden R. The ribosome as an entropy trap. Proceedings of the National Academy of Sciences of the United States of America. 101: 7897-901. PMID 15141076 DOI: 10.1073/Pnas.0402488101  0.631
2004 Callahan BP, Wolfenden R. Charge development in the transition state for decarboxylations in water: spontaneous and acetone-catalyzed decarboxylation of aminomalonate. Journal of the American Chemical Society. 126: 4514-5. PMID 15070358 DOI: 10.1021/Ja031720J  0.711
2004 Sievers A, Beringer M, Rodnina MV, Wolfenden RV. Erratum: The ribosome as an entropy trap (Proceedings of the National Academy of Sciences of the United States of America (May 25, 2004) 101, 21 (7897-7901)) Proceedings of the National Academy of Sciences of the United States of America. 101: 12397-12398. DOI: 10.1073/Pnas.0404478101  0.522
2004 Snider MG, Temple BS, Wolfenden R. The path to the transition state in enzyme reactions: A survey of catalytic efficiencies Journal of Physical Organic Chemistry. 17: 586-591. DOI: 10.1002/Poc.761  0.419
2003 Wolfenden R. Thermodynamic and extrathermodynamic requirements of enzyme catalysis Biophysical Chemistry. 105: 559-572. PMID 14499918 DOI: 10.1016/S0301-4622(03)00066-8  0.484
2003 Lad C, Williams NH, Wolfenden R. The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases. Proceedings of the National Academy of Sciences of the United States of America. 100: 5607-10. PMID 12721374 DOI: 10.1073/Pnas.0631607100  0.477
2003 Callahan BP, Wolfenden R. Migration of methyl groups between aliphatic amines in water. Journal of the American Chemical Society. 125: 310-1. PMID 12517124 DOI: 10.1021/Ja021212U  0.703
2002 Sievers A, Wolfenden R. Equilibrium of formation of the 6-carbanion of UMP, a potential intermediate in the action of OMP decarboxylase. Journal of the American Chemical Society. 124: 13986-7. PMID 12440884 DOI: 10.1021/Ja021073G  0.582
2002 Miller BG, Wolfenden R. Catalytic proficiency: the unusual case of OMP decarboxylase. Annual Review of Biochemistry. 71: 847-85. PMID 12045113 DOI: 10.1146/Annurev.Biochem.71.110601.135446  0.561
2002 Borders CL, Snider MJ, Wolfenden R, Edmiston PL. Determination of the affinity of each component of a composite quaternary transition-state analogue complex of creatine kinase. Biochemistry. 41: 6995-7000. PMID 12033932 DOI: 10.1021/Bi020105+  0.692
2002 Snider MJ, Lazarevic D, Wolfenden R. Catalysis by entropic effects: the action of cytidine deaminase on 5,6-dihydrocytidine. Biochemistry. 41: 3925-30. PMID 11900535 DOI: 10.1021/Bi011696R  0.744
2002 Snider MJ, Reinhardt L, Wolfenden R, Cleland WW. 15N kinetic isotope effects on uncatalyzed and enzymatic deamination of cytidine. Biochemistry. 41: 415-21. PMID 11772041 DOI: 10.1021/Bi011410I  0.714
2002 Sievers A, Wolfenden R. Equilibrium of formation of the 6-carbanion of UMP, a potential intermediate in the action of OMP decarboxylase Journal of the American Chemical Society. 124: 13986-13987. DOI: 10.1021/ja021073g  0.486
2001 Wolfenden R, Snider MJ. The depth of chemical time and the power of enzymes as catalysts. Accounts of Chemical Research. 34: 938-45. PMID 11747411 DOI: 10.1021/Ar000058I  0.748
2001 Snider MJ, Wolfenden R. Site-bound water and the shortcomings of a less than perfect transition state analogue. Biochemistry. 40: 11364-71. PMID 11560484 DOI: 10.1021/Bi011189+  0.728
