Paul D. Boyer
Paul D. Boyer
Paul Delos Boyer was born July 31, 1918, in Provo, Utah. He received a B.S. degree in chemistry from Brigham Young University in 1939 and obtained a Wisconsin Alumni Research Foundation Scholarship for graduate studies. Five days before leaving for Wisconsin, Paul married a beautiful and talented coed, Lyda Whicker. Together they have three children, Gail, Hali and Douglas, and eight grandchildren.
After he received his Ph.D. degree in Biochemistry from the University of Wisconsin in 1943, he spent years at Stanford University on a war-related research project dedicated to stabilization of serum alubumin for transfusions. He began his independent research career at the University of Minnesota and introduced kinetic, isotopic, and chemical methopds for investigating enzyme mechanisms. In 1955, he received a Guggenheim Fellowship and worked with Professor Hugo Theorell on the mechanism of alcohol dehydrogenase. In 1956, he accepted a Hill Foundation Professorship and moved to the medical campus of the Universithy of Minnesota. In 1959-60, he served as Chairman of the Biochemistry Section of the American Chemical Society and in 1969-70 as President of the American Society of Biological Chemists.
Since 1963, he has been a Professor in the Department of Chemistry and Biochemistry at UCLA. in 1965, he became the Founding Director of the Molecular Biology Institute and spearheaded the construction of the building and the organization of an interdepartmental Ph.D. program. This institutional service did not diminish the creativity and originality of his research program, which led to three postulates for the binding mechanism for ATP synthesis: i.e. that energy input was not used primarily to form ATP but to promote the binding of phosphate and mostly the release of tightly bound ATP; that three identical catalytic sites went through compulsory, sequential binding changes; and that the binding changes of the catalytic subunites, circularly arranged on the periphery of the enzyme, were driven by the rotation of a smaller internal subunit.
Paul Boyer was Editor or Associate Editor of the Annual Review of Biochemistry from 1963-89. He was Editor of the classic series, The Enzymes. In 1981, he was Faculty Research Lecturer at UCLA. He received the Rose Award of the American Society of Chemistry and Molecular Biology in 1989; Honorary doctorates from the Universities of Stockholm (1974), Minnesota (1996), and Wisconsin (1998); and the Nobel Prize in Chemistry in 1997.
Basic Features of the ATP Synthase Catalysis The membrane-bound ATP synthase of animals, plants, and microorganisms is a highly conserved enzyme with unusual subunit stoichiometry and properties. In the binding change mechanism for the synthase developed by our laboratory, translocation of protons is regarded as driving conformational changes that promote release of a tightly bound ATP at one catalytic site and the tight binding of ADP and Pi at another catalytic site. An interesting speculation is that catalysis is accompanied by a rotational movement of catalytic subunits relative to a noncatalytic core.
Probes of Catalysis and Controls We use a combination of chemical derivatization, nucleotide binding and other catalytic site occupancy measurements, conformational and structural probes, subunit isolation and interchange evaluations, subunit cross-linking 18 O-phosphate exchange measurements, site-specific mutagenesis, and rapid mixing and rate of catalysis approaches. One example is the use of 2-azido ATP and ADP. These are good substrates that when photoactivated covalently modify nucleotide binding sites. Another is the phosphate oxygen exchange methodology that reveals reactions occurring while substrates are still bound and whether the catalysis occurs by one of more pathways.
1997 Nobel Prize in Chemistry
Rose Award of the American Society of Biochemistry and Molecular Biology
National Academy of Sciences