ReviewTopics in current chemistry2013
Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.
Review in Topics in current chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Probing Rigidity and Fluidity in the Interfacial Region of Lipid Bilayers with a Novel IR Probe.The journal of physical chemistry. B · 2025Article
- Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development.ACS omega · 2024Review
- Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.Acta crystallographica. Section D, Structural biology · 2022Article
- Experimental mapping of short-wavelength phonons in proteins.Innovation (Cambridge (Mass.)) · 2022Article
- Oscillatory Active-site Motions Correlate with Kinetic Isotope Effects in Formate Dehydrogenase.ACS catalysis · 2019Article
- Conformational dynamics and enzyme evolution.Journal of the Royal Society, Interface · 2018Review
- Contribution of buried distal amino acid residues in horse liver alcohol dehydrogenase to structure and catalysis.Protein science : a publication of the Protein Society · 2018Article
- Protein Mass Effects on Formate Dehydrogenase.Journal of the American Chemical Society · 2017Article
- The Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Biochemistry · 2016Article
- Role of dynamics in enzyme catalysis: substantial versus semantic controversies.Accounts of chemical research · 2015Review
- Evolutionary aspects of enzyme dynamics.The Journal of biological chemistry · 2014Review
- Effects of cavities at the nicotinamide binding site of liver alcohol dehydrogenase on structure, dynamics and catalysis.Biochemistry · 2014Article
- Preservation of protein dynamics in dihydrofolate reductase evolution.The Journal of biological chemistry · 2013Article
- Hydrogen tunneling links protein dynamics to enzyme catalysis.Annual review of biochemistry · 2013Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
At physiological temperatures, enzymes exhibit a broad spectrum of conformations, which interchange via thermally activated dynamics. These conformations are sampled differently in different complexes of the protein and its ligands, and the dynamics of exchange between these conformers depends on the mass of the group that is moving and the length scale of the motion, as well as restrictions imposed by the globular fold of the enzymatic complex. Many of these motions have been examined and their role in the enzyme function illuminated, yet most experimental tools applied so far have identified dynamics at time scales of seconds to nanoseconds, which are much slower than the time scale for H-transfer between two heavy atoms. This chemical conversion and other processes involving cleavage of covalent bonds occur on picosecond to femtosecond time scales, where slower processes mask both the kinetics and dynamics. Here we present a combination of kinetic and spectroscopic methods that may enable closer examination of the relationship between enzymatic C-H → C transfer and the dynamics of the active site environment at the chemically relevant time scale. These methods include kinetic isotope effects and their temperature dependence, which are used to study the kinetic nature of the H-transfer, and 2D IR spectroscopy, which is used to study the dynamics of transition-state- and ground-state-analog complexes. The combination of these tools is likely to provide a new approach to examine the protein dynamics that directly influence the chemical conversion catalyzed by enzymes.
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