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

Tamás Beke-Somfai, Per Lincoln, Bengt Nordén

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

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.
Original languageEnglish (US)
Pages (from-to)401-403
Number of pages3
JournalBiochemistry
Volume49
Issue number3
DOIs
StatePublished - Jan 26 2010
Externally publishedYes

Fingerprint Dive into the research topics of 'Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites'. Together they form a unique fingerprint.

Cite this