The cyclic modulation of nucleotide‐binding properties of the three catalytic β subunits by a
series of conformational changes was an attractive explanation for the postulated binding …

Topical questions in ATP synthase research are:(1) how do protons cause subunit rotation
and how does rotation generate ATP synthesis from ADP+ Pi?(2) How does hydrolysis of …

The enzyme complex F 1-ATPase has been isolated from bovine heart mitochondria by gel
filtration of the enzyme released by chloroform from sub-mitochondrial particles. The five …

Membrane-bound ATP synthases (F0F1-ATPases) of bacteria serve two important
physiological functions. The enzyme catalyzes the synthesis of ATP from ADP and inorganic …

Bacterial proton translocating ATP-synthase couples the electrochemical potential difference
for H+ across the cytoplasmic membrane to synthesis of ATP from ADP and Pi [1, 2]. It also …

The peripheral stalk of F-ATPases is an essential component of these enzymes. It extends
from the membrane distal point of the F1 catalytic domain along the surface of the F1 domain …

The structure of most of the peripheral stalk, or stator, of the F‐ATPase from bovine
mitochondria, determined at 2.8 Å resolution, contains residues 79–183, 3–123 and 5–70 of …

INTRODUCTION As early as 1924, Albert J. Kluyver discussed the unity and diversity of
metabolism of microbes (128). He pointed out that there must be some underlying …

Abstract F 1 F 0-ATP synthases are multimeric protein complexes and common prerequisites
for their correct assembly are (i) provision of subunits in appropriate relative amounts,(ii) …

Proton ATPases function in biological energy conversion in every known living cell. Their
ubiquity and antiquity make them a prime source for evolutionary studies. There are two …