ArticleProceedings of the National Academy of Sciences of the United States of America2007
Substrate binding and protein conformational dynamics measured by 2D-IR vibrational echo spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 88 citations in OpenAlex.
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- Least-Squares Fitting of Multidimensional Spectra to Kubo Line-Shape Models.The journal of physical chemistry. B · 2021Article
- Probing Ligand Effects on the Ultrafast Dynamics of Copper Complexes via Midinfrared Pump-Probe and 2DIR Spectroscopies.The journal of physical chemistry. B · 2021Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Enzymatic Transition States and Drug Design.Chemical reviews · 2018Review
- Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions.International journal of molecular sciences · 2018Review
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Applications of two-dimensional infrared spectroscopy.The Analyst · 2015Review
- Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site.Chemical science · 2015Article
- pH-dependent picosecond structural dynamics in the distal pocket of nitrophorin 4 investigated by 2D IR spectroscopy.The journal of physical chemistry. B · 2013Article
- Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Topics in current chemistry · 2013Review
- Dynamics of Functionalized Surface Molecular Monolayers Studied with Ultrafast Infrared Vibrational Spectroscopy.The journal of physical chemistry. C, Nanomaterials and interfaces · 2012Article
- Fast dynamics of HP35 for folded and urea-unfolded conditions.The journal of physical chemistry. B · 2012Article
- Ribonuclease S dynamics measured using a nitrile label with 2D IR vibrational echo spectroscopy.The journal of physical chemistry. B · 2012Article
- 3-picolyl azide adenine dinucleotide as a probe of femtosecond to picosecond enzyme dynamics.The journal of physical chemistry. B · 2012Article
- Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.The journal of physical chemistry. B · 2011Article
- Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.The Journal of chemical physics · 2011Article
- Influence of histidine tag attachment on picosecond protein dynamics.Biochemistry · 2011Article
- Temperature dependent equilibrium native to unfolded protein dynamics and properties observed with IR absorption and 2D IR vibrational echo experiments.Journal of the American Chemical Society · 2011Article
- Protein dynamics in cytochrome P450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy.Journal of the American Chemical Society · 2011Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Enzyme structural dynamics play a pivotal role in substrate binding and biological function, but the influence of substrate binding on enzyme dynamics has not been examined on fast time scales. In this work, picosecond dynamics of horseradish peroxidase (HRP) isoenzyme C in the free form and when ligated to a variety of small organic molecule substrates is studied by using 2D-IR vibrational echo spectroscopy. Carbon monoxide bound at the heme active site of HRP serves as a spectroscopic marker that is sensitive to the structural dynamics of the protein. In the free form, HRP assumes two distinct spectroscopic conformations that undergo fluctuations on a tens-of-picoseconds time scale. After substrate binding, HRP is locked into a single conformation that exhibits reduced amplitudes and slower time-scale structural dynamics. The decrease in carbon monoxide frequency fluctuations is attributed to reduced dynamic freedom of the distal histidine and the distal arginine, which are key residues in modulating substrate binding affinity. It is suggested that dynamic quenching caused by substrate binding can cause the protein to be locked into a conformation suitable for downstream steps in the enzymatic cycle of HRP.
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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.