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Boyer, Paul Delos

Paul Delos Boyer

American biochemist Paul D. Boyer (born 1918) is the co–recipient of the 1997 Nobel Prize for Chemistry. He received his share of the award for explaining the enzymatic mechanism that underlies the synthesis of adenosine triphosphate (ATP), which fuels the metabolic processes of the cells of all living things. Boyer's Nobel recognition was the culmination of a long and fruitful research career that explored the biochemical processes affecting life.

Future Nobel Laureate Paul Delos Boyer was born July 31, 1918, in Provo, Utah, the son of Dell Boyer, an osteopathic physician, and Grace Guymon Boyer. Boyer spent the first 21 years of his life in Provo. At the time of his birth, the city had only 15,000 residents, as Mormon pioneers had settled the area only 70 years before. Both family and environment exerted a powerful influence on his early life. "I was fortunate, as a middle child in a family of six children, to have a loving mother and father and a nice home in the attractive Mormon community of Provo, Utah," he wrote in a 1997 article for Freethought Today magazine.

Early Life Influenced Career Direction

Boyer's father descended from the Boyers of Pennsylvania, who themselves came from Bayer ancestry in what is now Holland and Germany. Grace Boyer's family descended from the Huguenots who fled religious persecution in France. Boyer recalled in the autobiographical essay he wrote when he won the Nobel Prize in 1997 that his father taught by example the qualities of "logical reasoning, compassion, love of others, honesty, and discipline applied with understanding."

Boyer described his mother as possessing "vitality and charm," but these qualities were later diminished by Addison's disease. Grace Boyer died in 1933, at the age of 45, shortly after Paul Boyer turned fifteen. Boyer later revealed that her death contributed to his later interest in biochemistry. Boyer's father remarried and later succumbed to prostate cancer at the age of 82.

As a child, Boyer and his siblings were encouraged to be creative. One year for Christmas, he received a chemistry set. At night, he entertained himself with books read by the fireplace. When he was 12, Boyer became a Deacon in the Mormon Church, which allowed him to pass out the Eucharist. Religion, however, was not strictly emphasized in the Boyer household. (In fact, later in life, Boyer would forsake all religion and become an avowed atheist).

Boyer received an excellent primary and secondary education at Provo public schools. He excelled in his studies and was able to skip a grade and enter junior high school early. In high school, he participated on the debate team and in student government and was named senior class president. He was only sixteen years old when he graduated.

Obtained Graduate Scholarship

Boyer received a bachelor of sciences degree in chemistry from Brigham Young University in 1939 and then obtained a Wisconsin Alumni Research Foundation (WARF) Scholarship for graduate studies. "Dedicated teachers stimulated my interest in learning and I began to acquire an expanding understanding of science," he wrote in Freethought Today magazine. "Without my recognizing it, I was becoming one of the many who found education in the sciences, and not religion, was providing me with what might be called my philosophy of life."

On August 31, 1939, five days before he left Utah to fulfill his WARF scholarship, Boyer married Lyda Whicker. He was 21 and she was 20.

In Wisconsin, Boyer was stimulated by the scientific environment provided by the university's biochemistry department. At the time, the department was more advanced than other departments in the country, and a new wing had been added where researchers conducted new and exciting studies on vitamins, nutrition and metabolism. Boyer was assigned to work with Professor Paul Phillips whose research focused on reproductive and nutritional problems of farm animals. Boyer's own research included metabolic and enzyme interests. At the university, Boyer would obtain a master of science degree (1941) and a Ph.D. (1943).

Participated in Wartime Project

After earning his Ph.D., Boyer went to Stanford University in California, where he became involved in a wartime project sponsored by the Committee on Medical Research. Boyer worked on blood plasma proteins under the direction of J. Murray Luck, founder of the nonprofit Annual Review of Biochemistry. Project researchers focused on the stabilization of serum albumin for blood transfusions. Concentrated serum albumin taken from blood plasma was effective in the treatment of shock on the battlefield. The problem with the fractionation process was that when the albumin solution was heated to destroy microorganisms and viruses, it would turn cloudy because of the denaturation, or breakdown, of the protein. During the course of their work, Boyer and fellow researchers discovered that long chain fatty acids would effectively stabilize serum albumin to the heat denaturation and would even reverse the denaturation by heat or concentrated urea solutions. This stabilization method was soon implemented and is still used today.

