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
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,
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
(Penefsky H.S., E.P. Maynard, D. Anima, and E. Racker (1960) JBC 235
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
therefore, maintain a gradient of proton activity generated by
chain enzymes and used by ATP synthase.
(Mitchell, P. (1961) Nature 199, 144-148.)
Soluble adenosine triphosphotase (F1) was isolated by
Paul D. Boyer proposed that ATP is synthesised through structural
changes in the ATP synthase enzyme.
D. Boyer 's group: the step in ATP synthesis which requires energy is
the release of ATP from the enzyme.
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.
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.
Yoshida's lab: direct observation of the rotation in F1
during ATP hydrolysis.
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+
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.