ArticleScientific reports2019
Coupling of Redox and Structural States in Cytochrome P450 Reductase Studied by Molecular Dynamics Simulation.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Enhanced Sampling of Protein Conformations in AlphaFold3 with Repulsive Bias in the Diffusion Generative Model.JACS Au · 2026Article
- Enzymatic and Biophysical Analysis of two Highly Related Cytochrome P450 Reductases frombioRxiv : the preprint server for biology · 2026Article
- Recent Advances in Elucidating the Mechanism of the NADPH-Cytochrome P450 Reductase-Mediated Electron Transfer Cycle: Experimental and Computational Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Heme Regulatory Motif of Heme Oxygenase-2 Is Involved in the Interaction with NADPH-Cytochrome P450 Reductase and Regulates Enzymatic Activity.International journal of molecular sciences · 2025Article
- Gene fusion and functional diversification ofMycology · 2024Article
- Noncovalent interactions that tune the reactivities of the flavins in bifurcating electron transferring flavoprotein.The Journal of biological chemistry · 2023Article
- Improved Bioproduction of the Nylon 12 Monomer by Combining the Directed Evolution of P450 and Enhancing Heme Synthesis.Molecules (Basel, Switzerland) · 2023Article
- Modulating catalytic activity of a modified flavin analogueRSC advances · 2022Article
- Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps.The Biochemical journal · 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
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome P450 reductase (CPR) is the key protein that regulates the electron transfer from NADPH to various heme-containing monooxygenases. CPR has two flavin-containing domains: one with flavin adenine dinucleotide (FAD), called FAD domain, and the other with flavin mononucleotide (FMN), called FMN domain. It is considered that the electron transfer occurs via FAD and FMN (NADPH → FAD → FMN → monooxygenase) and is regulated by an interdomain open-close motion. It is generally thought that the structural state is coupled with the redox state, which, however, has not yet been firmly established. In this report, we studied the coupling of the redox and the structural states by full-scale molecular dynamics (MD) simulation of CPR (total 86.4 μs). Our MD result showed that while CPR predominantly adopts the closed state both in the oxidized and reduced states, it exhibits a tendency to open in the reduced state. We also found a correlation between the FAD-FMN distance and the predicted FMN-monooxygenase distance, which is embedded in the equilibrium thermal fluctuation of CPR. Based on these results, a physical mechanism for the electron transfer by CPR is discussed.
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