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A brief history of ATP synthase research

ATP was discovered by chemist Karl Lohmann.

Vladimir Engelhart  noted that muscle contractions require ATP.

Herman Kalckar established that ATP synthase is linked with cell respiration.
ATP had been considered to be the final product of catabolyc reactions.
(Kalckar, H. (1937) Enzymologia 2, 47-52.)

Term oxidative phosphorylation introduced
(Belitser, V.A., & Tsibakova, E.T. (1939) Biokhimiia 4, 516-535.)

Fritz Lipmann  shown that ATP is the main bearer of chemical energy in the cell. He coins the phrase "energy-rich phosphate bonds".

Alexander Todd synthesised ATP chemically.

Slater formulated a scheme involving chemical intermediates to explain the mechanism of oxidative phosphorylation
Slater, E.C. (1953) Nature 172, 975-978.

Coupled oxidative phosphorylation was shown to be activated by a soluble factor in bacterial particulate.
(Brodie, A.F., and C.T. Gray (1956) Biochim. Biophys. Acta, 19, pp 384-389)

Soluble adenosine triphosphotase was shown to participate in oxydative phosphorylation
(Penefsky H.S., E.P. Maynard, D. Anima, and E. Racker (1960) JBC 235 pp. 3330-3336)

R.J.P. Willams suggests that there was no energy-rich intermediate, but protons served to deliver energy from respiration chain enzymes and photosynthetic proteins  to ATP synthase.
(Williams, R.J.P. (1961) J. Theor. Biol. 1, 1-17)
Peter Mitchell published his chemiosmotic  hypothesis, postulating the primary role of membranes that separate two compartments, and, therefore, maintain a gradient of proton activity generated by respiration chain enzymes and used by ATP synthase.
(Mitchell, P. (1961) Nature 199, 144-148.)
Soluble adenosine triphosphotase (F1) was isolated by Ephraim Racker.

Paul D. Boyer proposed that ATP is synthesised through structural changes in the ATP synthase enzyme.

Paul D. Boyer 's group: the step in ATP synthesis which requires energy is the release of ATP from the enzyme.

Binding change mechanism of catalysis proposed in Paul D. Boyer's group.

John E. Walker's lab:  the DNA sequence of the genes encoding the proteins in ATP synthase was determined.

The first X-ray structure of F1 (lacking delta, epsilon and part of the gamma subunit) resolving individual aminoacid residues is determined by Walker and co-authors.

M. Yoshida's lab: direct observation of the rotation in F1 during ATP hydrolysis.

The Nobel prize in chemistry awarded to Paul D. Boyer and John E. Walker "for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)" and to Jens C. Skou "for the first discovery of an ion-transporting enzyme, Na+, K+ -ATPase"

Mechanically driven ATP synthesis by F1-ATPase was demonstrated by H. Itoh et al. - the first accomplishment of an endergonic chemical reaction being driven by direct precise input of mechanical energy.

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