Stepping Rotation of F1-ATPase with One, Two, or Three Altered Catalytic Sites That Bind ATP Only Slowly
Open Access
- 1 July 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (28) , 24870-24874
- https://doi.org/10.1074/jbc.m202582200
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Purine but Not Pyrimidine Nucleotides Support Rotation of F1-ATPaseJournal of Biological Chemistry, 2001
- 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 Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° StepsCell, 1998
- Direct observation of the rotation of F1-ATPaseNature, 1997
- Catalytic Activities of α3β3γ Complexes of F1-ATPase with 1, 2, or 3 Incompetent Catalytic SitesPublished by Elsevier ,1996
- Analysis of time-dependent change of Escherichia coli Fl-ATPase activity and its relationship with apparent negative cooperativityBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1995
- Expression of the wild-type and the Cys-/Trp-less α3β3γ complex of thermophilic F1-ATPase in Escherichia coliBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1995
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- [6] Efficient site-directed mutagenesis using uracil-containing DNAPublished by Elsevier ,1991