Born In: Provo, Utah, United States
Paul Boyer was an American biochemist who was bestowed with the Nobel Prize in Chemistry in 1997, for his research on the enzymatic mechanism underlying the synthesis of adenosine triphosphate. Boyer shared his Nobel Prize with John E Walker and Jens C Skou who independently carried out important work in the field. It was due to Boyer’s intensive research and investigation that the energy that is produced and stored in plants, animals and bacteria making life possible through ATP synthase mechanism, was discovered. While plants photosynthesize the lights through the membranes in chloroplast, in animals the ATP is located in a membrane of mitochondria inside each cell. Boyer also discovered the tiniest rotary machine known to exist in humans. Boyer postulated an unusual mechanism to explain the way in which ATP synthase functions. Known as his ‘binding change mechanism’, it was confirmed by John E. Walker’s research.
Born In: Provo, Utah, United States
Also Known As: Paul Delos Boyer
Died At Age: 99
Spouse/Ex-: Lyda Whicker
children: Gail Boyer Hayes
Born Country: United States
place of death: Los Angeles, California, U.S.
U.S. State: Utah
awards: 1997 - Nobel Prize in Chemistry
1955 - Guggenheim Fellowship for Natural Sciences
US & Canada
1989 - William C. Rose Award
Paul Delos Boyer was born on July 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 fifteen. It was her death that propelled young Boyer’s interest in studying biochemistry.
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.
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.
In 1963, he took up professorship at the Department of Chemistry and Biochemistry at the University of California, Los Angeles (UCLA).
Despite administrative duties, Boyer did not let his institutional service come in way of his research work. Through the decade of 1950s, he worked on how cells formed ATP. He had realized that energy was a vital source of life and that energy is stored and transported by a special molecule in plants and animals. Boyer began to research on how cells formed ATP.
While Boyer was investigating as to how cells formed ATP, a process that occurs in animal cells in a structure called a mitochondrion, a British chemist Peter Mitchell independently 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
Boyer’s later work emphasized what is involved in ATP synthesis. Through it, he demonstrated how the enzyme harnessed the energy produced by the hydrogen flow to form ATP out of adenosine diphosphate (ADP) and inorganic phosphate. He came up with a hypothesis that explained an unusual mechanism to explain the way in which ATP synthase functioned.
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.
In 1997, Boyer received the prestigious Nobel Prize in Chemistry for elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP). He shared one-half of the prize with John E Walker. The second half was presented to Jens C Skou for his discovery of Na+/K+ ATPase.
Boyer married Lyda Whicker just after finishing studies at Provo High School. The couple were blessed with three children, Gail Boyer, Alexander Boyer and Douglas Boyer. He had eight grandchildren.
Boyer resided with his family home in the hills, north of UCLA, where he conducted his research and studies.
Paul D. Boyer died on June 2, 2018, due to respiratory failure. He was 99.
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