2001 Miller BG, Butterfoss GL, Short SA, Wolfenden R. Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5'-phosphate decarboxylase: a role for substrate destabilization? Biochemistry. 40: 6227-32. PMID 11371183 DOI: 10.1021/Bi0028993  0.613
2001 Miller BG, Snider MJ, Wolfenden R, Short SA. Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase. The Journal of Biological Chemistry. 276: 15174-6. PMID 11278904 DOI: 10.1074/Jbc.M011429200  0.768
2000 Snider MJ, Gaunitz S, Ridgway C, Short SA, Wolfenden R. Temperature effects on the catalytic efficiency, rate enhancement, and transition state affinity of cytidine deaminase, and the thermodynamic consequences for catalysis of removing a substrate "anchor". Biochemistry. 39: 9746-53. PMID 10933791 DOI: 10.1021/Bi000914Y  0.735
2000 Miller BG, Snider MJ, Short SA, Wolfenden R. Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5'-phosphate decarboxylase. Biochemistry. 39: 8113-8. PMID 10889016 DOI: 10.1021/Bi000818X  0.767
2000 Miller BG, Hassell AM, Wolfenden R, Milburn MV, Short SA. Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog. Proceedings of the National Academy of Sciences of the United States of America. 97: 2011-6. PMID 10681417 DOI: 10.1073/Pnas.030409797  0.598
2000 Jencks WP, Wolfenden RV. Fritz Albert Lipmann. 12 June 1899 — 24 July 1986 Biographical Memoirs of Fellows of the Royal Society. 46: 333-344. DOI: 10.1098/Rsbm.1999.0088  0.564
2000 Snider MJ, Wolfenden R. The rate of spontaneous decarboxylation of amino acids [1] Journal of the American Chemical Society. 122: 11507-11508. DOI: 10.1021/Ja002851C  0.667
2000 Miller BG, Snider MJ, Short SA, Wolfenden R. Contribution of enzyme - Phosphoribosyl contacts to catalysis by orotidine 5′-phosphate decarboxylase Biochemistry. 39: X-8118.  0.732
1999 Carlow DC, Carter CW, Mejlhede N, Neuhard J, Wolfenden R. Cytidine deaminases from B. subtilis and E. coli: compensating effects of changing zinc coordination and quaternary structure. Biochemistry. 38: 12258-65. PMID 10493793 DOI: 10.1021/Bi990819T  0.387
1999 Miller BG, Smiley JA, Short SA, Wolfenden R. Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals. The Journal of Biological Chemistry. 274: 23841-3. PMID 10446147 DOI: 10.1074/Jbc.274.34.23841  0.545
1999 Wolfenden R. Conformational aspects of inhibitor design: Enzyme-substrate interactions in the transition state Bioorganic and Medicinal Chemistry. 7: 647-652. PMID 10400319 DOI: 10.1016/S0968-0896(98)00247-8  0.446
1999 Wolfenden R, Snider M, Ridgway C, Miller B. The temperature dependence of enzyme rate enhancements [8] Journal of the American Chemical Society. 121: 7419-7420. DOI: 10.1021/Ja991280P  0.746
1998 Carlow D, Wolfenden R. Substrate connectivity effects in the transition state for cytidine deaminase Biochemistry. 37: 11873-11878. PMID 9718310 DOI: 10.1021/Bi980959N  0.434
1998 Shih P, Pedersen LG, Gibbs PR, Wolfenden R. Hydrophobicities of the nucleic acid bases: distribution coefficients from water to cyclohexane. Journal of Molecular Biology. 280: 421-30. PMID 9665846 DOI: 10.1006/Jmbi.1998.1880  0.545
1998 Carlow DC, Short SA, Wolfenden R. Complementary truncations of a hydrogen bond to ribose involved in transition-state stabilization by cytidine deaminase Biochemistry. 37: 1199-1203. PMID 9477944 DOI: 10.1021/Bi971731N  0.44
