Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites

Handle URI:
http://hdl.handle.net/10754/598786
Title:
Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites
Authors:
Beke-Somfai, Tamás; Lincoln, Per; Nordén, Bengt
Abstract:
Despite exhaustive chemical and crystal structure studies, the mechanistic details of how FoF1-ATP synthase can convert mechanical energy to chemical, producing ATP, are still not fully understood. On the basis of quantum mechanical calculations using a recent highresolution X-ray structure, we conclude that formation of the P-O bond may be achieved through a transition state (TS) with a planar PO3 - ion. Surprisingly, there is a more than 40 kJ/mol difference between barrier heights of the loose and tight binding sites of the enzyme. This indicates that even a relatively small change in active site conformation, induced by the γ-subunit rotation, may effectively block the back reaction in βTP and, thus, promote ATP. © 2009 American Chemical Society.
Citation:
Beke-Somfai T, Lincoln P, Nordén B (2010) Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites. Biochemistry 49: 401–403. Available: http://dx.doi.org/10.1021/bi901965c.
Publisher:
American Chemical Society (ACS)
Journal:
Biochemistry
KAUST Grant Number:
KUK-11008-23
Issue Date:
26-Jan-2010
DOI:
10.1021/bi901965c
PubMed ID:
20000803
Type:
Article
ISSN:
0006-2960; 1520-4995
Sponsors:
This Publication is based oil work Financed by King Abdullah University of Science and Technology (KAUST) (Grant KUK-11008-23).
Appears in Collections:
Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorBeke-Somfai, Tamásen
dc.contributor.authorLincoln, Peren
dc.contributor.authorNordén, Bengten
dc.date.accessioned2016-02-25T13:41:12Zen
dc.date.available2016-02-25T13:41:12Zen
dc.date.issued2010-01-26en
dc.identifier.citationBeke-Somfai T, Lincoln P, Nordén B (2010) Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites. Biochemistry 49: 401–403. Available: http://dx.doi.org/10.1021/bi901965c.en
dc.identifier.issn0006-2960en
dc.identifier.issn1520-4995en
dc.identifier.pmid20000803en
dc.identifier.doi10.1021/bi901965cen
dc.identifier.urihttp://hdl.handle.net/10754/598786en
dc.description.abstractDespite exhaustive chemical and crystal structure studies, the mechanistic details of how FoF1-ATP synthase can convert mechanical energy to chemical, producing ATP, are still not fully understood. On the basis of quantum mechanical calculations using a recent highresolution X-ray structure, we conclude that formation of the P-O bond may be achieved through a transition state (TS) with a planar PO3 - ion. Surprisingly, there is a more than 40 kJ/mol difference between barrier heights of the loose and tight binding sites of the enzyme. This indicates that even a relatively small change in active site conformation, induced by the γ-subunit rotation, may effectively block the back reaction in βTP and, thus, promote ATP. © 2009 American Chemical Society.en
dc.description.sponsorshipThis Publication is based oil work Financed by King Abdullah University of Science and Technology (KAUST) (Grant KUK-11008-23).en
dc.publisherAmerican Chemical Society (ACS)en
dc.titleMechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sitesen
dc.typeArticleen
dc.identifier.journalBiochemistryen
dc.contributor.institutionChalmers University of Technology, Göteborg, Swedenen
dc.contributor.institutionEötvös Loránd University, Budapest, Hungaryen
kaust.grant.numberKUK-11008-23en
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