The Escherichia coli FOF1 γM23K Uncoupling Mutant Has a Higher K0.5 for Pi. Transition State Analysis of This Mutant and Others Reveals That Synthesis and Hydrolysis Utilize the Same Kinetic Pathway
Author:
Affiliation:
1. Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22906-0011
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi971478r
Reference59 articles.
1. Correlations of structure and function in subunit c of Escherichia coli FoF1 ATP synthase
2. THE F0F1-TYPE ATP SYNTHASES OF BACTERIA: Structure and Function of the F0 Complex
3. Mechanisms of Active Transport in the F O F 1 ATP Synthase
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