Paul D. Boyer

Boyer married Lyda Whicker just after finishing studies at Provo High School. The couple is blessed with three children, Gail Boyer, Alexander Boyer and Douglas Boyer. They have eight grandchildren.

Currently, Boyer resides at his family home in the hills north of UCLA, where he conducts his research and studies.

In 1999, a hall in UCLA was dedicated to Boyer to mark his legacy in scientific world. It was named after him and is today widely known as the Paul D. Boyer Hall.

Paul Delos Boyer was born on Jul 31, 1918 in Provo, Utah, to Dell Delos Boyer, an osteopathic physician, and Grace Guymon. He had five siblings.

Tragedy struck Boyer’s childhood early as his mother, who was a victim of Addison’s disease breathed her last in 1933, when he was just 15. It was her death that propelled young Boyer’s interest in studying biochemistry.

Academically good, he attained his early education from Provo High School. Later, he enrolled at the Brigham Young University from where he received a BS degree in chemistry in 1939. He also received a Wisconsin Alumni Research Foundation Scholarship for graduate studies.

The scholarship allowed Boyer to take up graduate studies in biochemistry in the University of Wisconsin in Madison. His years at Wisconsin were very influential. Research on vitamins, nutrition and metabolism ruled the environment. Several discoveries were made and numerous patents were done during his time of study by prominent researchers at the department. In 1943, Boyer gained his Ph.D. degree.

At the time when Boyer finished his doctorate studies, the nation was at war. Consequently, he took up a war project at Stanford University. It basically involved studying blood plasma proteins. It was known that concentrated serum albumin fractionated from blood plasma was effective in battlefield treatment of shock. But the same when heated, developed cloudiness from protein denaturation. At Stanford, he developed a stabilization method that was extremely successful.

Following the end of World War II and completion of the war project at Stanford, Boyer accepted an offer for the position of assistant professorship at the University of Minnesota. However, in between, he became a member of the US Navy. He served in the Navy’s Medical Research Institute in Bethesda, Maryland where he carried out private research. In a matter of months, he returned to civilian life at Minnesota.

University of Minnesota offered Boyer better opportunities in biochemistry than Stanford did. He began his independent research career at the University of Minnesota and introduced kinetic, isotopic, and chemical methods for investigating enzyme mechanisms.

In 1955, Boyer received a Guggenheim Fellowship which gave him the opportunity to work with Professor Hugo Theorell on the mechanism of alcohol dehydrogenase at the Nobel Medical Institute.

Following his Guggenheim Fellowship, Boyer accepted a Hill Foundation Professorship that caused him to move to the medical campus at the University of Minnesota. During this period, he carried out the research work on the enzymes rather than ATP synthase. A combined work led to the discovery of a new type of phosphorylated protein, a catalytic intermediate in ATP formation with a phosphoryl group attached to a histidine residue. However, they soon discovered that the enzyme-bound phosphohistidine discovered was an intermediate in the substrate level phosphorylation of the citric acid cycle.

Boyer’s most significant work came when he explained the enzymatic mechanism underlying the synthesis of adenosine triphosphate. While in the 1950s he began research of how cells formed ATP, later he focussed his research to find out what is involved in ATP synthesis. His work focused on the enzyme ATP synthase, and he demonstrated how the enzyme harnesses the energy produced by the hydrogen flow to form ATP out of adenosine diphosphate (ADP) and inorganic phosphate. Boyer came up with an unusual mechanism, known as the binding change mechanism, to explain how ATP synthase functioned.