Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites
Journal article, 2010

Despite exhaustive chemical and crystal structure studies, the mechanistic details of how F o F 1 -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 PO 3 - 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 β TP and, thus, promote ATP. © 2009 American Chemical Society.

Author

Tamas Beke-Somfai

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Per Lincoln

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Bengt Nordén

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Biochemistry

0006-2960 (ISSN) 1520-4995 (eISSN)

Vol. 49 3 401-403

Areas of Advance

Nanoscience and Nanotechnology

Energy

Life Science Engineering

Materials Science

Subject Categories

Physical Chemistry

Chemical Sciences

Roots

Basic sciences

DOI

10.1021/bi901965c

More information

Created

10/8/2017