Efficient ATP Synthesis by Thermophilic Bacillus FoF1-ATP Synthase
Author Information
Author(s): Soga Naoki, Kinosita Kazuhiko Jr, Yoshida Masasuke, Suzuki Toshiharu
Primary Institution: Waseda University
Hypothesis
Can a mutant TFoF1 lacking an inhibitory segment of the ε-subunit improve ATP synthesis activity?
Conclusion
The study developed procedures that significantly increased ATP synthesis activity of TFoF1 to about 16 s−1 at 30 °C.
Supporting Evidence
- The ATP synthesis activity reached approximately 16 s−1 at 30 °C.
- Michaelis–Menten constants for ADP and inorganic phosphate were found to be 13 μm and 0.55 mm, respectively.
- The study demonstrated that the removal of the inhibitory C-terminal segment of the ε-subunit increased synthesis activity.
Takeaway
Scientists found a way to make a special protein work much better at making energy, which is important for cells.
Methodology
The study involved preparing active proteoliposomes of TFoF1 and measuring ATP synthesis activity under controlled conditions.
Limitations
The orientation of the enzyme in the reconstituted membrane was not controlled, which may lead to underestimated activity values.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website