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  Synthesis of ATP from ADP and Inorganic Phosphate at the Myosin-Subfragment 1 Active Site

Mannherz, H. G., Schenk, H., & Goody, R. S. (1974). Synthesis of ATP from ADP and Inorganic Phosphate at the Myosin-Subfragment 1 Active Site. European Journal of Biochemistry, 48(1), 287-295. doi:10.1111/j.1432-1033.1974.tb03767.x.

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EurJBiochem_48_1974_287.pdf (Any fulltext), 690KB
 
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Mannherz, Hans Georg1, Author           
Schenk, Helmut2, Author           
Goody, Roger S.1, Author           
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1Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              
2Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: Experiments on the synthesis of ATP from ADP and Pi bound at the active site of the myosin S1 fragment show that the rate limiting step in the ATPase mechanism at 23 °C is associated with a surprisingly low equilibrium constant (about 16 at pH 8.). This, together with the dissociation constant of Pi from the S1 · ADP complex (about 10 mM) obtained from these measurements, and the previously measured rate constants for this system indicate that the dissociation constant of ATP is extremely small, probably in the region of 0.10 pM.

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Language(s): eng - English
 Dates: 1974-04-091974-06-242005-03-031974-10
 Publication Status: Issued
 Pages: 9
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 Rev. Type: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 48 (1) Sequence Number: - Start / End Page: 287 - 295 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040