ArticleCommunications biology2021
An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Lipid nanoparticles as active biointerfaces: From membrane interaction to systemic dysregulation.Acta pharmaceutica Sinica. B · 2026Review
- Cryo-EM reveals an ensemble of cytochrome P450 reductase conformations in solution.Protein science : a publication of the Protein Society · 2026Article
- Heme and CO metabolism by the canonical human heme oxygenases.Journal of inorganic biochemistry · 2026Review
- Complex Roles of Insect Cytochrome P450s in Chemical Adaptation.International journal of biological sciences · 2026Review
- Reconstitution of Human Cytochrome P450 Activity using aACS synthetic biology · 2025Article
- Recent Advances in Elucidating the Mechanism of the NADPH-Cytochrome P450 Reductase-Mediated Electron Transfer Cycle: Experimental and Computational Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Phytochemical profiling, antioxidant properties, and anticancer activity of Pourouma cecropiifolia Mart. from the Ecuadorian Amazon.NPJ science of food · 2025Article
- Unraveling the Role of P450 Reductase in Herbicide Metabolic Resistance Mechanism.Plant direct · 2025Article
- Geometry-encoded molecular dynamics enables deep learning insights into P450 regiospecificity control.Scientific reports · 2025Article
- Protein subinteractomes of human microsomal cytochromes P450.Molecular biology reports · 2025Review
- Multiresolution molecular dynamics simulations reveal the interplay between conformational variability and functional interactions in membrane-bound cytochrome P450 2B4.Protein science : a publication of the Protein Society · 2024Article
- Sterol 14-alpha demethylase (CYP51) activity in Leishmania donovani is likely dependent upon cytochrome P450 reductase 1.PLoS pathogens · 2024Article
- Charged Amino Acids in the Transmembrane Helix Strongly Affect the Enzyme Activity of Aromatase.International journal of molecular sciences · 2024Article
- Influence of cholesterol on kinetic parameters for human aromatase (P450 19A1) in phospholipid nanodiscs.Journal of inorganic biochemistry · 2023Article
- Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of Human Cytochrome P450 1A2-Mediated Caffeine Metabolism.Biomolecules · 2023Article
- Cytochrome P450 Surface Domains Prevent the β-Carotene Monohydroxylase CYP97H1 ofBiomolecules · 2023Article
- Phylogenetic Analysis and Protein Modelling of Isoflavonoid Synthase Highlights Key Catalytic Sites towards Realising New Bioengineering Endeavours.Bioengineering (Basel, Switzerland) · 2022Article
- Non-Ionic Inulin-Based Polymer Nanodiscs Enable Functional Reconstitution of a Redox Complex Composed of Oppositely Charged CYP450 and CPR in a Lipid Bilayer Membrane.Analytical chemistry · 2022Article
- Functional expression and regulation of eukaryotic cytochrome P450 enzymes in surrogate microbial cell factories.Engineering microbiology · 2022Review
- Mapping protein-protein interactions in homodimeric CYP102A1 by crosslinking and mass spectrometry.Biophysical chemistry · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome P450 (CYP) heme monooxygenases require two electrons for their catalytic cycle. For mammalian microsomal CYPs, key enzymes for xenobiotic metabolism and steroidogenesis and important drug targets and biocatalysts, the electrons are transferred by NADPH-cytochrome P450 oxidoreductase (CPR). No structure of a mammalian CYP-CPR complex has been solved experimentally, hindering understanding of the determinants of electron transfer (ET), which is often rate-limiting for CYP reactions. Here, we investigated the interactions between membrane-bound CYP 1A1, an antitumor drug target, and CPR by a multiresolution computational approach. We find that upon binding to CPR, the CYP 1A1 catalytic domain becomes less embedded in the membrane and reorients, indicating that CPR may affect ligand passage to the CYP active site. Despite the constraints imposed by membrane binding, we identify several arrangements of CPR around CYP 1A1 that are compatible with ET. In the complexes, the interactions of the CPR FMN domain with the proximal side of CYP 1A1 are supplemented by more transient interactions of the CPR NADP domain with the distal side of CYP 1A1. Computed ET rates and pathways agree well with available experimental data and suggest why the CYP-CPR ET rates are low compared to those of soluble bacterial CYPs.
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