Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.

Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.

An electrogenic proton-translocating adenosine triphosphatase from bovine kidney medulla.

Urinary acidification in the mammalian collecting tubule is similar to that in the turtle bladder, an epithelium whose H+ secretion is due to a luminal proton-translocating ATPase. We isolated a fraction from bovine renal medulla, which contains ATP-dependent proton transport. H+ transport was found to be electrogenic in that its rate was reduced by a membrane potential. H+ transport activity w...

Biosynthesis and assembly of the proton-translocating adenosine triphosphatase complex from chloroplasts.

The H(+)-translocating ATPase complex of chloroplasts consists of at least eight nonidentical subunits. Five of these (alpha, beta, gamma, delta, and epsilon subunits) collectively constitute the globular extramembranous CF(1) portion of the complex. The remaining three subunits (I-III) represent the membrane-embedded portion. Biosynthesis and assembly of these subunits were studied by pulse-la...

Purification and properties of the proton-translocating adenosine triphosphatase complex of bovine heart mitochondria.

1. The proton-translocating adenosine triphosphatase (ATPase) of bovine heart mitochondria was highly purified by extraction of submitochondrial particles with cholate, fractionation with ammonium sulfate, and sucrose gradient centrifugation in the presence of methanol, deoxycholate, and lysolecithin. 2. The preparation had a very low content of phospholipids, respiratory components, and adenin...

The Stoicheiometry and Molecular Mechanism of Adenosine Diphosphate Phosphorylation Catalysed by the Proton-Translocating Adenosine Triphosphatase Systems of Mitochondria, Chloroplasts and Bacteria

The family of fundamentally similar Mg2+-activated ATPase* systems found in the membranes of mitochondria, chloroplasts and bacteria, acting reversibly as an ATP synthase in practically all cells containing either photosynthetic pigments or cytochromes, probably represents one of the most widely distributed of all enzyme systems (Racker, 1970; Harold, 1972; Jagendorf, 1973). Under the circumsta...