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Energy, Life, and ATP by Paul D. Boyer Created 2026-10-24 Updated 2026-10-31
By Paul D. Boyer. Nobel lecture (1997): www.nobelprize.org/uploads/2018/06/boyer-lecture.pdf
The lecture describes binding changes, catalytic-site occupancy and coupling in ATP synthase.
Paul D. Boyer Created 2026-10-24 Updated 2026-11-05
Paul D. Boyer developed a binding-change mechanism for ATP synthase. Different conformations of catalytic sites bind substrates, form ATP, and release it at different stages of the cycle.
This connects mechanical coupling with catalysis: rotation changes the state of a catalytic site rather than requiring an identical chemical environment at every moment.[ref]
https://www.nobelprize.org/prizes/chemistry/1997/summary/. Official prize account: enzymatic mechanism underlying ATP synthesis
Biochemist (1918–2018), recognized for elucidating the enzymatic mechanism of ATP synthase.
Portrait of Paul D. Boyer
. GBHayes. CC BY-SA 4.0, via Wikimedia Commons. Source.