| 1 | Name: | Dr. Paul D. Boyer | |
| Institution: | University of California, Los Angeles | ||
| Year Elected: | 1998 | ||
| Class: | 2. Biological Sciences | ||
| Subdivision: | 201. Molecular Biology and Biochemistry | ||
| Residency: | Resident | ||
| Living? : | Deceased | ||
| Birth Date: | 1918 | ||
| Death Date: | June 2, 2018 | ||
Paul Delos Boyer was born July 31, 1918 in Provo, Utah. He received his B.S. in chemistry from Brigham Young University in 1939 and a Ph.D. degree in biochemistry from the University of Wisconsin in 1943. He served at Stanford University with a war research project on stabilization of human serum albumin from 1943-45 and with the Naval Medical Research Institute in Bethesda, MD in 1946. From 1946-63 he was a faculty member at the University of Minnesota and from 1963 to 1999 a faculty member at the University of California, Los Angeles, becoming emeritus in 1999. In 1965 he became founding director of UCLA's Molecular Biology Institute. Dr. Boyer received the American Chemical Society Award in Enzyme Chemistry in 1955 and during that year he was a Guggenheim Fellow for studies in Sweden. He was a member of the American Academy of Arts & Sciences (1968) and the National Academy of Sciences (1970). He has received the Rose Award of the American Society of Biochemistry (1989) and honorary doctorates from the University of Stockholm (1974), the University of Minnesota (1996) and the University of Wisconsin (1998). In 1997 he shared a Nobel Prize in Chemistry with Walker and Skou for their studies with ATP (adenosine triphosphate). Throughout nature ATP serves for the capture and use of energy. Dr. Boyer also served as editor of the 18-volume treatise "The Enzymes" (1971-90) and has published over 300 papers, mostly about enzymes. About half of these relate to the mechanism of the complex membrane-bound ATP synthase. With his associates Boyer discovered that during ATP synthesis the three catalytic sites, even though they have identical amino acid sequences, proceed sequentially through strikingly different conformations. They obtained the first evidence that this occurs by a novel rotational catalysis. The rotational movement of a multi-subunit portion in the membrane drives the rotation of a single subunit in the center of the catalytic site cluster, resulting in the sequential conformational changes necessary for the binding, formation, and release of ATP. Dr. Paul D. Boyer died June 2, 2018, at the age of 99 at home in Los Angeles, California. | |||