Literature DB >> 8901461

Reinstatement of the ATP high energy paradigm.

K R Repke1.   

Abstract

The paradigm that the hydrolysis of ATP releases high Gibbs energy able to perform work has increasingly been questioned over the last two decades. Results from theoretical and experimental studies have been interpreted to indicate that the synthesis of ATP from ADP and P(i) does not require energy supply and that binding of ATP per se can transmit utilizable energy to an enzyme. As has recently been concluded, all this has led to a change of the ATP high energy paradigm in bioenergetics. Starting from this challenge, the present review singles out the striking sources of the apparent dichotomy in bioenergetics, and endeavours to eliminate the apparent contradictions by the application of the prior knowledge on both the participation of the enzyme protein in energy exchange processes and the particular reactivities of phosphorus that make it an outstanding element for functionally variable work assignments in enzymatic systems.

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Year:  1996        PMID: 8901461     DOI: 10.1007/bf00240037

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  32 in total

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Journal:  FEBS Lett       Date:  1975-02-01       Impact factor: 4.124

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Journal:  Methods Enzymol       Date:  1989       Impact factor: 1.600

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Journal:  Biochem Pharmacol       Date:  1965-12       Impact factor: 5.858

7.  A chemiosmotic molecular mechanism for proton-translocating adenosine triphosphatases.

Authors:  P Mitchell
Journal:  FEBS Lett       Date:  1974-07-15       Impact factor: 4.124

Review 8.  ATP synthases. Structure, reaction center, mechanism, and regulation of one of nature's most unique machines.

Authors:  P L Pedersen; L M Amzel
Journal:  J Biol Chem       Date:  1993-05-15       Impact factor: 5.157

Review 9.  The mechanism and regulation of ATP synthesis by F1-ATPases.

Authors:  R L Cross
Journal:  Annu Rev Biochem       Date:  1981       Impact factor: 23.643

10.  The stereochemical course of phosphoric residue transfer catalyzed by beef heart mitochondrial ATPase.

Authors:  M R Webb; C Grubmeyer; H S Penefsky; D R Trentham
Journal:  J Biol Chem       Date:  1980-12-25       Impact factor: 5.157

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