Paul D. Boyer (born July 31, 1918, Provo, Utah, U.S.—died June 2, 2018, Los Angeles, California) was an American biochemist who, with John E. Walker, was awarded the Nobel Prize for Chemistry in 1997 for their explanation of the enzymatic process involved in the production of the energy-storage molecule adenosine triphosphate (ATP), which fuels the metabolic processes of the cells of all living things. (Danish chemist Jens C. Skou also shared the award for separate research on the molecule.)
After receiving his doctorate in biochemistry in 1943 from the University of Wisconsin, Boyer held a number of teaching positions before joining the faculty of the University of California at Los Angeles in 1963. There he served as professor (1963–89) and director of the Molecular Biology Institute (1965–83) before being named professor emeritus in 1990.
In the early 1950s Boyer began to research how cells form ATP, a process that occurs in animal cells in a structure called a mitochondrion. In 1961 the British chemist Peter D. Mitchell showed that the energy required to make ATP is supplied as hydrogen ions flow across the mitochondrial membrane down their concentration gradient in an energy-producing direction. (For this work Mitchell won the 1978 Nobel Prize for Chemistry.) Boyer’s later research revealed more specifically 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 postulated an unusual mechanism to explain the way in which ATP synthase functions. Known as his “binding change mechanism,” it was partially confirmed by Walker’s research.