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Rotation of subunits during catalysis by Escherichia coli F1-ATPase.
- T. Duncan, V. V. Bulygin, Y. Zhou, M. L. Hutcheon, R. L. Cross
- BiologyProceedings of the National Academy of Sciences…
- 21 November 1995
The results demonstrate that gamma subunit rotates relative to the beta subunits during catalysis, and similar reactivities of unlabeled and radiolabeled beta sub units with gamma C87 upon reoxidation.
Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site.
A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions.
- P. Boyer, R. L. Cross, W. Momsen
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 October 1973
The results lead to the working hypothesis that in oxidative phosphorylation energy from electron transport causes release of preformed ATP from the catalytic site, which could logically involve energy-requiring protein conformational change.
The evolution of A‐, F‐, and V‐type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio
Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases
The mode of inhibition of oxidative phosphorylation by efrapeptin (A23871): measurement of substrate effects on rates of inactivation by a tight-binding inhibitor.
Structure and mechanism of FoF1-type ATP synthases and ATPases.
The mode of inhibition of oxidative phosphorylation by efrapeptin (A23871). Evidence for an alternating site mechanism for ATP synthesis.
Data are presented which suggest that ATP promotes the binding of efrapeptin to the enzyme, andications that efrapptin is a catalytic site inhibitor make these results difficult to reconcile with a simple mechanistic scheme involving a single independnet catalytic sites for ATP synthesis and hydrolysis.
Adenine nucleotide-binding sites on mitochondrial F1-ATPase. Evidence for an adenylate kinase-like orientation of catalytic and noncatalytic sites.