Mechanical Control of ATP Synthase Function: Activation Energy Difference between Tight and Loose Binding Sites
Artikel i vetenskaplig tidskrift, 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.

Författare

Tamas Beke-Somfai

Chalmers, Kemi- och bioteknik, Fysikalisk kemi

Per Lincoln

Chalmers, Kemi- och bioteknik, Fysikalisk kemi

Bengt Nordén

Chalmers, Kemi- och bioteknik, Fysikalisk kemi

Biochemistry

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

Vol. 49 401-403

Styrkeområden

Nanovetenskap och nanoteknik

Energi

Livsvetenskaper och teknik

Materialvetenskap

Ämneskategorier

Fysikalisk kemi

Kemi

Fundament

Grundläggande vetenskaper

DOI

10.1021/bi901965c