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Paul D. Boyer
1918–2018 · United States · 20th century
Nobel Chemistry 1997
American biochemist at UCLA who unravelled how the molecular machine ATP synthase makes the cell’s energy currency.
Nobel Prize work
Boyer proposed the binding-change mechanism for ATP synthase: the enzyme’s catalytic sites cycle through tight, loose and open conformations, driven by rotation of a central shaft powered by the proton gradient. This rotary model of the cell’s energy machine earned him a share of the 1997 Nobel Prize in Chemistry with John Walker.
Fields
Related topics
Enzymes and enzyme kinetics
Enzymes accelerate reactions by lowering the activation free-energy barrier; they do not change the equilibrium constant.
Metabolism (glycolysis, Krebs cycle, electron transport chain)
Metabolism is a network of linked reactions that captures energy and supplies building blocks; ATP and reduced cofactors connect pathways.