ArticleBiophysical journal2015
A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Cryo-EM reveals an ensemble of cytochrome P450 reductase conformations in solution.Protein science : a publication of the Protein Society · 2026Article
- 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
- Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase.Nature communications · 2021Article
- Interaction Modes of Microsomal Cytochrome P450s with Its Reductase and the Role of Substrate Binding.International journal of molecular sciences · 2020Article
- Conformational Equilibrium of NADPH-Cytochrome P450 Oxidoreductase Is Essential for Heme Oxygenase Reaction.Antioxidants (Basel, Switzerland) · 2020Article
- The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promiscuous Interactions With Structurally Diverse Redox Partners.Frontiers in pharmacology · 2020Article
- Biochemical and structural insights into the cytochrome P450 reductase from Candida tropicalis.Scientific reports · 2019Article
- Coupling of Redox and Structural States in Cytochrome P450 Reductase Studied by Molecular Dynamics Simulation.Scientific reports · 2019Article
- Enzyme-fusion strategies for redirecting and improving carotenoid synthesis inMetabolic engineering communications · 2019Article
- Probing the Role of the Hinge Segment of Cytochrome P450 Oxidoreductase in the Interaction with Cytochrome P450.International journal of molecular sciences · 2018Article
- Direct observation of multiple conformational states in Cytochrome P450 oxidoreductase and their modulation by membrane environment and ionic strength.Scientific reports · 2018Article
- Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Scientific reports · 2017Article
- Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis.The Journal of biological chemistry · 2017Article
- The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.Frontiers in pharmacology · 2017Article
- Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast Transient Absorption Spectroscopy.Biochemistry · 2016Article
- Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.The Journal of biological chemistry · 2016Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diflavin reductases are bidomain electron transfer proteins in which structural reorientation is necessary to account for the various intramolecular and intermolecular electron transfer steps. Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions. The CPR enzyme exists in a salt- and pH-dependent rapid equilibrium between a previously described rigid, locked state and a newly characterized, highly flexible, unlocked state. We further establish that maximal electron flux through CPR is conditioned by adjustable stability of the locked-state domain interface under resting conditions. This is rationalized by a kinetic scheme coupling rapid conformational sampling and slow chemical reaction rates. Regulated domain interface stability associated with fast stochastic domain contacts during the catalytic cycle thus provides, to our knowledge, a new paradigm for improving our understanding of multidomain enzyme function.
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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.