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A brief history of ATP synthase research

1929
ATP was discovered by chemist Karl Lohmann.

1935
Vladimir Engelhart  noted that muscle contractions require ATP.

1937
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.)

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

1939-1941
Fritz Lipmann  shown that ATP is the main bearer of chemical energy in the cell. He coins the phrase "energy-rich phosphate bonds".

1948
Alexander Todd synthesised ATP chemically.

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

1956
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)

1960
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)

1961
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.

1964
Paul D. Boyer proposed that ATP is synthesised through structural changes in the ATP synthase enzyme.

1973
Paul D. Boyer 's group: the step in ATP synthesis which requires energy is the release of ATP from the enzyme.

1977
Binding change mechanism of catalysis proposed in Paul D. Boyer's group.

1981
John E. Walker's lab:  the DNA sequence of the genes encoding the proteins in ATP synthase was determined.
 

1994
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.

1997
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"

2004
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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