Catalytic site occupancy during ATP synthase catalysis
Open Access
- 23 January 2002
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 512 (1-3) , 29-32
- https://doi.org/10.1016/s0014-5793(02)02293-7
Abstract
An early proposal was that for rapid ATP synthesis by the rotational ATP synthase, a specific second site must bind ADP and Pi, and for rapid ATP hydrolysis a different second site must bind ATP. Such bi‐site activation was considered to occur whether or not an ADP or ATP was at a third site. In contrast, a more recent proposal is that rapid ATP hydrolysis requires that all three sites have bound ADP or ATP present. However, discovery that one second site binds ADP better than ATP, together with other data and considerations support the earlier proposal. The retention or rebinding of ADP can explain why three sites fill during hydrolysis as ATP concentration is increased although bi‐site activation still prevails.Keywords
This publication has 28 references indexed in Scilit:
- Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPaseNature, 2001
- Structural model of F 1 –ATPase and the implications for rotary catalysisPhilosophical Transactions Of The Royal Society B-Biological Sciences, 2000
- Substitution of βGlu201 in the α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 Increases the Affinity of Catalytic Sites for NucleotidesPublished by Elsevier ,2000
- Cross-linking of Two β Subunits in the Closed Conformation in F1-ATPasePublished by Elsevier ,1999
- F1-ATPase: A Molecular Motor That Hydrolyzes ATP with Sequential Opening and Closing of Catalytic Sites Coupled to Rotation of Its γ SubunitAccounts of Chemical Research, 1998
- Direct observation of the rotation of F1-ATPaseNature, 1997
- Specific Tryptophan Substitution in Catalytic Sites of Escherichia coli F1-ATPase Allows Differentiation between Bound Substrate ATP and Product ADP in Steady-state CatalysisJournal of Biological Chemistry, 1996
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Kinetics of ATP synthesis catalyzed by the H+‐ATPase from chloroplasts (CF0F1) reconstituted into liposomes and coreconstituted with bacteriorhodopsinEuropean Journal of Biochemistry, 1992
- Kinetics of oxidative phosphorylation in Paracoccus denitrificans. 1. Mechanism of ATP synthesis at the active site(s) of F0F1-ATPaseBiochemistry, 1990