Abstract
The immobilization of F0F1-ATPase in uniform orientation is reported. The biotinylated and histidine-tagged subunits of the bacterial F0F1-ATPase complex were used for immobilization of the complex on artificial semi-permeable membranes resulting in 88 ± 7.8 and 72 ± 5.2% coupling of the enzymes. The immobilized enzymes retained over 90% activity. The immobilized ATPase/synthase was used for generation of ATP from ADP and Pi at the expense of electrochemical potential energy. The re-usability, ratio of amount of enzyme immobilized to enzymic activity conferred on the membranes, ATP synthesized by assembled system and suitability of ATP generated for use in coupled enzymic reactions were determined.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 293-301 |
| Number of pages | 9 |
| Journal | Biotechnology and Applied Biochemistry |
| Volume | 39 |
| Issue number | 3 |
| State | Published - Jun 1 2004 |
| Externally published | Yes |
Keywords
- ATP synthesis
- Bacterial FF-ATPase
- Biotin tag
- Energy transduction
- Immobilization
- Uniform orientation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
Fingerprint Dive into the research topics of 'Uniformly oriented bacterial F<sub>0</sub>F<sub>1</sub>-ATPase immobilized on a semi-permeable membrane: A step towards biotechnological energy transduction'. Together they form a unique fingerprint.
Cite this
Bhattacharya, S., Schiavone, M., Nayak, A., & Bhattacharya, S. K. (2004). Uniformly oriented bacterial F0F1-ATPase immobilized on a semi-permeable membrane: A step towards biotechnological energy transduction. Biotechnology and Applied Biochemistry, 39(3), 293-301.