ArticleThe Journal of biological chemistry2016
Cytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMR.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Structural context of NADPH-cytochrome P450 reductase mutations that alter cytochrome P450 1A2 substrate regioselectivity.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Deletion of the Mouse Homolog of Human FHR1 (muFHR1) Alleviates Atherosclerosis in ApoE-/- mice.International journal of medical sciences · 2026Article
- Tracking protein-protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochromePhysical chemistry chemical physics : PCCP · 2024Article
- Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of Human Cytochrome P450 1A2-Mediated Caffeine Metabolism.Biomolecules · 2023Article
- Non-steroidal CYP17A1 Inhibitors: Discovery and Assessment.Journal of medicinal chemistry · 2023Review
- Steroid 17α-hydroxylase/17, 20-lyase (cytochrome P450 17A1).Methods in enzymology · 2023Article
- Four Decades of Cytochrome P450 2B Research: From Protein Adducts to Protein Structures and Beyond.Drug metabolism and disposition: the biological fate of chemicals · 2023Review
- Thermodynamic Driving Forces of Redox-Dependent CPR Insertion into Biomimetic Endoplasmic Reticulum Membranes.The journal of physical chemistry. B · 2022Article
- Measurement of Residual Dipolar Couplings Using Magnetically Aligned and Flipped Nanodiscs.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Exploiting photosynthesis-driven P450 activity to produce indican in tobacco chloroplasts.Frontiers in plant science · 2022Article
- Structural Basis for the Diminished Ligand Binding and Catalytic Ability of Human Fetal-Specific CYP3A7.International journal of molecular sciences · 2021Article
- Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing.Chemical communications (Cambridge, England) · 2021Article
- Substrate-Specific Allosteric Effects on the Enhancement of CYP17A1 Lyase Efficiency by CytochromeJournal of the American Chemical Society · 2021Article
- An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase.Communications biology · 2021Article
- Crystal Structures of Drug-Metabolizing CYPs.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Probing protein-protein and protein-substrate interactions in the dynamic membrane-associated ternary complex of cytochromes P450, bChemical communications (Cambridge, England) · 2019Article
- Probing membrane enhanced protein-protein interactions in a minimal redox complex of cytochrome-P450 and P450-reductase.Chemical communications (Cambridge, England) · 2019Article
- A Minimal Functional Complex of Cytochrome P450 and FBD of Cytochrome P450 Reductase in Nanodiscs.Angewandte Chemie (International ed. in English) · 2018Article
- Cytochrome bFEBS letters · 2018Article
- Substrate mediated redox partner selectivity of cytochrome P450.Chemical communications (Cambridge, England) · 2018Article
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3 authors.
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Abstract
To accomplish key physiological processes ranging from drug metabolism to steroidogenesis, human microsomal cytochrome P450 enzymes require the sequential input of two electrons delivered by the FMN domain of NADPH-cytochrome P450 reductase. Although some human microsomal P450 enzymes can instead accept the second electron from cytochrome b5, for human steroidogenic CYP17A1, the cytochrome P450 reductase FMN domain delivers both electrons, and b5 is an allosteric modulator. The structural basis of these key but poorly understood protein interactions was probed by solution NMR using the catalytically competent soluble domains of each protein. Formation of the CYP17A1·FMN domain complex induced differential line broadening of the NMR signal for each protein. Alterations in the exchange dynamics generally occurred for residues near the surface of the flavin mononucleotide, including 87-90 (loop 1), and for key CYP17A1 active site residues. These interactions were modulated by the identity of the substrate in the buried CYP17A1 active site and by b5. The FMN domain outcompetes b5 for binding to CYP17A1 in the three-component system. These results and comparison with previous NMR studies of the CYP17A1·b5 complex suggest a model of CYP17A1 enzyme regulation.
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