Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping F_oF₁-ATP Synthase Trapped in Solution.

ABSTRACT: F_oF₁-ATP synthases in mitochondria, in chloroplasts, and in most bacteria are proton-driven membrane enzymes that supply the cells with ATP made from ADP and phosphate. Different control mechanisms exist to monitor and prevent the enzymes' reverse chemical reaction of fast wasteful ATP hydrolysis, including mechanical or redox-based blockade of catalysis and ADP inhibition. In general, product inhibition is expected to slow down the mean catalytic turnover. Biochemical assays are ensemble measurements and cannot discriminate between a mechanism affecting all enzymes equally or individually. For example, all enzymes could work more slowly at a decreasing substrate/product ratio, or an increasing number of individual enzymes could be completely blocked. Here, we examine

SUBMITTER: Perez I 

PROVIDER: S-EPMC10178918 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature