Single-molecule Study on the Temperature-sensitive Reaction of F1-ATPase with a Hybrid F1 Carrying a Single β(E190D)
Open Access
- 1 August 2009
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (34) , 23169-23176
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Correlation between the conformational states of F 1 -ATPase as determined from its crystal structure and single-molecule rotationProceedings of the National Academy of Sciences, 2008
- Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80° and 40° substep rotationsNature Structural & Molecular Biology, 2008
- Temperature Dependence of the Rotation and Hydrolysis Activities of F1-ATPaseBiophysical Journal, 2008
- Temperature‐sensitive reaction intermediate of F1‐ATPaseEMBO Reports, 2007
- Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPaseNature, 2001
- F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° StepsCell, 1998
- Direct observation of the rotation of F1-ATPaseNature, 1997
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Spatial precision of a catalytic carboxylate of F1‐ATPase β subunit probed by introducing different carboxylate‐containing side chainsFEBS Letters, 1994
- Invitro mutated β subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the α and γ subunits to produce inactive complexesBiochemical and Biophysical Research Communications, 1987