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  Mutual synchronization of molecular turnover cycles in allosteric enzymes II. product inhibition

Stange, P., Mikhailov, A. S., & Hess, B. (1999). Mutual synchronization of molecular turnover cycles in allosteric enzymes II. product inhibition. The Journal of Physical Chemistry B, 103(29), 6111-6210. doi:10.1021/jp9900640.

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JPhysChemB_103_1999_6111.pdf (Any fulltext), 203KB
 
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Stange, Pedro1, Author           
Mikhailov, Alexander S., Author
Hess, Benno2, Author           
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Emeritus Group Prof. Dr. B. Hess, Max Planck Institute for Medical Research, Max Planck Society, ou_1497713              

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 Abstract: Diffusion of regulatory molecules during an enzymic reaction in micrometer and submicrometer reaction volumes can lead to mixing and transport times much shorter than the turnover time of enzymes. Our theoretical investigations of a stochastic model of an allosterically product-inhibited enzymic reaction show that under these conditions the turnover cycles of individual enzymes can become synchronized. Interactions between different enzymes realized by means of fast moving inhibitor molecules are responsible for such mutual synchronization. This synchronization is accompanied by rapid oscillations in the concentration of the reaction product.

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Language(s): eng - English
 Dates: 1999-01-051999-05-111999-07-021999
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jp9900640
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Title: The Journal of Physical Chemistry B
  Other : J. Phys. Chem. B
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 103 (29) Sequence Number: - Start / End Page: 6111 - 6210 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1