Paul D. Boyer

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Provo, Utah
Birth Sign
Provo, Utah

Paul Boyer is an American biochemist who won the Nobel Prize in Chemistry in 1997 for his work on the enzymatic mechanism behind adenosine triphosphate production. Boyer shared the Nobel Prize with John E Walker and Jens C Skou, all of whom contributed significantly to the field. The energy that is produced and stored in plants, animals, and microbes to make life possible through the ATP synthase mechanism was identified because to Boyer’s extensive research and investigation. While plants photosynthesize light through chloroplast membranes, ATP is produced in a mitochondrial membrane inside each cell in animals. Boyer also discovered the world’s tiniest rotary machine in humans. In order to explain how ATP synthase works, Boyer proposed an unconventional mechanism. John E. Walker’s research confirmed what he called his “binding change mechanism.”

Childhood and Adolescence

Dell Delos Boyer, an osteopathic physician, and Grace Guymon had Paul Delos Boyer on July 31, 1918, in Provo, Utah. He was one of five siblings.
Boyer’s youth was marred by tragedy when his mother, a victim of Addison’s illness, died when he was only 15 years old. It was her death that inspired young Boyer to pursue a career in biochemistry.

He received his early schooling from Provo High School, where he excelled academically. He went on to Brigham Young University, where he earned a bachelor’s degree in chemistry in 1939. For his graduate studies, he was also awarded a Wisconsin Alumni Research Foundation Scholarship.

Boyer was able to pursue doctoral studies in biochemistry at the University of Wisconsin in Madison because of the scholarship. His time in Wisconsin had a big impact on him. The environment was governed by vitamin, nutrition, and metabolism research.

During his stay in the department, famous researchers achieved significant discoveries and filed numerous patents. Boyer received his doctorate in 1943.

Paul Boyer’s  Career

The country was at war when Boyer completed his Ph.D. studies. As a result, he enrolled at Stanford University to work on a war project. It ultimately came down to looking at blood plasma proteins. Concentrated serum albumin separated from blood plasma was recognized to be beneficial in the treatment of shock on the battlefield.

When heated, however, the same developed cloudiness due to protein denaturation. He created an incredibly successful stabilizing approach at Stanford.

Boyer accepted an offer for an assistant professorship at the University of Minnesota when World War II ended and the war project at Stanford was completed. He did, however, join the US Navy in the interim. He conducted private research while serving in the Navy’s Medical Research Institute in Bethesda, Maryland. He returned to civilian life in Minnesota in a few of months.

Boyer had superior biochemistry possibilities at the University of Minnesota than at Stanford. At the University of Minnesota, he launched his independent research career and established kinetic, isotopic, and chemical approaches for studying enzyme processes.

Boyer earned a Guggenheim Fellowship in 1955, which allowed him to concentrate on the mechanism of alcohol dehydrogenase at the Nobel Medical Institute with Professor Hugo Theorell.

Following his Guggenheim Fellowship, Boyer accepted a Hill Foundation Professorship, which required him to relocate to the University of Minnesota’s medical campus. He concentrated his research on enzymes rather than ATP synthase during this time.

The discovery of a new type of phosphorylated protein, a catalytic intermediate in ATP synthesis with a phosphoryl group connected to a histidine residue, was the result of a collaborative effort. They soon discovered, however, that the enzyme-bound phosphohistidine identified as an intermediary in the citric acid cycle’s substrate-level phosphorylation.

Boyer was Chairman of the American Chemical Society’s Biochemistry Section from 1959 to 1960. (ACS).
He joined the Department of Chemistry and Biochemistry at the University of California, Los Angeles (UCLA) in 1963 and has held that job ever since.

He became the Molecular Biology Institute’s Founding Director in 1965, spearheading the building’s construction and the establishment of an interdepartmental Ph.D. program.
Between 1969 and 1970, he served as President of the American Society of Biological Chemists for a year.

Despite his administrative responsibilities, Boyer did not allow his research to be hampered by his institutional duty. He studied how cells made ATP during the 1950s decade. He discovered that energy is an essential source of life for plants and animals and that energy is stored and transmitted by a specific molecule. Boyer started looking at how cells made ATP.

While Boyer was researching how cells make ATP, a process that takes place in animal cells in a structure called a mitochondrion, a British chemist named Peter Mitchell independently demonstrated 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.

A later study by Boyer focused on the steps involved in ATP production. He showed how the enzyme used the energy generated by the hydrogen flow to make ATP from adenosine diphosphate (ADP) and inorganic phosphate. He came up with a theory to explain the action of ATP synthase that explained an uncommon mechanism.

Boyer was the editor of the Annual Review of Biochemistry from 1963 to 1989. He was Editor of the renowned series ‘The Enzymes’ during his stay there. Meanwhile, he worked at UCLA as a Faculty Research Lecturer in 1981.
He was named Professor Emeritus of the Molecular Biology Institute, which he helped found, in 1990.

Paul’s Major Projects

Boyer’s most important contribution was his explanation of the enzymatic process underpinning adenosine triphosphate production. While he began researching how cells made ATP in the 1950s, he later narrowed his focus to what is involved in ATP synthesis.

His research centered on the enzyme ATP synthase, and he established how the enzyme uses the energy supplied by hydrogen flow to convert ADP and inorganic phosphate into ATP. To explain how ATP synthase worked, Boyer proposed an odd mechanism known as the binding change mechanism.

Achievements and Awards

He won the Paul Lewis Award in Enzyme Chemistry in 1955. He received the American Chemical Society Award and a Guggenheim Fellowship in Sweden in the same year.
He won the UCLA McCoy Award in 1976.
The American Chemical Society’s Southern California Section awarded him the coveted Tolman Medal in 1981.

The American Society for Biochemistry and Molecular Biology awarded him the Rose Award in 1989.
Boyer was awarded the Nobel Prize in Chemistry in 1997 for his discovery of the enzymatic process behind the creation of adenosine triphosphate (ATP). He and John E Walker split the award equally. Jens C Skou received the second part of the award for discovering Na+/K+ ATPase.

The UCLA Medal, the American Academy of Achievement Golden Plate Award, the American Philosophical Society Award, and the UCLA Seaborg Award were all given to him in 1998.
He was elected to the National Academy of Sciences and the American Academy of Arts and Sciences.

Several universities have awarded him honorary doctorates, including the University of Stockholm, the University of Minnesota, and the University of Wisconsin.

Personal History and Legacy

After graduating from Provo High School, Boyer married Lyda Whicker. Gail Boyer, Alexander Boyer, and Douglas Boyer are the couple’s three children. They have eight grandchildren between them.

Boyer currently lives in the hills north of UCLA with his family, where he does his research and studies.
In 1999, a hall at UCLA was named after Boyer to honor his contributions to science. The Paul D. Boyer Hall was named after him and is now well-known.

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