ArticleProceedings of the National Academy of Sciences of the United States of America2015
Delicate conformational balance of the redox enzyme cytochrome P450cam.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 44 citations in OpenAlex.
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Updating the Paradigm: Redox Partner Binding and Conformational Dynamics in Cytochromes P450.Accounts of chemical research · 2022Review
- Partial Opening of Cytochrome P450cam (CYP101A1) Is Driven by Allostery and Putidaredoxin Binding.Biochemistry · 2021Article
- Active Site Hydrogen Bonding Induced in Cytochrome P450cam by Effector Putidaredoxin.Biochemistry · 2021Article
- Reconciling conformational heterogeneity and substrate recognition in cytochrome P450.Biophysical journal · 2021Article
- Kinetic Evidence for an Induced Fit Mechanism in the Binding of the Substrate Camphor by Cytochrome P450ACS catalysis · 2021Article
- The Photocatalyzed Thiol-ene reaction: A New Tag to Yield Fast, Selective and reversible Paramagnetic Tagging of Proteins.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- An Intermediate Conformational State of Cytochrome P450cam-CN in Complex with Putidaredoxin.Biochemistry · 2019Article
- Mechanisms of Cytochrome P450-Catalyzed Oxidations.ACS catalysis · 2018Article
- Structure of cytochrome P450 2B4 with an acetate ligand and an active site hydrogen bond network similar to oxyferrous P450cam.Journal of inorganic biochemistry · 2018Article
- Conformational Change Induced by Putidaredoxin Binding to Ferrous CO-ligated Cytochrome P450cam Characterized by 2D IR Spectroscopy.Frontiers in molecular biosciences · 2018Article
- Thermodynamics of camphor migration in cytochrome P450cam by atomistic simulations.Scientific reports · 2017Article
- Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites.Journal of biomolecular NMR · 2017Article
- Identification of productive and futile encounters in an electron transfer protein complex.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conformational selectivity in cytochrome P450 redox partner interactions.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications.Biochemistry · 2016Article
- Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance.Scientific reports · 2016Article
- An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins.Journal of biomolecular NMR · 2016Article
- Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags.Journal of biomolecular NMR · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The energy landscapes of proteins are highly complex and can be influenced by changes in physical and chemical conditions under which the protein is studied. The redox enzyme cytochrome P450cam undergoes a multistep catalytic cycle wherein two electrons are transferred to the heme group and the enzyme visits several conformational states. Using paramagnetic NMR spectroscopy with a lanthanoid tag, we show that the enzyme bound to its redox partner, putidaredoxin, is in a closed state at ambient temperature in solution. This result contrasts with recent crystal structures of the complex, which suggest that the enzyme opens up when bound to its partner. The closed state supports a model of catalysis in which the substrate is locked in the active site pocket and the enzyme acts as an insulator for the reactive intermediates of the reaction.
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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.