Rotational coupling in the F0F1 ATP synthase

Citation
Rk. Nakamoto et al., Rotational coupling in the F0F1 ATP synthase, ANN R BIO B, 28, 1999, pp. 205-234
Citations number
131
Categorie Soggetti
Biochemistry & Biophysics
Journal title
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE
ISSN journal
10568700 → ACNP
Volume
28
Year of publication
1999
Pages
205 - 234
Database
ISI
SICI code
1056-8700(1999)28:<205:RCITFA>2.0.ZU;2-E
Abstract
The F0F1 ATP synthase is a large multisubunit complex that couples transloc ation of protons down an electrochemical gradient to the synthesis of ATP. Recent advances in structural analyses have led to the demonstration that t he enzyme utilizes a rotational catalytic mechanism. Kinetic and biochemica l evidence is consistent with the expected equal participation of the three catalytic sites in the alpha(3)beta(3) hexamer, which operate in sequentia l, cooperative reaction pathways. The rotation of the core gamma subunit pl ays critical roles in establishing the conformation of the sites and the co operative interactions. Mutational analyses have shown that the rotor subun its are responsible for coupling and in doing so transmit specific conforma tional information between transport and catalysis.