ArticleNature communications2020
Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Synergistic Tuning of Conformational Dynamics, Electron Tunneling, and Substrate Positioning Enhances Electron Transfer in a P450 Chimera for Calcifediol Biosynthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Enhanced Catalytic Performance of P450 Monooxygenase CYP11B1 by Constructing Fusion Protein with Preferred Reductase Domain and Linker.Applied biochemistry and biotechnology · 2026Article
- Hydrogen-deuterium exchange reveals catalytically linked protein flexibility in myoglobin-mediated intramolecular C(spProtein science : a publication of the Protein Society · 2026Article
- A Dynamic Gate Enables Regioselective Hydroxylation of Free Arginine by a Non-Canonical Heme Enzyme.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Mechanism of Growth Phase-Dependent Nanoplastic Bioaccumulation inAntioxidants (Basel, Switzerland) · 2025Article
- Electron transfer engineering of artificially designed cell factory for complete biosynthesis of steroids.Nature communications · 2025Article
- 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
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- Characterization and Expression of the Cytochrome P450 Genes inInternational journal of molecular sciences · 2024Article
- A flexible linker of 8-amino acids between the membrane binding segment and the FMN domain of cytochrome P450 reductase is necessary for optimal activity.Journal of inorganic biochemistry · 2024Article
- Machine learning-assisted substrate binding pocket engineering based on structural information.Briefings in bioinformatics · 2024Article
- Cytochrome P450 for environmental remediation: catalytic mechanism, engineering strategies and future prospects.World journal of microbiology & biotechnology · 2023Review
- Differences of Atomic-Level Interactions between Midazolam and Two CYP Isoforms 3A4 and 3A5.Molecules (Basel, Switzerland) · 2023Article
- ALKBH5 facilitates CYP1B1 mRNA degradation via m6A demethylation to alleviate MSC senescence and osteoarthritis progression.Experimental & molecular medicine · 2023Article
- Improved Bioproduction of the Nylon 12 Monomer by Combining the Directed Evolution of P450 and Enhancing Heme Synthesis.Molecules (Basel, Switzerland) · 2023Article
- Engineering Catalytically Self-Sufficient P450s.Biochemistry · 2023Review
- Androgen Metabolism and Response in Prostate Cancer Anti-Androgen Therapy Resistance.International journal of molecular sciences · 2022Review
- Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Review
- Two-component carnitine monooxygenase from Escherichia coli: functional characterization, inhibition and mutagenesis of the molecular interface.Bioscience reports · 2022Article
Corrections and comments
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions. Self-sufficient cytochrome P450 enzymes contain the redox partners in a single polypeptide chain. Here, we present the crystal structure of full-length CYP116B46, a self-sufficient P450. The continuous polypeptide chain comprises three functional domains, which align well with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 Å. The role of several residues located between the [2Fe-2S] cluster and heme in the catalytic reaction is probed in mutagenesis experiments. These findings not only provide insights into the intramolecular electron transfer of self-sufficient P450s, but are also of interest for biotechnological applications of self-sufficient P450s.
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