US biochemist who with English chemist John Walker and Danish biophysicist Jens C Skou shared the Nobel Prize for Chemistry in 1997 for their explanation of the enzymatic process that produces adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate.
Boyer proposed his ‘binding change mechanism’ to explain the mechanisms required for the formation of ATP, the source of chemical energy in the cells of a living organism. The function of an enzyme is to catalyse the chemical reactions in living organisms. The majority of enzymes bind and release the component parts of a required molecule at the same time, with the overall catalytic reaction requiring energy to work. ATP molecules provide this energy. However, the mechanism for the formation of ATP molecules themselves was not known. Boyer suggested that the energy requiring step was not the synthesis of ATP from ADP and inorganic phosphate, but was the binding of the catalytic enzyme, ATP synthase, to the ADP and inorganic phosphate molecules. Boyer went on to clarify the mechanism for this reaction and proposed the type of molecular structures that were required for his mechanism to work. Clarification of the three-dimensional structure of the enzyme carried out by English chemist John Walker confirmed Boyer's findings. Their work has significantly increased our understanding of how chemical reactions work in living organisms.
Boyer was born in Provo, Utah, USA. He received his PhD in biochemistry from the University of Wisconsin in 1943. He became professor of chemistry at the University of California at Los Angeles (UCLA) in 1963 and retained this position until 1989. He was the director of the Molecular Biology Institute at UCLA 1965–83 and in 1990 and became professor emeritus at the department of chemistry and biology at UCLA. He has been a member of the Academy of Sciences since 1970.
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A ribonucleoside with one or more phosphate groups esteri-fied to the 5’ position of the sugar moiety. See nucleic acid.