Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F
1, situated in the mitochondrial matrix, and F o, located in the inner mitochondrial …

The F-ATP synthase, consisting of F1 and FO motors connected by a central rotor and the
stators, is the enzyme responsible for synthesizing the majority of ATP in all organisms. The …

The mitochondrial ATP synthase is a multimeric enzyme complex with an overall molecular
weight of about 600,000 Da. The ATP synthase is a molecular motor composed of two …

Mitochondrial membrane potential (MMP) is the most reliable indicator of mitochondrial
function. The MMP value range of− 136 to− 140 mV has been considered optimal for …

Abstract ATP synthases (F o F 1) are found ubiquitously in energy-transducing membranes
of bacteria, mitochondria, and chloroplasts. These enzymes couple proton transport and …

F-type ATP synthases are extraordinary multisubunit proteins that operate as nanomotors.
The Escherichia coli (E. coli) enzyme uses the proton motive force (pmf) across the bacterial …

ATP synthases are part of the sophisticated cellular metabolic network and therefore
multiple interactions have to be considered. As discussed in this review, ATP synthases form …

F 1-ATPase is an ATP-driven rotary motor that generates torque at the interface between the
catalytic β-subunits and the rotor γ-subunit. The β-subunit inwardly rotates the C-terminal …

Individual aspects of the mode of action of histatin 5, a human salivary antifungal protein,
have been partially elucidated, but the mechanism likely involves a complex set of events …

The" stator stalk" of F 1 F o-ATP synthase is essential for rotational catalysis as it connects
the nonrotating portions of the enzyme. In Escherichia coli, the stator stalk consists of two …