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  Mutual Synchronization of Molecular Turnover Cycles in Allosteric Enzymes

Stange, P., Mikhailov, A. S., & Hess, B. (1998). Mutual Synchronization of Molecular Turnover Cycles in Allosteric Enzymes. The Journal of Physical Chemistry B, 102(32), 6273-6289. doi:10.1021/jp9813185.

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 Creators:
Stange, Pedro1, Author           
Mikhailov, Alexander S.1, Author           
Hess, Benno2, Author
Affiliations:
1Physical Chemistry, Fritz Haber Institute, Max Planck Society, ou_634546              
2Max-Planck-Institut für medizinische Forschung, Heidelberg, Deutschland, ou_persistent22              

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 Abstract: The diffusive transport and mixing times of regulatory molecules in micrometer and submicrometer reaction volumes can be shorter than characteristic times of conformational transformations in single enzyme molecules. Under these conditions, mutual synchronization of individual molecular turnover cycles takes place when strong allosteric activation by the reaction products is present. Using simple automaton models to describe the cycles of single molecules, we analyze properties of the synchronization transition and the role of statistical fluctuations in the synchronization phenomena.

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Language(s): eng - English
 Dates: 1998-02-261998-05-191998-07-211998-08-01
 Publication Status: Issued
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jp9813185
 Degree: -

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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: 17 Volume / Issue: 102 (32) Sequence Number: - Start / End Page: 6273 - 6289 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1