= Paul D. Boyer
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<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.https://www.nobelprize.org/prizes/chemistry/1997/summary/[Official prize account: enzymatic mechanism underlying ATP synthesis]{ref}
Biochemist (1918–2018), recognized for elucidating the enzymatic mechanism of <ATP synthase>.
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{title=Portrait of <Paul D. Boyer>}
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