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Journal Article

18O-exchange by hydrolyzing enzymes: an ab initio calculation

MPS-Authors
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Rösch,  Paul
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;
Abt. III: Strukturbiochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

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https://www.degruyter.com/downloadpdf/j/znc.1981.36.issue-7-8/znc-1981-7-804/znc-1981-7-804.xml
(Any fulltext)

https://doi.org/10.1515/znc-1981-7-804
(Any fulltext)

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Citation

Rösch, P., Kalbitzer, H. R., & Goody, R. S. (1981). 18O-exchange by hydrolyzing enzymes: an ab initio calculation. Zeitschrift für Naturforschung, C: Journal of Biosciences, 36(7-8), 534-538. doi:10.1515/znc-1981-7-804.


Cite as: https://hdl.handle.net/21.11116/0000-0004-E938-7
Abstract
Enzymes which hydrolyse ATP cause an exchange of 180 of labelled Pi in the presence of ADP. A theory for the evaluation of rate constants from an observation of the time dependence of the concentration of the various Pi species is presented. Application to the 180 exchange catalysed by myosin SI as observed by 31P-NMR shows excellent agreement with values of the rate constants determined earlier.