1998 Miller BG, Traut TW, Wolfenden R. A role for zinc in OMP decarboxylase, an unusually proficient enzyme [9] Journal of the American Chemical Society. 120: 2666-2667. DOI: 10.1021/Ja980066I  0.528
1998 Miller BG, Traut TW, Wolfenden R. Effects of substrate binding determinants in the transition state for orotidine 5'-monophosphate decarboxylase Bioorganic Chemistry. 26: 283-288. DOI: 10.1006/Bioo.1998.1105  0.576
1997 Xiang S, Short SA, Wolfenden R, Carter CW. The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization. Biochemistry. 36: 4768-74. PMID 9125497 DOI: 10.1021/Bi963091E  0.386
1997 Bearne SL, Wolfenden R. Mandelate racemase in pieces: Effective concentrations of enzyme functional groups in the transition state Biochemistry. 36: 1646-1656. PMID 9048548 DOI: 10.1021/Bi9620722  0.682
1996 Shih P, Wolfenden R. Enzyme - Substrate complexes of adenosine and cytidine deaminases: Absence of accumulation of water adducts Biochemistry. 35: 4697-4703. PMID 8664259 DOI: 10.1021/Bi952357Z  0.468
1996 Xiang S, Short SA, Wolfenden R, Carter CW. Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis. Biochemistry. 35: 1335-41. PMID 8634261 DOI: 10.1021/Bi9525583  0.415
1996 Carlow DC, Short SA, Wolfenden R. Role of glutamate-104 in generating a transition state analogue inhibitor at the active site of cytidine deaminase Biochemistry. 35: 948-954. PMID 8547277 DOI: 10.1021/Bi951498Y  0.432
1996 Radzicka A, Wolfenden R. Rates of uncatalyzed peptide bond hydrolysis in neutral solution and the transition state affinities of proteases Journal of the American Chemical Society. 118: 6105-6109. DOI: 10.1021/Ja954077C  0.366
1995 Radzicka A, Wolfenden R. A proficient enzyme Science. 267: 90-93. PMID 7809611 DOI: 10.1126/Science.7809611  0.452
1995 Radzicka A, Wolfenden R. Transition state and multisubstrate analog inhibitors Methods in Enzymology. 249: 284-312. PMID 7791615 DOI: 10.1016/0076-6879(95)49039-6  0.438
1995 Xiang S, Short SA, Wolfenden R, Carter CW. Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase. Biochemistry. 34: 4516-23. PMID 7718553 DOI: 10.1021/Bi00014A003  0.381
1995 Carlow DC, Smith AA, Yang CC, Short SA, Wolfenden R. Major contribution of a carboxymethyl group to transition-state stabilization by cytidine deaminase: mutation and rescue. Biochemistry. 34: 4220-4224. PMID 7703234 DOI: 10.1021/Bi00013A010  0.436
1995 Bearne SL, Wolfenden R. Glutamate γ-semialdehyde as a natural transition state analogue inhibitor of escherichia coli glucosamine-6-phosphate synthase Biochemistry. 34: 11515-11520. PMID 7547881 DOI: 10.1021/Bi00036A026  0.631
1995 Bearne SL, Wolfenden R. Enzymatic hydration of an olefin: The burden borne by fumarase Journal of the American Chemical Society. 117: 9588-9589. DOI: 10.1021/Ja00142A037  0.59
1994 Betts L, Xiang S, Short SA, Wolfenden R, Carter CW. Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex. Journal of Molecular Biology. 235: 635-56. PMID 8289286 DOI: 10.1006/Jmbi.1994.1018  0.356
1994 Smith AA, Carlow DC, Wolfenden R, Short SA. Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase Biochemistry®. 6468-6474. PMID 8204580 DOI: 10.1021/Bi00187A012  0.399
1993 Grosshans J, Wolfenden R. Transition-state discrimination by adenosine deaminase from Aspergillus oryzae. Biochimica Et Biophysica Acta. 1161: 28-32. PMID 8422418 DOI: 10.1016/0167-4838(93)90191-S  0.448
