F1F0-type ATPases catalyse both ATP-driven proton translocation and proton-gradient-driven ATP synthesis. Recent cryoelectronmicroscopy and low-resolution X-ray studies provide a first glimpse at the structure of this complicated membrane-bound enzyme. The F1 part is roughly globular and linked to the membrane-intercalated F0 part by a narrow stalk domain, which contains the γ-, σ- and ω-subunits along with domains of the b-subunit of the F0 part. Here, we review evidence that conformational and positional changes in the γ- and ε{lunate}-subunits provide the coupling between catalytic sites and proton translocation within the F1F0 complex. © 1994.
Capaldi R.A., Aggeler R., Turina P., Wilkens S. (1994). Coupling between catalytic sites and the proton channel in F1F0-type ATPases. TRENDS IN BIOCHEMICAL SCIENCES, 19(7), 284-289 [10.1016/0968-0004(94)90006-X].
Coupling between catalytic sites and the proton channel in F1F0-type ATPases
Turina P.;
1994
Abstract
F1F0-type ATPases catalyse both ATP-driven proton translocation and proton-gradient-driven ATP synthesis. Recent cryoelectronmicroscopy and low-resolution X-ray studies provide a first glimpse at the structure of this complicated membrane-bound enzyme. The F1 part is roughly globular and linked to the membrane-intercalated F0 part by a narrow stalk domain, which contains the γ-, σ- and ω-subunits along with domains of the b-subunit of the F0 part. Here, we review evidence that conformational and positional changes in the γ- and ε{lunate}-subunits provide the coupling between catalytic sites and proton translocation within the F1F0 complex. © 1994.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
