Abstract
Background: It is unknown how enzymes actually achieve the catalytic pathways proposed for ATP hydrolysis. Results: A quantum mechanical analysis of myosin ATPase quantifies the relevant interactions that stabilize a metaphosphate intermediate. Conclusion: The protein is designed to stabilize this metaphosphate, key to the enzymatic mechanism. Significance: This yields a chemically consistent model for the catalytic strategy of nucleotide-hydrolyzing enzymes in general. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Kiani, F. A., & Fischer, S. (2013). Stabilization of the ADP/Metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin: Quantitative anatomy of an enzyme. Journal of Biological Chemistry, 288(49), 35058–35067. https://doi.org/10.1074/jbc.M113.500298
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