1993 Dzingeleski GD, Wolfenden R. Hypersensitivity of an enzyme reaction to solvent water Biochemistry. 32: 9143-9147. PMID 8369284 DOI: 10.1021/Bi00086A020  0.42
1993 Radzicka A, Young GB, Wolfenden R. Lack of water transport by amino acid side chains or peptides entering a nonpolar environment Biochemistry. 32: 6807-6809. PMID 8334113 DOI: 10.1021/Bi00078A001  0.304
1993 Wolfenden R. Are there limits to enzyme-inhibitor binding discrimination? Inferences from the behavior of nucleoside deaminases Pharmacology & Therapeutics. 60: 235-244. PMID 8022859 DOI: 10.1016/0163-7258(93)90008-2  0.426
1992 Yang C, Carlow D, Wolfenden R, Short SA. Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene. Biochemistry. 31: 4168-4174. PMID 1567863 DOI: 10.1021/Bi00132A003  0.307
1992 Kati WM, Acheson SA, Wolfenden R. A transition state in pieces: major contributions of entropic effects to ligand binding by adenosine deaminase. Biochemistry. 31: 7356-7366. PMID 1510925 DOI: 10.1021/Bi00147A021  0.441
1992 Radzicka A, Acheson SA, Wolfenden R. Cis/trans isomerization at proline: Desolvation and its consequences for protein folding Bioorganic Chemistry. 20: 382-386. DOI: 10.1016/0045-2068(92)90048-8  0.316
1991 Radzicka A, Wolfenden R. Analogues of intermediates in the action of pig kidney prolidase. Biochemistry. 30: 4160-4164. PMID 2021607 DOI: 10.1021/Bi00231A008  0.419
1991 Smar M, Short SA, Wolfenden R. Lyase activity of nucleoside 2-deoxyribosyltransferase : transient generation of ribal and its use in the synthesis of 2'-deoxynucleosides Biochemistry. 30: 7908-7912. PMID 1868066 DOI: 10.1021/Bi00246A006  0.36
1991 Wolfenden R, Radzicka A. Transition-state analogues Current Opinion in Structural Biology. 1: 780-787. DOI: 10.1016/0959-440X(91)90179-W  0.363
1991 Wolfenden RV, Liang YL. Relative free energies of solvation of PO, PN, and PC derivatives related to phosphoramide inhibitors of metallopeptidases Bioorganic Chemistry. 19: 152-156. DOI: 10.1016/0045-2068(91)90031-J  0.354
1990 Acheson SA, Bell JB, Jones ME, Wolfenden R. Orotidine-5′-monophosphate decarboxylase catalysis: Kinetic isotope effects and the state of hybridization of a bound transition-state analogue Biochemistry. 29: 3158-3202. PMID 2334689 DOI: 10.1021/Bi00465A007  0.574
1989 Kati WM, Wolfenden R. Major enhancement of the affinity of an enzyme for a transition-state analog by a single hydroxyl group. Science. 243: 1591-1593. PMID 2928795 DOI: 10.1126/Science.2928795  0.402
1989 Jones W, Kurz LC, Wolfenden R. Transition-state stabilization by adenosine deaminase: 1,6-Addition of water to purine ribonucleoside, the enzyme's affinity for 6-hydroxy-1,6-dihydropurine ribonucleoside, and the effective concentration of substrate water at the active site Biochemistry. 28: 1242-1247. PMID 2713361 DOI: 10.1021/Bi00429A043  0.473
1989 Frick L, Yang C, Marquez VE, Wolfenden RV. Binding of pyrimidin-2-one ribonucleoside by cytidine deaminase as the transition-state analogue 3,4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity Biochemistry. 28: 9423-9430. PMID 2692708 DOI: 10.1021/Bi00450A027  0.408
1989 Kati WM, Wolfenden R. Contribution of a single hydroxyl group to transition-state discrimination by adenosine deaminase: Evidence for an "entropy trap" mechanism Biochemistry. 28: 7919-7927. PMID 2558714 DOI: 10.1021/Bi00445A055  0.41
