Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Biophysics and Biomolecular Structure
28 (1999), S. 205-234
ISSN:
1056-8700
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Biology
,
Physics
Notes:
Abstract The F0F1 ATP synthase is a large multisubunit complex that couples translocation of protons down an electrochemical gradient to the synthesis of ATP. Recent advances in structural analyses have led to the demonstration that the enzyme utilizes a rotational catalytic mechanism. Kinetic and biochemical evidence is consistent with the expected equal participation of the three catalytic sites in the alpha3beta3 hexamer, which operate in sequential, cooperative reaction pathways. The rotation of the core gamma subunit plays critical roles in establishing the conformation of the sites and the cooperative interactions. Mutational analyses have shown that the rotor subunits are responsible for coupling and in doing so transmit specific conformational information between transport and catalysis.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.biophys.28.1.205
|
Location |
Call Number |
Expected |
Availability |
