The Open Biochemistry Journal




ISSN: 1874-091X ― Volume 13, 2019

Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds



Laurent Jaeken*, 1, Vladimir Vasilievich Matveev2
1 Laboratory of Biochemistry, Karel de Grote University College, Department of Applied Engineering, Salesianenlaan 30, B-2660, Antwerp, Belgium
2 Laboratory of Cell Physiology, Institute of Cytology, Russian Academy of Sciences, Tikhoretsky Ave 4, St. Petersburg 194064, Russia

Abstract

Observations of coherent cellular behavior cannot be integrated into widely accepted membrane (pump) theory (MT) and its steady state energetics because of the thermal noise of assumed ordinary cell water and freely soluble cytoplasmic K+. However, Ling disproved MT and proposed an alternative based on coherence, showing that rest (R) and action (A) are two different phases of protoplasm with different energy levels. The R-state is a coherent metastable low-entropy state as water and K+ are bound to unfolded proteins. The A-state is the higher-entropy state because water and K+ are free. The R-to-A phase transition is regarded as a mechanism to release energy for biological work, replacing the classical concept of high-energy bonds. Subsequent inactivation during the endergonic A-to-R phase transition needs an input of metabolic energy to restore the low entropy R-state. Matveev’s native aggregation hypothesis allows to integrate the energetic details of globular proteins into this view.

Keywords:: Entropy, coherence, polarized water, unfolded proteins, native aggregation, association-induction hypothesis.


Article Information


Identifiers and Pagination:

Year: 2012
Volume: 6
First Page: 139
Last Page: 159
Publisher Id: TOBIOCJ-6-139
DOI: 10.2174/1874091X01206010139

Article History:

Received Date: 11/5/2012
Revision Received Date: 06/9/2012
Acceptance Date: 12/9/2012
Electronic publication date: 11/12/2012
Collection year: 2012

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© Jaeken and Matveev; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http: //creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.


* Address correspondence to this author at the Laboratory of Biochemistry, Karel de Grote University College, Department of Applied Engineering, Salesianenlaan 30, B-2660, Antwerp, Belgium; Tel:+1323 663 30 31;Fax: +1323 293 34 08; Emails: laurentjaeken@hotmail.com;; laurentjaeken@kdg.be



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