1989 Wolfenden R, Liang YL. Contributions of solvent water to biological group-transfer potentials: Mixed anhydrides of phosphoric and carboxylic acids Bioorganic Chemistry. 17: 486-489. DOI: 10.1016/0045-2068(89)90049-7  0.337
1988 Radzicka A, Pedersen L, Wolfenden R. Influences of solvent water on protein folding: free energies of solvation of cis and trans peptides are nearly identical Biochemistry. 27: 4538-4541. PMID 3166998 DOI: 10.1021/Bi00412A047  0.502
1988 Acheson SA, Kirkman HN, Wolfenden R. Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration Biochemistry. 27: 7371-7375. PMID 3061454 DOI: 10.1021/Bi00419A030  0.378
1987 Wolfenden R, Liang YL, Matthews M, Williams R. Cooperativity and anticooperativity in solvation by water: imidazoles, quinones, nitrophenols, nitrophenolate, and nitrothiophenolate ions Journal of the American Chemical Society. 109: 463-466. DOI: 10.1021/Ja00236A026  0.319
1987 Frick L, Neela JPM, Wolfenden R. Transition state stabilization by deaminases: Rates of nonenzymatic hydrolysis of adenosine and cytidine Bioorganic Chemistry. 15: 100-108. DOI: 10.1016/0045-2068(87)90011-3  0.397
1986 Frick L, Wolfenden R, Smal E, Baker DC. Transition-state stabilization by adenosine deaminase: structural studies of its inhibitory complex with deoxycoformycin. Biochemistry. 25: 1616-1621. PMID 3486673 DOI: 10.1021/Bi00355A025  0.451
1986 Wolfenden R, Frick L. Mechanisms of Enzyme Action and Inhibition: Transition State Analogues for Acid-Base Catalysis ~ Journal of Protein Chemistry. 5: 147-155. DOI: 10.1007/Bf01025198  0.486
1985 Andersson L, MacNeela J, Wolfenden R. Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidase. Biochemistry. 24: 330-333. PMID 3978076 DOI: 10.1021/Bi00323A014  0.402
1985 Frick L, Wolfenden R. Mechanistic implications of the inhibition of peptidases by amino aldehydes and bestatin Biochimica Et Biophysica Acta. 829: 311-318. PMID 3890953 DOI: 10.1016/0167-4838(85)90238-9  0.369
1983 Davis KR, Wolfenden RV. Solvent isotope effects on equilibriums of mono- and dihydration of neutral pteridine Journal of Organic Chemistry. 48: 2280-2281. DOI: 10.1021/Jo00161A029  0.339
1983 Wolfenden R, Williams R. Affinities Of Phosphoric Acids, Esters, And Amides For Solvent Water. Journal of the American Chemical Society. 105: 1028-1031. DOI: 10.1021/Ja00342A063  0.312
1983 Wolfenden R, Williams R. Affinities Of Phosphoric Acids, Esters, And Amides For Solvent Water Cheminform. 14. DOI: 10.1002/Chin.198322092  0.312
1982 Andersson L, Isley TC, Wolfenden R. alpha-aminoaldehydes: transition state analogue inhibitors of leucine aminopeptidase. Biochemistry. 21: 4177-4180. PMID 7126535 DOI: 10.1021/Bi00260A040  0.375
1981 Wolfenden R, Andersson L, Cullis PM, Southgate CCB. Affinities of Amino Acid Side Chains for Solvent Water Biochemistry. 20: 849-855. PMID 7213619 DOI: 10.1021/Bi00507A030  0.304
1978 Wolfenden R. Interaction of the peptide bond with solvent water: a vapor phase analysis. Biochemistry. 17: 201-204. PMID 618544 DOI: 10.1021/Bi00594A030  0.315
1978 Wentworth DF, Wolfenden R. [52] Cytidine deaminases (from Escherichia coli and human liver) Methods in Enzymology. 51: 401-407. PMID 357900 DOI: 10.1016/S0076-6879(78)51054-9  0.324
1978 Campbell ID, Jones RB, Kiener PA, Richards E, Waley SC, Wolfenden R. The form of 2-phosphoglycollic acid bound by triosephosphate isomerase. Biochemical and Biophysical Research Communications. 83: 347-52. PMID 29623 DOI: 10.1016/0006-291X(78)90438-2  0.405
