ArticleThe journal of physical chemistry letters2012
Mass Modulation of Protein Dynamics Associated with Barrier Crossing in Purine Nucleoside Phosphorylase.
Article in The journal of physical chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Fast Motions in 5 Alpha Reductase and Its Impact on Enzyme Kinetics.ACS catalysis · 2026Article
- Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023Review
- Connecting Conformational Motions to Rapid Dynamics in Human Purine Nucleoside Phosphorylase.The journal of physical chemistry. B · 2023Article
- Atomistic description of the relationship between protein dynamics and catalysis with transition path sampling.Methods in enzymology · 2023Review
- Perspective: Path Sampling Methods Applied to Enzymatic Catalysis.Journal of chemical theory and computation · 2022Review
- The physical origin of rate promoting vibrations in enzymes revealed by structural rigidity.Scientific reports · 2020Article
- Multiple Reaction Pathways in the Morphinone Reductase-Catalyzed Hydride Transfer Reaction.ACS omega · 2020Article
- Effect of Protein Isotope Labeling on the Catalytic Mechanism of Lactate Dehydrogenase.The journal of physical chemistry. B · 2019Article
- Heavy Enzymes and the Rational Redesign of Protein Catalysts.Chembiochem : a European journal of chemical biology · 2019Article
- Examining the Origin of Catalytic Power of Catechol O-Methyltransferase.ACS catalysis · 2019Article
- Crystal Structure and Biophysical Analysis of Furfural-Detoxifying Aldehyde Reductase from Clostridium beijerinckii.Applied and environmental microbiology · 2019Article
- Enzymatic Transition States and Drug Design.Chemical reviews · 2018Review
- Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.Biochemistry · 2018Review
- Directed Evolution as a Probe of Rate Promoting Vibrations Introduced via Mutational Change.Biochemistry · 2018Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
- Electric Fields and Fast Protein Dynamics in Enzymes.The journal of physical chemistry letters · 2017Article
- Protein Mass Effects on Formate Dehydrogenase.Journal of the American Chemical Society · 2017Article
- Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Triple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate Dehydrogenase.Journal of the American Chemical Society · 2016Article
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4 authors.
Funding
Abstract
The role of protein dynamics on different time scales in enzyme catalysis remains an area of active debate. The connection between enzyme dynamics on the femtosecond time scale and transition state formation has been demonstrated in human purine nucleoside phosphorylase (PNP) through the study of a mass-altered enzyme. Isotopic substitution in human PNP (heavy PNP) decreased the rate of on-enzyme chemistry but did not alter either the transition state structure or steady-state kinetic parameters. Here we investigate the underlying atomic motions associated with altered barrier crossing probability for heavy PNP. Transition path sampling was employed to illuminate the molecular differences between barrier crossing in light and heavy enzymes. The mass effect is apparent in promoting vibrations that polarize the N-ribosidic bond, and that promote the stability of the purine leaving group. These motions facilitate barrier crossing.
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