Abstract
During ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. Thus, for efficient ATP synthesis it would be desirable if incoming substrate could be bound to a catalytic site with a preference for MgADP over MgATP. We tested three hypotheses predicting the existence of such a site. However, our results showed that, at least in absence of an electrochemical proton gradient, none of the three catalytic sites has a higher affinity for MgADP than for MgATP.
| Original language | English |
|---|---|
| Pages (from-to) | 4131-4135 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 580 |
| Issue number | 17 |
| DOIs | |
| State | Published - Jul 24 2006 |
Keywords
- ATP synthase
- Binding change
- Catalytic sites
- Enzyme mechanism
- F-ATPase
- High-affinity site
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Cite this
Mao, H. Z., Gray, W. D., & Weber, J. (2006). Does F1-ATPase have a catalytic site that preferentially binds MgADP? FEBS Letters, 580(17), 4131-4135. https://doi.org/10.1016/j.febslet.2006.06.059