Abstract
The F-type ATPase, TF0F1, from the thermophilic Bacillus PS3, which is free of nucleotides after isolation, was specifically loaded with one 2-azido ADP on a non-catalytic site. The enzyme was covalently modified to various extents and the rate of ATP synthesis and ATP hydrolysis was measured. Both ATP synthesis and ATP hydrolysis extrapolated to zero for covalentiy binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.
Original language | English |
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Pages (from-to) | 141-144 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta: Bioenergetics |
Volume | 1275 |
Issue number | 3 |
DOIs | |
Publication status | Published - 31 Jul 1996 |
MoE publication type | Not Eligible |
Funding
This work was supportedb y the Commission of the EuropeanU nion throughG rant No. BIO2CT-930078.T he author is also indebtedt o J.-L. Rigaud for the use of his laboratorya nd to Jonathan Hanley for correctingt he English.
Keywords
- 2-Azido nucleotide
- Adenosine binding site
- ATPase
- ATPase TFF
- F-type
- H-
- Thermophilic Bacillus PS3