AbstractNa+ transport through the F0 domain of Na+-F1F0-ATPases involves the combined action of subunits c and a but the residues involved in Na+ liganding in subunit a are unknown. As a first step towards the identification of these residues, we have cloned and sequenced the gene encoding subunit a of the Na+-F1F0-ATPase of Acetobacterium woodii. This is the second sequence available now for this subunit from Na+-F1F0-ATPases. A comparison of subunit a from Na+-F1F0-ATPases with those from H+-translocating enzymes unraveled structural similarity in a C-terminal segment including the ultimate and penultimate transmembrane helix. Seven residues are conserved in this region and, therefore, likely to be involved in Na+ liganding
AbstractThe acetogenic bacterium Acetobacterium woodii uses a transmembrane electrochemical sodium i...
The ATP synthase of many archaea has the conserved sodium ion binding motif in its rotor subunit, im...
AbstractThe Na+-translocating F1F0-ATPase of Acetobacterium woodii was examined by electron microsco...
AbstractA 3.2 kb EcoRI fragment carrying genes for Na+-F1FO ATPase was cloned from chromosomal DNA o...
AbstractThe homoacetogenic bacterium Acetobacterium woodii relies on a sodium ion current across its...
AbstractThe Na+-translocating F1F0-ATPase of Acetobacterium woodii was stimulated not only by Na+ bu...
AbstractA 4.5 kbp EcoRI fragment hybridizing to a fragment of uncD (coding for subunit β of F1F0-ATP...
The Na+translocating F1FO ATP synthase from Acetobacterium woodii shows a subunit stoichiometry of α...
AbstractV-ATPases make up a family of proton pumps distributed widely from bacteria to higher organi...
Energy transduction in the anaerobic, thermophilic bacterium Clostridium fervidus relies exclusively...
An analysis of the distribution of the Na+-translocating ATPases/ATP synthases among microbial genom...
All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is couple...
The ion-driven membrane rotors of ATP synthases consist of multiple copies of subunit c, forming a c...
AbstractWe report here the N-terminal protein sequences of the subunits of the ATPase from Propionig...
A1AO ATP synthases with a V-type c subunit have only been found in hyperthermophilic archaea which m...
AbstractThe acetogenic bacterium Acetobacterium woodii uses a transmembrane electrochemical sodium i...
The ATP synthase of many archaea has the conserved sodium ion binding motif in its rotor subunit, im...
AbstractThe Na+-translocating F1F0-ATPase of Acetobacterium woodii was examined by electron microsco...
AbstractA 3.2 kb EcoRI fragment carrying genes for Na+-F1FO ATPase was cloned from chromosomal DNA o...
AbstractThe homoacetogenic bacterium Acetobacterium woodii relies on a sodium ion current across its...
AbstractThe Na+-translocating F1F0-ATPase of Acetobacterium woodii was stimulated not only by Na+ bu...
AbstractA 4.5 kbp EcoRI fragment hybridizing to a fragment of uncD (coding for subunit β of F1F0-ATP...
The Na+translocating F1FO ATP synthase from Acetobacterium woodii shows a subunit stoichiometry of α...
AbstractV-ATPases make up a family of proton pumps distributed widely from bacteria to higher organi...
Energy transduction in the anaerobic, thermophilic bacterium Clostridium fervidus relies exclusively...
An analysis of the distribution of the Na+-translocating ATPases/ATP synthases among microbial genom...
All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is couple...
The ion-driven membrane rotors of ATP synthases consist of multiple copies of subunit c, forming a c...
AbstractWe report here the N-terminal protein sequences of the subunits of the ATPase from Propionig...
A1AO ATP synthases with a V-type c subunit have only been found in hyperthermophilic archaea which m...
AbstractThe acetogenic bacterium Acetobacterium woodii uses a transmembrane electrochemical sodium i...
The ATP synthase of many archaea has the conserved sodium ion binding motif in its rotor subunit, im...
AbstractThe Na+-translocating F1F0-ATPase of Acetobacterium woodii was examined by electron microsco...