Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping FF-ATP Synthase Trapped in Solution
International Journal of Molecular Sciences, ISSN: 1422-0067, Vol: 24, Issue: 9
2023
- 5Citations
- 6Captures
- 1Mentions
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Metrics Details
- Citations5
- Citation Indexes5
- Captures6
- Readers6
- Mentions1
- News Mentions1
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Jena University Hospital Researchers Discuss Research in Molecular Science (Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping F [ [o] ] F [ [1] ] -ATP Synthase Trapped in Solution)
2023 MAY 25 (NewsRx) -- By a News Reporter-Staff News Editor at NewsRx Life Science Daily -- New research on molecular science is the subject
Article Description
FF-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 examined the effect of increasing amounts of ADP on ATP hydrolysis of single Escherichia coli FF-ATP synthases in liposomes. We observed the individual catalytic turnover of the enzymes one after another by monitoring the internal subunit rotation using single-molecule Förster resonance energy transfer (smFRET). Observation times of single FRET-labeled FF-ATP synthases in solution were extended up to several seconds using a confocal anti-Brownian electrokinetic trap (ABEL trap). By counting active versus inhibited enzymes, we revealed that ADP inhibition did not decrease the catalytic turnover of all FF-ATP synthases equally. Instead, increasing ADP in the ADP/ATP mixture reduced the number of remaining active enzymes that operated at similar catalytic rates for varying substrate/product ratios.
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