ArticleProceedings of the National Academy of Sciences of the United States of America2016
Conformational selectivity in cytochrome P450 redox partner interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 59 citations in OpenAlex.
- Characterization of a CYP107 family vitamin DArchives of biochemistry and biophysics · 2026Article
- In silico studies on nicotinamide analogs as competitive inhibitors of nicotinamidase in methicillin-resistant Staphylococcus aureus.Molecular diversity · 2025Article
- Computational insights in CD58 binding to ASFV CD2v and in silico optimization of nanobody designs against the interface.Open veterinary journal · 2025Article
- Interactions of human mitochondrial Ferredoxin 1 (Adrenodoxin) by NMR; modulation by cytochrome P450 substrate and by truncation of the C-terminal tail.Journal of inorganic biochemistry · 2023Article
- Three pairs of surrogate redox partners comparison for Class I cytochrome P450 enzyme activity reconstitution.Communications biology · 2022Article
- A computational essential dynamics approach to investigate structural influences of ligand binding on Papain like protease from SARS-CoV-2.Computational biology and chemistry · 2022Article
- 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
- Structural Dynamics of Cytochrome P450 3A4 in the Presence of Substrates and Cytochrome P450 Reductase.Biochemistry · 2021Article
- Kinetic Evidence for an Induced Fit Mechanism in the Binding of the Substrate Camphor by Cytochrome P450ACS catalysis · 2021Article
- Molecular and Structural Evolution of Cytochrome P450 Aromatase.International journal of molecular sciences · 2021Article
- Unexpected Differences between Two Closely Related Bacterial P450 Camphor Monooxygenases.Biochemistry · 2020Article
- Linkage between Proximal and Distal Movements of P450cam Induced by Putidaredoxin.Biochemistry · 2020Article
- Conformational turn triggers regio-selectivity in the bioactivation of thiophene-contained compounds mediated by cytochrome P450.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Specificity of the Redox Complex between Cytochrome P450 24A1 and Adrenodoxin Relies on Carbon-25 Hydroxylation of Vitamin-D Substrate.Drug metabolism and disposition: the biological fate of chemicals · 2019Article
- An Intermediate Conformational State of Cytochrome P450cam-CN in Complex with Putidaredoxin.Biochemistry · 2019Article
- Molecular Dynamics Simulation for All.Neuron · 2018Review
- Effect of redox partner binding on CYP101D1 conformational dynamics.Journal of inorganic biochemistry · 2018Article
- Cytochrome-P450-Induced Ordering of Microsomal Membranes Modulates Affinity for Drugs.Angewandte Chemie (International ed. in English) · 2018Article
- The cytochrome P450 24A1 interaction with adrenodoxin relies on multiple recognition sites that vary among species.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The heme iron of cytochromes P450 must be reduced to bind and activate molecular oxygen for substrate oxidation. Reducing equivalents are derived from a redox partner, which requires the formation of a protein-protein complex. A subject of increasing discussion is the role that redox partner binding plays, if any, in favoring significant structural changes in the P450s that are required for activity. Many P450s now have been shown to experience large open and closed motions. Several structural and spectral studies indicate that the well-studied P450cam adopts the open conformation when its redox partner, putidaredoxin (Pdx), binds, whereas recent NMR studies indicate that this view is incorrect. Given the relevance of this discrepancy to P450 chemistry, it is important to determine whether Pdx favors the open or closed form of P450cam. Here, we have used both computational and experimental isothermal titration calorimetry studies that unequivocally show Pdx favors binding to the open form of P450cam. Analyses of molecular-dynamic trajectories also provide insights into intermediate conformational states that could be relevant to 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.