1977 Lewis CA, Wolfenden R. Thiohemiacetal formation by inhibitory aldehydes at the active site of papain Biochemistry. 16: 4890-4895. PMID 911798 DOI: 10.1021/Bi00641A023  0.394
1977 Lewis CA, Wolfenden R. Antiproteolytic aldehydes and ketones: Substituent and secondary deuterium isotope effects on equilibrium addition of water and other nucleophiles Biochemistry. 16: 4886-4890. PMID 911797 DOI: 10.1021/Bi00641A022  0.377
1977 Wolfenden R, Wentworth DF, Mitchell GN. Influence of substituent ribose on transition state affinity in reactions catalyzed by adenosine deaminase. Biochemistry. 16: 5071-5077. PMID 562185 DOI: 10.1021/Bi00642A020  0.416
1975 Evans BE, Mitchell GN, Wolfenden R. The action of bacterial cytidine deaminase on 5,6-dihydrocytidine. Biochemistry. 14: 621-4. PMID 1090298 DOI: 10.1021/Bi00674A024  0.431
1975 Wentworth DF, Wolfenden R. On the interaction of 3,4,5,6-tetrahydrouridine with human liver cytidine deaminase. Biochemistry. 14: 5099-5105. PMID 53069 DOI: 10.1021/Bi00694A012  0.437
1975 Hartman FC, LaMuraglia GM, Tomozawa Y, Wolfenden R. The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the Active-site carboxyl group Biochemistry. 14: 5274-5279. PMID 47 DOI: 10.1021/Bi00695A007  0.397
1974 Wolfenden R. Enzyme catalysis: Conflicting requirements of substrate access and transition state affinity Molecular and Cellular Biochemistry. 3: 207-211. PMID 4365214 DOI: 10.1007/Bf01686645  0.418
1973 Byers LD, Wolfenden R. Binding of the by-product analog benzylsuccinic acid by carboxypeptidase A. Biochemistry. 12: 2070-8. PMID 4735879 DOI: 10.1021/Bi00735A008  0.532
1973 Evans BE, Wolfenden RV. Catalysis of the covalent hydration of pteridine by adenosine aminohydrolase. Biochemistry. 12: 392-8. PMID 4734229 DOI: 10.1021/Bi00727A005  0.328
1973 Byers L, Wolfenden R. Corrections - Binding of the By-Product Analog Benzylsuccinin Acid by Carboxypeptidase A. Biochemistry. 12: 3584-3584. DOI: 10.1021/Bi00742A602  0.531
1972 Wolfenden R. Analog approaches to the structure of the transition state in enzyme reactions Accounts of Chemical Research. 5: 10-18. DOI: 10.1021/Ar50049A002  0.376
1970 Wolfenden RV. Binding of Substrate and Transition State Analogs to Triosephosphate Isomerase Biochemistry. 9: 3404-3407. PMID 5535476 DOI: 10.1021/Bi00819A018  0.343
1969 Wolfenden RV, Kaufman J, Macon JB. Ring-modified substrates of adenosine deaminases. Biochemistry. 8: 2412-2415. PMID 5816378 DOI: 10.1021/Bi00834A024  0.301
1968 Wolfenden RV, Kirsch JF. Enzymatic displacement of oxygen and sulfur from purines. Journal of the American Chemical Society. 90: 6849-50. PMID 5687711 DOI: 10.1021/Ja01026A054  0.484
1966 Wolfenden RV. Enzymatic Hydrolysis of 6-Substituents on Purine Ribosides1 Journal of the American Chemical Society. 88: 3157-3158. DOI: 10.1021/Ja00965A064  0.392
1964 WOLFENDEN R, RAMMLER DH, LIPMANN F. ON THE SITE OF ESTERIFICATION OF AMINO ACIDS TO SOLUBLE RNA. Biochemistry. 3: 329-38. PMID 14155094 DOI: 10.1021/Bi00891A006  0.625
1961 Wolfenden R, Jencks WP. The Effect of o-Substituents on Benzaldehyde Semicarbazone Formation1 Journal of the American Chemical Society. 83: 2763-2768. DOI: 10.1021/Ja01473A037  0.575
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