ArticleStructure (London, England : 1993)2013
Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 77 citations in OpenAlex.
- Enzymatic and Biophysical Analysis of two Highly Related Cytochrome P450 Reductases frombioRxiv : the preprint server for biology · 2026Article
- Structure and dynamics of a multidomain nitric oxide synthase regulated by a C2 domain.Science advances · 2026Article
- 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
- Recent Advances in Elucidating the Mechanism of the NADPH-Cytochrome P450 Reductase-Mediated Electron Transfer Cycle: Experimental and Computational Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.Nature communications · 2025Article
- Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.bioRxiv : the preprint server for biology · 2025Article
- Sedimentation of large, soluble proteins up to 140 kDa forJournal of biomolecular NMR · 2024Article
- Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of Human Cytochrome P450 1A2-Mediated Caffeine Metabolism.Biomolecules · 2023Article
- Exploring optimal Taxol® CYP725A4 activity in Saccharomyces cerevisiae.Microbial cell factories · 2022Article
- Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase.Biophysical journal · 2022Article
- Conformational Rearrangements in the Redox Cycling of NADPH-Cytochrome P450 Reductase fromBiology · 2022Article
- Thermodynamic Driving Forces of Redox-Dependent CPR Insertion into Biomimetic Endoplasmic Reticulum Membranes.The journal of physical chemistry. B · 2022Article
- Conformational states and fluctuations in endothelial nitric oxide synthase under calmodulin regulation.Biophysical journal · 2021Article
- Fundamentals to function: Quantitative and scalable approaches for measuring protein stability.Cell systems · 2021Review
- Structural and kinetic investigations of the carboxy terminus of NADPH-cytochrome P450 oxidoreductase.Archives of biochemistry and biophysics · 2021Article
- Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase.Nature communications · 2021Article
- Conformational Landscape of Cytochrome P450 Reductase Interactions.International journal of molecular sciences · 2021Article
- Conformational Equilibrium of NADPH-Cytochrome P450 Oxidoreductase Is Essential for Heme Oxygenase Reaction.Antioxidants (Basel, Switzerland) · 2020Article
- Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.Nature communications · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
NADPH-cytochrome P450 reductase is a key component of the P450 mono-oxygenase drug-metabolizing system. There is evidence for a conformational equilibrium involving large-scale domain motions in this enzyme. We now show, using small-angle X-ray scattering (SAXS) and small-angle neutron scattering, that delivery of two electrons to cytochrome P450 reductase leads to a shift in this equilibrium from a compact form, similar to the crystal structure, toward an extended form, while coenzyme binding favors the compact form. We present a model for the extended form of the enzyme based on nuclear magnetic resonance and SAXS data. Using the effects of changes in solution conditions and of site-directed mutagenesis, we demonstrate that the conversion to the extended form leads to an enhanced ability to transfer electrons to cytochrome c. This structural evidence shows that domain motion is linked closely to the individual steps of the catalytic cycle of cytochrome P450 reductase, and we propose a mechanism for this.
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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.