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   <subfield code="a">Reinstatement of the ATP high energy paradigm</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Kurt Repke]</subfield>
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   <subfield code="a">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 Pi 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 biocnergetics, 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.</subfield>
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   <subfield code="a">ATP synthesis</subfield>
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   <subfield code="a">ATP hydrolysis</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">phosphoryl transfer</subfield>
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   <subfield code="a">ion-motive force</subfield>
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   <subfield code="a">energy transfer</subfield>
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   <subfield code="a">coupling mechanism</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="t">Molecular and Cellular Biochemistry</subfield>
   <subfield code="d">Kluwer Academic Publishers; http://www.wkap.nl</subfield>
   <subfield code="g">160-161/1(1996-03-01), 95-99</subfield>
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   <subfield code="B">NATIONALLICENCE</subfield>
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   <subfield code="t">Molecular and Cellular Biochemistry</subfield>
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   <subfield code="g">160-161/1(1996-03-01), 95-99</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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