Paul D. Boyer, 99, Dies; Nobel Winner Studied What Makes the Body Go
Posted June 7, 2018 5:48 p.m. EDT
Paul D. Boyer, a molecular biologist who shared the 1997 Nobel Prize in chemistry for his contributions to understanding the way all living organisms get energy from their environments and process it to sustain life and fuel their activities, died Saturday at his home in Los Angeles. He was 99.
His death was confirmed by his daughter Alexandra Boyer.
A professor emeritus at the University of California, Los Angeles, where he taught chemistry and conducted research for more than 50 years, Boyer devoted his career to the study of enzymes, those mysterious proteins that power biochemical processes in the cells of plants and animals.
Building on the work of other scientists and his own decades of research, Boyer deciphered the mechanics of the enzyme ATP (adenosine triphosphate), the link in every cell that acts like a tiny motor, chemically capturing energy from its surroundings and releasing it as mechanical energy for life to run on.
In a series of 20th-century discoveries, scientists had learned that ATP was the universal carrier of cell energy; that plants and animals created it naturally, although it could be made in a lab; that its structure consisted of a rotating wheel, an attached axle jutting up from its center and at the top of the axle a fixed cylinder, each carrying its own sets of proteins; and that ATP was created and released by the interactions of proteins on the wheel, axle and cylinder.
What Boyer discovered was the underlying mechanism for ATP formation and the true function of the catalyst ATP synthase. With wheel and axle rotating together like a turbine, he said, protein on the outside of the axle brushed catalytic sites inside the cylinder and produced a sequence of changes, making the catalyst ATP synthase and then ATP itself in the form of tightly bound molecules.
Boyer’s revolutionary insight, which he called the “binding change mechanism,” was to recognize that ATP synthase was not primarily used to form the tightly bound ATP molecules themselves, but to release the energy in ATP for use in all of life’s tasks: movement, breathing, growing — and building more proteins to keep the ball of life rolling.
“The concepts of Boyer’s binding change mechanism helped to clarify the basic chemistry of life on earth, what makes life ‘go,'” the University of Minnesota, where Boyer began his research, said in a statement after he won the Nobel. “They illuminated a greater understanding of the beautiful complexity of the world around — and within — us all.”
Paul Delos Boyer was born on July 31, 1918, in Provo, Utah, one of six children of Dr. Dell Boyer, an osteopathic physician, and Grace Guymon Boyer, a homemaker. His mother’s death, from Addison’s disease, when he was 15 contributed to his interest in biochemistry.
Boyer grew up in a nonpracticing Mormon family, attended Provo High School and earned a bachelor’s degree in chemistry from Brigham Young University in 1939 and a doctorate in biochemistry from the University of Wisconsin in 1943.
Besides his daughter Alexandra, he is survived by his wife, Lyda (Whicker) Boyer, whom he married in 1939; another daughter, Gail Boyer Hayes; eight grandchildren; and six great-grandchildren. A son, Douglas, died in 2001. From 1943 to 1945, Boyer worked on war-related research at Stanford University, studying ways of stabilizing solutions of serum albumin for battlefield blood transfusions. He then joined the University of Minnesota, and for the next 18 years he taught biochemistry there and began his independent research on enzymes.
He also built his own home in St. Paul, working as contractor, plumber, electrician and carpenter. “My warm memories of this home include looking at a sparkling, snow-covered landscape while seated at the desk in the bedroom corner that served as my study, and struggling with the interpretation of some puzzling isotope exchanges accompanying enzyme catalysis,” he recalled in his Nobel Prize autobiography.
In 1963, Boyer moved to UCLA as a chemistry professor. He soon became director of the university’s new Molecular Biology Institute and directed its biochemistry program from 1983 to 1989. He also edited the Annual Review of Biochemistry. In 1990 he was named professor emeritus of chemistry and biology.
His research on ATP began in the late 1950s, focusing on the role of ATP synthase in creating new ATP. He proposed his binding change mechanism in the early 1970s. It closely resembled what is now accepted knowledge, although ATP’s complete structure was then still unknown and much work by Boyer and others remained before the Royal Swedish Academy of Sciences cited his model for a Nobel Prize in 1997.
Boyer shared half the prize with British biochemist John E. Walker, who independently established ATP’s structure and substantiated Boyer’s model of its mechanics. The other half went to Jens C. Skou of Aarhus University in Denmark for discovering the enzyme that maintains the balance of sodium and potassium ions in cells. The prize recipients also shared an accompanying $1 million.
Skou died on May 28 at 99.
In January 2003, Boyer was among 41 Nobel laureates in science and economics who issued a declaration opposing a preventive U.S. war against Iraq without wide international support, saying that even a victory “would undermine, not protect, U.S. security and standing in the world.”
Boyer received many honors, including the Rose Award from the American Society of Chemistry and Molecular Biology in 1989. While his work opened new fields of study in biochemistry, molecular biology and nutrition, it was never easy to explain to laymen without metaphors.
“Imagine trying to repair a TV if you didn’t know how it worked,” he said in an interview with The New York Times on the day his Nobel was announced. “This tells you how the machinery of the cell works.”