Reconstitution of energy-linked activities of the solubilized F1F0 ATP synthase from Bacillus subtilis.
The F1F0 ATP synthases from wild-type Bacillus subtilis and an uncoupler-resistant mutant have comparable subunit structures. In accord with an earlier hypothesis, ATP hydrolysis and ATP-Pi exchange by the two synthases were equally stimulated and inhibited by protonophores, respectively, when reconstituted alone in either wild-type or mutant lipids.
Department of Biochemistry, Mount Sinai School of Medicine of the City University of New York, New York 10029.
D B
DB
Hicks
D M
DM
Cohen
T A
TA
Krulwich
D000255:Adenosine Triphosphate / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology* / Q000378:metabolism; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D004734:Energy Metabolism; D006868:Hydrolysis; D010455:Peptides / Q000032:analysis; D010710:Phosphates / Q000378:metabolism; D011510:Proteolipids; D017494:Proton Pumps; D006180:Proton-Translocating ATPases / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*
D010455:Peptides; D010710:Phosphates; D011510:Proteolipids; D017494:Proton Pumps; C020485:proteoliposomes; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases