ArticleThe journal of physical chemistry letters2016
Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy.
Article in The journal of physical chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 42 citations in OpenAlex.
- Two-Dimensional Infrared Spectroscopy Resolves the Vibrational Landscape in Donor-Bridge-Acceptor Complexes with Site-Specific Isotopic Labeling.ACS physical chemistry Au · 2024Article
- Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development.ACS omega · 2024Review
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- Increasing Pump-Probe Signal toward Asymptotic Limits.The journal of physical chemistry. B · 2023Review
- Method for Identifying Common Features in Reactive Trajectories of a Transition Path Sampling Ensemble.Journal of chemical theory and computation · 2022Article
- Cross-Correlated Motions in Azidolysozyme.Molecules (Basel, Switzerland) · 2022Article
- Least-Squares Fitting of Multidimensional Spectra to Kubo Line-Shape Models.The journal of physical chemistry. B · 2021Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Role of Protein Motions in Catalysis by Formate Dehydrogenase.The journal of physical chemistry. B · 2020Article
- Effect of Metal Ions on the Activity of Ten NAD-Dependent Formate Dehydrogenases.The protein journal · 2020Article
- Oscillatory Active-site Motions Correlate with Kinetic Isotope Effects in Formate Dehydrogenase.ACS catalysis · 2019Article
- Recent advances in multidimensional ultrafast spectroscopy.Royal Society open science · 2018Review
- Protein Mass Effects on Formate Dehydrogenase.Journal of the American Chemical Society · 2017Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Enzymes move on a variety of length and time scales. While much is known about large structural fluctuations that impact binding of the substrates and release of products, little is known about faster motions of enzymes and how these motions may influence enzyme-catalyzed reactions. This Letter reports frequency fluctuations of the azide anion bound to the active site of formate dehydrogenase measured via 2D IR spectroscopy. These measurements reveal an underdamped oscillatory component to the frequency-frequency correlation function when the azide is bound to the NAD(+) ternary complex. This oscillation disappears when the reduced cofactor is added, indicating that the oscillating contributions most likely come from the charged nicotinamide ring. These oscillatory motions may be relevant to donor-acceptor distance sampling of the catalyzed hydride transfer and therefore may give future insights into the dynamic behavior involved in enzyme catalysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.