After the project, Boyer accepted a position as an assistant professor at the University of Minnesota in Minneapolis. He was attracted to the institution because of its fine biochemistry department. His plans were delayed, however, when he was drafted into the U.S. Navy in 1945. But the war was almost over, and Boyer spent most of his time in laboratory at the Navy Medical Research Institute in Bethesda, Maryland. In less than a year, he was a civilian again.

Boyer returned to the University of Minnesota and began the independent research phase of his career. His early work resulted in the introduction of kinetic, isotopic, and chemical methods for investigating enzyme mechanisms. Boyer described this period as a "golden era for biochemistry," as National Institute of Health and National Science Foundation grants were increasing. In Boyer's field this sparked new discoveries about metabolism, enzyme action, and protein structure and function.

Received Research Fellowships and Professorships

In 1955, Boyer received a Guggenheim Fellowship in Sweden and worked with Nobel Prize–winning scientist Axel Hugo Theorell at the Nobel Medical Institute, researching the mechanism of alcohol dehydrogenase. He also conducted research at the Wenner–Gren Institute of the University of Stockholm with scientists Olov Lindberg and Lars Ernster. That same year, Boyer received the Award in Enzyme Chemistry of the American Chemical Society.

He returned to America the following year, when he accepted a Hill Foundation Professorship and moved to the medical campus of the University of Minnesota. Boyer was part of a research group that focused on enzymes other than the ATP synthase as well as trying to solve how oxidative phosphorylation occurred. Boyer described this as one of the most challenging problems of biochemistry. Eventually, the researchers (which included scientists, graduate students, and post–doctorate researchers) discovered a new kind of phosphorylated protein, a catalytic intermediate in ATP formation with a phosphoryl group attached to a histidine residue.

Developed ATP Postulates

For one year (1959–60), Boyer served as chairman of the biochemistry section of the American Chemical Society. Then, in 1963, his 17–year association with the University of Minnesota came to an end when he became a professor in the department of chemistry and biochemistry at the University of California in Los Angeles (UCLA). Working with a group of graduate students and post–doctorates, Boyer helped open laboratories in the chemistry building. Their work soon proved fruitful. "We soon found that the enzyme–bound phosphohistidine we had discovered was an intermediate in the substrate level phosphorylation of the citric acid cycle," recalled Boyer.

In 1965, Boyer founded the Molecular Biology Institute and led the construction of the building and the organization of an interdepartmental Ph.D. program. Despite a growing set of administrative responsibilities, Boyer still continued his own research on oxidative phosphorylation, and this led to his most important discoveries: three postulates for the binding mechanism for ATP synthesis.

These postulates, developed in the 1970s and 1980s, stated that energy input was not used primarily to form the ATP molecule but to promote the release of and already–formed and tightly bound ATP; that three identical catalytic sites went through compulsory, sequential binding changes; and that the binding changes of the catalytic subunits, circularly arranged on the periphery of the enzyme, were driven by the rotation of a smaller internal subunit.

Received Nobel Prize

Boyer's research career culminated in being awarded a Nobel Prize. In 1997, Boyer shared that year's Nobel Prize in Chemistry with Dr. John E. Walker of the Medical Research Council Laboratory of Molecular Biology at Cambridge in England, and with Jens C. Skou, professor at Aarhus University in Denmark. The three scientists were recognized for their pioneering discoveries related to adenosine triphosphate, or ATP, the compound that stores and transfers energy in living cells. Boyer and Walker were recognized for promoting understanding of ATP synthesis. Skou was recognized for discovering the enzyme that regulates the concentration of sodium and potassium in cells.

