ArticleJournal of the American Chemical Society2011
Protein dynamics in cytochrome P450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 62 citations in OpenAlex.
- Substrate Positioning Dynamics Involves a Non-Electrostatic Component to Mediate Catalysis.The journal of physical chemistry letters · 2023Article
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- From random to rational: improving enzyme design through electric fields, second coordination sphere interactions, and conformational dynamics.Chemical science · 2023Review
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- Conformational Change Induced by Putidaredoxin Binding to Ferrous CO-ligated Cytochrome P450cam Characterized by 2D IR Spectroscopy.Frontiers in molecular biosciences · 2018Article
- Examining the role of protein structural dynamics in drug resistance inChemical science · 2017Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Thermodynamics of camphor migration in cytochrome P450cam by atomistic simulations.Scientific reports · 2017Article
- Conformational Heterogeneity and the Affinity of Substrate Molecular Recognition by Cytochrome P450cam.Biochemistry · 2017Article
- Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy.The journal of physical chemistry letters · 2016Article
- Comparison of intrinsic dynamics of cytochrome p450 proteins using normal mode analysis.Protein science : a publication of the Protein Society · 2015Article
- 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
- Size-dependent ultrafast structural dynamics inside phospholipid vesicle bilayers measured with 2D IR vibrational echoes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
- Protein dynamics studied with ultrafast two-dimensional infrared vibrational echo spectroscopy.Accounts of chemical research · 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
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome (cyt) P450s hydroxylate a variety of substrates that can differ widely in their chemical structure. The importance of these enzymes in drug metabolism and other biological processes has motivated the study of the factors that enable their activity on diverse classes of molecules. Protein dynamics have been implicated in cyt P450 substrate specificity. Here, 2D IR vibrational echo spectroscopy is employed to measure the dynamics of cyt P450(cam) from Pseudomonas putida on fast time scales using CO bound at the active site as a vibrational probe. The substrate-free enzyme and the enzyme bound to both its natural substrate, camphor, and a series of related substrates are investigated to explicate the role of dynamics in molecular recognition in cyt P450(cam) and to delineate how the motions may contribute to hydroxylation specificity. In substrate-free cyt P450(cam), three conformational states are populated, and the structural fluctuations within a conformational state are relatively slow. Substrate binding selectively stabilizes one conformational state, and the dynamics become faster. Correlations in the observed dynamics with the specificity of hydroxylation of the substrates, the binding affinity, and the substrates' molecular volume suggest that motions on the hundreds of picosecond time scale contribute to the variation in activity of cyt P450(cam) toward different substrates.
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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.