The mechanism of ATP synthase: A reassessment of the functions of the b and a subunits

Role of the carboxyl‐terminal region of the PVP protein (F0I subunit) in the H+ conduction of F0F1 H+‐ATP synthase of bovine heart mitochondria

“…Because of its peripheral location at the M surface of the membrane this carboxylterminal tail cannot participate directly in transmembrane proton conduction. The present results show, however, that this segment of the PVP protein promotes proton conduction in F. possibly by favouring exchange of protons between the aqueous phase and the channel and/or by bringing the membrane-spanning protein segment [17,20] of the channel into the proper active configuration. This conclusion is also supported by the fact that removal of the carboxyl-terminal tail of the PVP protein induces loss of sensitivity of the FO proton 'channel to oligomycin.…”

Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP‐synthase

“…It has been proposed that subunit a from E. coli plays an important role in the coupling of proton transport to ATP synthesis/hydrolysis [32,33]. Since the mechanism of chemiosmotic ATP synthesis/hydrolysis appears to be similar in all FoF~ type ATP-synthases, the presence of subunit IV in CFoF1 as a homologue of subunit a of E. coli FoF~ is a very welcome result.…”

Mitochondrial F0F1 H+‐ATP synthase Characterization of F0 components involved in H+ translocation

“…otes [2,37], where it apparently functions in an oligomeric state [3,10,11]. Definite evidence is available showing that in the E. coli enzyme, in addition to subunit c, subunit a (uncB of the atp operon [2,33]) is also directly involved in proton conduction [34,35]. Subunit b (uncF of the atp operon) appears to be essential in E. coli for proper assembly of functional FO in the membrane [36,37].…”