Physical mechanism of ATP formation in biomembranes.
Membrane-bound and isolated H+ ATPases of various origin are able to synthesize ATP from ADP and Pi after a jump-like pH increase. In the course of this increase the pH of solution (or suspension) must cross a value corresponding to pK of certain acid groups in the catalytic component of ATPase. In the case of isolated soluble enzymes it is possible to obtain up to 10 ATP molecules per one pH jump per one enzyme molecule. A physical mechanism of this phenomenon as well as of oxidative and photosynthetic phosphorylation is suggested.
Blumenfeld
L A
LA
Institute of Chemical Physics, USSR Academy of Sciences, Moscow.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002736:Chloroplasts / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008928:Mitochondria / Q000378:metabolism*; D010766:Phosphorylation; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D051381:Rats; D013211:Staphylococcus aureus / Q000378:metabolism
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases