This enzyme catalyzes the cleavage of RNA via a cyclic phosphate intermediate. DNA lacks the 2-hydroxyl group essential for formation of this cyclic form. In this enzyme two histidines are located near the bond to be broken.
In the cyclization step one acts as a general-base catalyst and the other as a general acid catalyst (His-12 and His-119 in bovine pancreatic ribonuclease). These roles are reversed in the step involving hydrolysis of the cyclic phosphate.
The molecule has a well-defined binding cleft. The mechanism seems to involve nucleophilic displacement on phosphorus with a pentacovalent intermediate, with the attacking nucleophile entering opposite the leaving group (`in-line').
Born in Monessen, Pennsylvania, March 26, 1916 Dr. Anfinsen obtained a B.A.
degree from Swarthmore College in 1937 and an M.S. in organic chemistry in 1939 from the University of Pennsylvania. He spent the year 1939-40 as a Visiting Investigator at the Carlsberg Laboratory in Copenhagen. In 1943, he received a Ph.D. from Harvard Medical School in biochemistry and spent the next seven years at Harvard Medical School; first as Instructor and then as Assistant Professor of Biological Chemistry. During this time, he spent a year (1947-48) as a Senior Fellow of the American Cancer Society working with Dr. Hugo Theorell at the Medical Nobel Institute. Dr. Anfinsen left Harvard in 1950 to become Chief of the Laboratory of Cellular Physiology and Metabolism in the National Heart Institute of the National Institutes of Health. He was again at Harvard Medical School as Professor of Biological Chemistry in 1962-63 and then returned to the National Institutes of Health to assume his present position.
In Anfinsen's early work, he and Steinberg studied the non-uniform labelling in newly synthesized proteins - a technique which later permitted Dintzis, Canfield and others to determine that proteins are synthesized sequentially from the amino-terminal and in vivo, and to calculate the rate at which amino acids are polymerized.
In the mid 1950's Anfinsen began to concentrate on the problem of the relationship between structure and function in enzymes. On the basis of studies on ribonuclease with Sela and White, he proposed that the information determining the tertiary structure of a protein resides in the chemistry of its amino acid sequence. Investigations on reversible denaturation of several proteins served to verify this proposal experimentally. It was demonstrated that, after cleavage of disulfide bonds and disruption of tertiary structure, many proteins could spontaneously refold to their native forms. This work resulted in general acceptance of the "thermodynamic hypothesis". Studies on the rate and extent of renaturation in vitro led to the discovery of a microsomal enzyme which catalyzes sulfhydryl-disulfide interchange and thereby accelerates, in vitro, the refolding of denatured proteins containing disulfide bonds. In the presence of this enzyme the rate of renaturation approaches that sufficient to account for folding of newly completed polypeptide chains during protein biosynthesis. These findings have given important impetus to studies on the organic synthesis of proteins, since they demonstrate that, under physiological conditions of environment, attainment of the native structure rests solely upon the correct sequential polymerization of the amino acids.
In addition to his research activities, Dr. Anfinsen is an editor of Advances in Protein Chemistry, served on the Editorial Board of the Journal of Biological Chemistry and wrote "The Molecular Basis of Evolution" which was published in 1959. He is active as a member of the Board of Governors of the Weizmann Institute of Science in Rehovot, Israel, and was elected President of the American Society of Biological Chemists for the Academic Year 1971-72. His honors include a Rockefeller Foundation Public Service Award in 1954, a Guggenheim Fellowship in 1958, election to the National Academy of Sciences in 1963 and the Royal Danish Academy in 1964, and Honorary Doctor of Science degrees from Swarthmore College (1965), Georgetown University (1967), and New York Medical College (1969).
In recent years, Anfinsen has devoted himself primarily to comprehensive investigations of an extracellular nuclease of Staphylococcus aureus. He and his colleagues have determined the sequence of its 149 amino acids and have described its fundamental enzymological, physical, and immunological properties. They have used an extensive range of spectroscopic and chemical techniques, including new methods of affinity labeling and cross-linking, to delineate the identity and relationship of amino acids in its active site. Dr. Anfinsen has collaborated closely with a crystallographic group at M.I.T., under Professor F.A. Cotton, which has determined the three-dimensional structure of nuclease at high resolution.
1969 Honorary Fellow, Weizmann Institute of Science, Rehovot, Israel
Leon Lecture, University of Pennsylvania
Hadassah Myrtle Leaf Award
1970 EMBO Lecture for Sweden
Visiting Fellow, All Souls College, Oxford, England
1972 Jubilee Lecture, British Biochemical Society, England
Nobel Prize in Chemistry
1973 Doctor of Science, (Honorary) University of Pennsylvania
1974 Mathers Lectures, Indiana University, Bloomington, Indiana
Feinberg Graduate School, Christian B. Anfinsen Scholarship established
Scientific Advisory Committee of Weizmann Institute Chairman
1975 Doctor of Science (Honorary), Gustavus Adolphus College - Lecture
Kempner Lectureship, University of Texas Medical Branch, Galveston, Texas
Participant, Encounter for the Universality of UNESCO, Paris
1976 Bicentennial Exhibit Chosen for 20th Century Scientist, Maryland Academy of Science
1977 Doctor of Science, (Honorary), Brandeis University
Naff Lectures, University of Kentucky, Lexington, Kentucky
1978 Doctor of Science, (Honorary), Providence College, Rhode Island
Herbert A. Sober Memorial Lectureship
Consultant to ABC Cancer Foundation
1979 Berson Memorial Lecture, Mount Sinai School of Medicine, New York City, New York
Fritz Lippmann Life Sciences Medal, Paris, France
1980 Case Institute of Technoogy, Centennial Medal
1981 Pontifical Academy of Science, The Vatican
NIH Scientist Emeritus Award
Fogarty International Symposium in honor of CBA on Contributions of Chemical Biology to Biomedical Science
1982 Doctor of Medicine, M.D. (Honorary), University of Naples, Italy
Doctor of Science, (Honorary) Yeshiva University, New York City, New York
1984 Distinguished Scientist Lectures Series, Bard College, New York
Theobald Smith Lecture Award, Albany College of Medicine, New York
1985 Hebrew University of Jerusalem Medal
1986 National Library of Medicine Medal, Bethesda, Maryland
1987 Doctor of Science (Honorary), Adelphi University, New York
1988 Genetic Engineering Lectures, Kon Kuk University, Seoul, Korea
1990 Pioneer in Science Award, Bar Ilan University, Ramat Aviv, Israel
Participant in Oslo Conference, "Anatomy of Hate", Norwegian Nobel Committee & Elie Wiesel Fund
1991 Morris Brown College Research Symposium Award, Outstanding Nobelist
University of Texas Medical Branch, Centennial Symposium Medal, Galveston, Texas
1992 Protein Folding Symposium to Honor Christian B. Anfinsen, NIH, Bethesda, Maryland
1993 Doctor of Science, University of Las Palmas, Canary Islands (Honorary)
1994 National Institutes of Health/Israel Alumni Association Lectureship established in honor of Christian B. Anfinsen, Rehovot, Israel: Memorial Biennial Lecture
Johns Hopkins University Lectureship honoring CBA established, Baltimore, Maryland
National Institutes of Health Anfinsen Lectureship established
Department of Health, Education and Welfare, Distinguished Service Medal
Department of Health, Education and Welfare, Superior Service Medal
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