ArticleThe Journal of biological chemistry
Structural and functional insights into aldosterone synthase interaction with its redox partner protein adrenodoxin.
Article in The Journal of biological chemistry. 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.
- The regulatory potential of cytochrome P450-adrenodoxin interactions: Insights toward understanding redox partner regulation in drug metabolizing enzymes.Drug metabolism and disposition: the biological fate of chemicals · 2026Review
- Supporting activities of cognate redox partners for sterol-metabolizing P450 enzymes in Mycobacterium neoaurum.The Journal of biological chemistry · 2026Article
- Mass spectrometry footprinting reveals microsomal CYP2A6 structural changes induced by interaction with its reductase flavin mononucleotide domain.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Mycobacteriumabscessus CYP123 is a steroid hydroxylase with an implication in host infection.Drug metabolism and disposition: the biological fate of chemicals · 2025Article
- The curious family of cytochrome P450 4F fatty acid ω-hydroxylases: recent developments in their function and relevance for human health.Open biology · 2025Review
- Characterization of lncRNA-protein interactions associated with Prostate cancer and Androgen receptors by molecular docking simulations.Biochemistry and biophysics reports · 2025Article
- Human Cytochrome P450 Cancer-Related Metabolic Activities and Gene Polymorphisms: A Review.Cells · 2024Review
- Interactions of human mitochondrial Ferredoxin 1 (Adrenodoxin) by NMR; modulation by cytochrome P450 substrate and by truncation of the C-terminal tail.Journal of inorganic biochemistry · 2023Article
- Allosteric modulation of cytochrome P450 enzymes by the NADPH cytochrome P450 reductase FMN-containing domain.The Journal of biological chemistry · 2023Article
- Aldosterone: Renal Action and Physiological Effects.Comprehensive Physiology · 2023Article
- Drug Metabolism: A Half-Century Plus of Progress, Continued Needs, and New Opportunities.Drug metabolism and disposition: the biological fate of chemicals · 2023Article
- Generation of human steroidogenic cytochrome P450 enzymes for structural and functional characterization.Methods in enzymology · 2023Article
- Redox partner adrenodoxin alters cytochrome P450 11B1 ligand binding and inhibition.Journal of inorganic biochemistry · 2022Article
- Unravelling the role of transient redox partner complexes in P450 electron transfer mechanics.Scientific reports · 2022Article
- Characterization of a Cleavable Fusion of Human CYP24A1 with Adrenodoxin Reveals the Variable Role of Hydrophobics in Redox Partner Binding.Biochemistry · 2022Article
- Diverse reactions catalyzed by cytochrome P450 and biosynthesis of steroid hormone.Biophysics and physicobiology · 2022Article
- Binding of cytochrome P450 27C1, a retinoid desaturase, to its accessory protein adrenodoxin.Archives of biochemistry and biophysics · 2021Article
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2 authors.
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Abstract
Aldosterone is the major mineralocorticoid in the human body controlling blood pressure and salt homeostasis. Overproduction of aldosterone leads to primary aldosteronism, which is the most common form of secondary hypertension with limited treatment options. Production of aldosterone by cytochrome P450 11B2 (CYP11B2, aldosterone synthase) requires two reduction events with the electrons delivered by the iron/sulfur protein adrenodoxin. Very limited information is available about the structural and functional basis of adrenodoxin/CYP11B2 interaction, which impedes the development of new treatment options for primary aldosteronism. A systematic study was carried out to determine if adrenodoxin interaction with CYP11B2 might also have an allosteric component in addition to electron transfer. Indeed, local increases in adrenodoxin concentration promote binding of the substrate 11-deoxycorticosterone and the inhibitor osilodrostat (LCI699) in the active site-over 17 Å away-as well as enhance the inhibitory effect of this latter drug. The CYP11B2 structure in complex with adrenodoxin identified specific residues at the protein-protein interface interacting via five salt bridges and four hydrogen bonds. Comparisons with cholesterol-metabolizing CYP11A1 and cortisol-producing CYP11B1, which also bind adrenodoxin, revealed substantial structural differences in these regions. The structural and functional differences between different P450 interactions with adrenodoxin may provide valuable clues for an orthogonal treatment approach for primary aldosteronism by specifically targeting the interaction between CYP11B2 and adrenodoxin.
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