Other Achievements

In addition to his research activities, Boyer served as editor or associate editor of the Annual Review of Biochemistry from 1963 to 1989. He also wrote or co–wrote more than 200 scientific papers in biochemistry and molecular biology. In 1970, Boyer embarked on a long project when he completed the first of what would turn out to be an 18–volume series on enzymes. The complete work, entitled Enzymes became a classic in the field, and Boyer was assisted by his wife, who helped edit the volumes.

Throughout his career, Boyer has received many awards for his scientific achievements. In addition to his Nobel prize, Boyer has received the Rose Award of the American Society of Chemistry and Molecular Biology in 1989; the UCLA Medal in 1998; and honorary doctorates from the University of Stockholm (1974); the University of Minnesota (1996); and the University of Wisconsin (1997). He was elected to the American Academy of Arts and Sciences in 1968 and to the National Academy of Sciences in 1970. In 1969–70, he served as President of the American Society of Biological Chemists.

Writing in Freethought Today magazine, he said that the "study of life processes has given me a deep appreciation for the marvel of the living cell. The beauty, the design, and the controls honed by years of evolution, and the ability humans have to gain more and more understanding of life, the earth and the universe, are wonderful to contemplate. I firmly believe that our present and future knowledge of all that we are and what surrounds us depends on the tools and approaches of science."

When Boyer assumed his Professor Emeritus status at UCLA, he continued working from an office on the university campus. In addition, he maintains an active role in his area of research. In recent years, he has traveled across the globe with his wife, who he describes as a "travelophilic." Together, they attend scientific conferences and visiting researchers in their home laboratories.

The Boyers make their home in California, just north of the UCLA campus, in a house the Paul Boyer built when he first came to the university. The Boyers raised three children: daughters Gail and Hali and son Douglas. In 2003, they had eight grandchildren.

On Science and Religion

Looking to the future, Boyer feels the most critical problem facing humanity is the prospect for its survival. "In my less optimistic moments," he wrote in nobelprize.org, "I feel that we will continue to decimate the environment that surrounds us, even though we know of our folly and of what has happened to others. Humans could become quite transient occupants of planet earth. The most important cause of our problem is over–population, which nature, as with other species, will deal with severely."

The most problematic barriers to the survival of the species, he believes, are posed by political and religious leaders. As he relates in his autobiography essay on the Nobel Prize website, "I hear the cry from capable environmental leaders and organizations for movement toward sustainable societies. They are calling for sensible approaches to steer us away from impending disaster. But their voices remain largely unheard as those with power, and those misled by religious or nationality concerns, become immersed in unimportant, self–centered and short range pursuits," he wrote.

As an atheist, Boyer promotes science over religion in his autobiography. "It is disappointing how little the understanding that science provides seems to have permeated into society as a whole," he commented. "All too common attitudes and approaches seem to have progressed little since the days of Galileo. Religious fundamentalists successfully oppose the teaching of evolution, and by this decry the teaching of critical thinking. We humans have a remarkable ability to blind ourselves to unpleasant facts. This applies not only to mystical and religious beliefs, but also to long–term environmental consequences of our actions."

Online

"Biography of Paul D. Boyer," UCLA Department of Chemistry and Biochemistry, http://www.chem.ucla.edu/dept/alumni/Boyer–bio.html (December 29, 2004).

Boyer, Paul D., "A Path to Atheism," Freethought Today, http://www.ffrf.org/fttoday/2004/march/?ft=boyer (December 29, 2004).

"Paul D. Boyer," Nobel Prize Winning Chemist, http://www.sanbenito.k12.tx.us/district/webpages2002/judymedrano/Nobel%20Winners/paul–d–boyer.htm (December 29, 2004).

"Paul D. Boyer," The Free Dictionary, http://encyclopedia.thefreedictionary.com/Paul%20D.%20Boyer (December 29, 2004).

"Paul D. Boyer–Autobiography," Nobelprize.org, http://nobelprize.org/chemistry/laureates/1997/boyer–autobio.html (December 29, 2004).

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Boyer, Paul D.

Boyer, Paul D. (born 1918) American biochemist; Nobel Prize 1997, for elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP).

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