Paul Boyer received the Nobel Prize in Chemistry in 1997 quite late in his career; he was 79 years old at the time and had focused on research in enzymes for nearly fifty years. He is currently a professor emeritus of the University of California, Los Angeles, where he has worked since 1963.
The motivation for awarding the Nobel Prize was for the “elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)”, and the central theme of Boyer’s lecture given in Lindau is the description of ATP and the enzyme responsible for its synthesis, ATP synthase, including an overview of experiments on ATP synthase using the oxygen isotope 18O.
ATP is an energy-carrying molecule, produced in mitochondria, or “the powerhouses of the cell” as a result of metabolic processes (photosynthesis in plants, oxidation in aerobic organisms and fermentation or anaerobic respiration in anaerobic organisms). The production of ATP is the most common chemical reaction in the world, and according to Boyer’s calculations, “an active individual will turn over a body weight of ATP a day”. The mushroom-like diagram of ATP synthase is known to anyone who has studied biochemistry in high school or university. The enzyme is embedded in the mitochondrial membrane, capturing the energy from the protons travelling through the synthase into the three catalytic sites to make the ATP compound.
Many years of research have not diminished Boyer’s profound admiration of the ATP molecule and he claims ATP to be “the best”; “DNA is a wonderful molecule but in terms of total properties I feel it takes a second seat to the protein molecule.”
Boyer also comments on the three reasons for which he believes he obtained the Nobel Prize; life – or a passion for science and the explanation of living processes; luck – his team could have worked equally hard on an enzyme that didn’t have the wonderful features of rotational catalysis; and longevity – he outlived all his competitors!
By Hanna Kurlanda-Witek