Reaction mechanisms, catalysis, and movement

Protein ScienceVolume 3, Issue 12 p. 2459-2464 RecollectionFree Access Reaction mechanisms, catalysis, and movement William P. Jencks, Corresponding Author William P. Jencks jencks@binah.cc.brandeis.edu Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254–9110 William P. Jencks graduated from Harvard Medical School in 1951. After an internship in the Medical Service at Peter Bent Brigham Hospital (1951–1952), Dr. Jencks spent 2 years in postdoctoral work with Fritz Lipmann at the Massachusetts General Hospital (1952–1953 and 1955–1956). This period was interrupted by 2 years in the Army at the Army Medical Service Graduate School of the Walter Reed Army Medical Center. Dr. Jencks was Chief of the Pharmacology Department during the second year. Following this, he spent a year in R.B. Woodward's laboratory at Harvard. In 1957, Dr. Jencks joined the Graduate Department of Biochemistry at Brandeis University, where he has remained since. His research has centered around 3 areas: (1) the mechanism of catalysis of acyl and carbonyl group reactions in water; (2) the mechanism of acyl transfer and hydrolysis reactions catalyzed by enzymes; and (3) the mechanism of the interaction of small and large molecules with each other in aqueous solution. Recently, Dr. Jencks has been particularly concerned with the way in which reaction mechanisms are determined by the lifetime of reaction intermediates in general acid-base catalysis, carbanion, carbocation, and ligand exchange reactions, and the use of structure-reactivity interactions to characterize transition states. Dr. Jencks is a member of the American Society of Biological Chemists, Alpha Omega Alpha, and served as Councilor of the American Chemical Society (1989–1992). He is a fellow of the American Association for the Advancement of Science and former Councilor of the American Academy of Arts and Sciences (1971–1975). In 1971, Dr. Jencks was elected to the National Academy of Sciences. He was elected a foreign member of the Royal Society in 1992. He received the American Chemical Society Award in Biological Chemistry sponsored by the Eli Lilly Company in 1962 and he was the recipient of the American Society of Biological Chemists Award sponsored by Merck, Sharp, and Dohme Research Laboratories Division of Merck and Company, Inc. Dr. Jencks is the author of a text, Catalysis in Chemistry and Enzymology (1969), and a review, “Binding energy, specificity and enzyme catalysis-The Circe effect” (1975), that updates much of this text; coauthor of a recent biochemistry text (Abeles et al., 1992); and has published more than 360 articles in scientific journals.Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254–9110Search for more papers by this author William P. Jencks, Corresponding Author William P. Jencks jencks@binah.cc.brandeis.edu Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254–9110 William P. Jencks graduated from Harvard Medical School in 1951. After an internship in the Medical Service at Peter Bent Brigham Hospital (1951–1952), Dr. Jencks spent 2 years in postdoctoral work with Fritz Lipmann at the Massachusetts General Hospital (1952–1953 and 1955–1956). This period was interrupted by 2 years in the Army at the Army Medical Service Graduate School of the Walter Reed Army Medical Center. Dr. Jencks was Chief of the Pharmacology Department during the second year. Following this, he spent a year in R.B. Woodward's laboratory at Harvard. In 1957, Dr. Jencks joined the Graduate Department of Biochemistry at Brandeis University, where he has remained since. His research has centered around 3 areas: (1) the mechanism of catalysis of acyl and carbonyl group reactions in water; (2) the mechanism of acyl transfer and hydrolysis reactions catalyzed by enzymes; and (3) the mechanism of the interaction of small and large molecules with each other in aqueous solution. Recently, Dr. Jencks has been particularly concerned with the way in which reaction mechanisms are determined by the lifetime of reaction intermediates in general acid-base catalysis, carbanion, carbocation, and ligand exchange reactions, and the use of structure-reactivity interactions to characterize transition states. Dr. Jencks is a member of the American Society of Biological Chemists, Alpha Omega Alpha, and served as Councilor of the American Chemical Society (1989–1992). He is a fellow of the American Association for the Advancement of Science and former Councilor of the American Academy of Arts and Sciences (1971–1975). In 1971, Dr. Jencks was elected to the National Academy of Sciences. He was elected a foreign member of the Royal Society in 1992. He received the American Chemical Society Award in Biological Chemistry sponsored by the Eli Lilly Company in 1962 and he was the recipient of the American Society of Biological Chemists Award sponsored by Merck, Sharp, and Dohme Research Laboratories Division of Merck and Company, Inc. Dr. Jencks is the author of a text, Catalysis in Chemistry and Enzymology (1969), and a review, “Binding energy, specificity and enzyme catalysis-The Circe effect” (1975), that updates much of this text; coauthor of a recent biochemistry text (Abeles et al., 1992); and has published more than 360 articles in scientific journals.Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254–9110Search for more papers by this author First published: December 1994 https://doi.org/10.1002/pro.5560031232Citations: 10 AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References Abeles RH, Frey PA, Jencks WP. 1992. Biochemistry. New York: Jones and Barlett. Anderson BM, Cordes E, Jencks WP. 1961. Reactivity and catalysis in reactions of the serine hydroxyl group and of O-acyl serines. J Biol Chem 236: 455– 463. Barrett E, Lapworth A. 1908. The influence of acids and alkalis on the velocity of formation of acetoxime. J Chem Soc 93: 85– 93. Betts RL, Hammett LP. 1937. A kinetic study of the ammonolysis of phenylacetic esters in methanol solution. J Am Chem Soc 59: 1568– 1572. Buchwald SL, Friedman JM, Knowles JR. 1984. Stereochemistry of nucleophilic displacement on two phosphoric monoesters and a phosphogua-nidine: The role of metaphosphate. J Am Chem Soc 106: 4911– 4916. Conant JB, Bartlett PD. 1932. A quantitative study of semicarbazone formation. J Am Chem Soc 54: 2881– 2899. Di Sabato G, Jencks WP. 1961a. Mechanism and catalysis of reactions of acyl phosphates. I. Nucleophilic reactions. J Am Chem Soc 83: 4393– 4400. Di Sabato G, Jencks WP. 1961b. Mechanism and catalysis of reactions of acyl phosphates. II. Hydrolysis. J Am Chem Soc 83: 4400– 4405. Friedman JM, Knowies JR. 1985. The quest for free metaphosphate in solution: Racemization at phosphorus in the transfer of the phospho group from phenyl phosphate to tert-butyl alcohol in acetonitrile. J Am Chem Soc 107: 6126– 6127. Hammett LP. 1940. Physical organic chemistry. New York: McGraw-Hill Book Company, Inc. p 31. Jencks WP. 1953. Discussion (fatty acid activating enzyme). Fed Proc 12: 703. Jencks WP. 1959. Studies on the mechanism of oxime and semicarbazone formation. J Am Chem Soc 81: 475– 481. Jencks WP. 1969. Catalysis in chemistry and enzymology. New York: McGraw-Hill. Jencks WP. 1972. General acid-base catalysis of complex reactions in water. Chem Rev 72: 705– 718. Jencks WP. 1975. Binding energy, specificity, and enzyme catalysis—The Circe effect. Adv Enzymol 43: 219– 410. Jencks WP. 1980. The utilization of binding energy in coupled vectorial processes. Adv Enzymol 51: 75– 106. Jencks WP. 1989. Utilization of binding energy and coupling rules for active transport and other coupled vectorial processes. Methods Enzymol 171: 145– 164. Jencks WP, Carriuolo J. 1959a. Imidazole catalysis. II. Acyl transfer and the reactions of acetylimidazole with water and oxygen anions. J Biol Chem 234: 1272– 1279. Jencks WP, Carriuolo J. 1959b. Imidazole catalysis. III. General base catalysis and the reactions of acetylimidazole with thiols and amines. J Biol Chem 234: 1280– 1285. Jencks WP, Carriuolo J. 1960. General base catalysis of the aminolysis of phenyl acetate. J Am Chem Soc 82: 675– 681. Jencks WP, Carriuolo J. 1961. General base catalysis of ester hydrolysis. J Am Chem Soc 83: 1743– 1750. Jencks WP, Cordes S, Carriuolo J. 1960. The free energy of thiol ester hydrolysis. J Biol Chem 235: 3608– 3614. Jencks WP, Durrum EL. 1955. Paper electrophoresis as a quantitative method: The staining of serum lipoproteins. J Clin Invest 34: 1437– 1448. Jencks WP, Hyatt MR, Jetton MR, Mattingly TW, Durrum EL. 1956a. A study of serum lipoproteins in normal and atherosclerotic patients by paper electrophoretic techniques. J Clin Invest 35: 980– 990. Jencks WP, Jetton MR, Durrum E. 1955. Paper electrophoresis as a quantitative method: Serum proteins. Biochem J 60: 205– 215. Jencks WP, Lipmann F. 1957. Studies on the initial step of fatty acid activation. J Biol Chem 225: 207– 223. Jencks WP, Smith ERB, Durrum EL. 1956b. The clinical significance of the analysis of serum protein distribution by filter paper electrophoresis. Am J Med 27: 387– 405. Langan TA, Jencks WP, Durrum EL. 1955. Paper electrophoresis as a quantitative method: The measurement of alpha and beta lipoprotein cholesterol. J Clin Invest 34: 1427– 1436. Page MI, Jencks WP. 1971. Entropic contributions to rate accelerations in enzymic intramolecular reactions and the chelate effect. Proc Natl Acad Sci USA 68: 1678– 1683. Pickart CM, Jencks WP. 1984. Energetics of the calcium-transporting ATPase. J Biol Chem 259: 1629– 1643. Stadtman ER. 1954. On the energy-rich nature of acetylimidazole, an enzymatically active compound. In: WD McElroy, B Glass, eds. Mechanism of enzyme action. Baltimore, Maryland: Johns Hopkins Press. p 581. Wald G, Nathanson N, Jencks WP, Tarr E. 1948. Crustacyanin, the blue carotenoid-protein of the lobster shell. Biol Bull 95: 249– 250. Citing Literature Volume3, Issue12December 1994Pages 2459-2464 ReferencesRelatedInformation