ArticleArchives of biochemistry and biophysics2020
Functional interactions of adrenodoxin with several human mitochondrial cytochrome P450 enzymes.
Article in Archives of biochemistry and biophysics, 2020. 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.
- Mitochondrial Iron Handling and Lipid Peroxidation as Drivers of Ferroptosis.International journal of molecular sciences · 2026Review
- Heme and CO metabolism by the canonical human heme oxygenases.Journal of inorganic biochemistry · 2026Review
- Integrated network toxicology and multi-omics profiling reveal cell cycle, DNA damage repair, and metabolic alterations in cyclophosphamide-induced premature ovarian insufficiency.Frontiers in pharmacology · 2026Article
- Deep Mutational Scanning of FDX1 Identifies Key Structural Determinants of Lipoylation and Cuproptosis.Nature communications · 2025Article
- Exploring the roles of cytochrome P450 enzymes and their inhibitors in cancers and non-neoplastic human diseases.Archives of pharmacal research · 2025Review
- A molecular basis of Ferredoxin Reductase (FdxR) mutations that result in mitochondriopathies.Journal of inorganic biochemistry · 2025Article
- Optimization of CYP27A1 recombinant protein expression.Protein expression and purification · 2025Article
- 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
- Redox partner adrenodoxin alters cytochrome P450 11B1 ligand binding and inhibition.Journal of inorganic biochemistry · 2022Article
- Binding of cytochrome P450 27C1, a retinoid desaturase, to its accessory protein adrenodoxin.Archives of biochemistry and biophysics · 2021Article
- Tight binding of cytochrome bThe Journal of biological chemistryArticle
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Authors and funding
6 authors.
Funding
Abstract
Seven of the 57 human cytochrome P450 (P450) enzymes are mitochondrial and carry out important reactions with steroids and vitamins A and D. These seven P450s utilize an electron transport chain that includes NADPH, NADPH-adrenodoxin reductase (AdR), and adrenodoxin (Adx) instead of the diflavin NADPH-P450 reductase (POR) used by the other P450s in the endoplasmic reticulum. Although numerous studies have been published involving mitochondrial P450 systems, the experimental conditions vary considerably. We compared human Adx and bovine Adx, a commonly used component, and found very similar catalytic activities in reactions catalyzed by human P450s 11B2, 27A1, and 27C1. Binding constants of 6-200 nM were estimated for Adx binding to these P450s using microscale thermophoresis. All P450 catalytic reactions were saturated at 10 μM Adx, and higher concentrations were not inhibitory up to at least 50 μM. Collectively these studies demonstrate the tight binding of Adx (both human and bovine) to AdR and to several mitochondrial P450s and provide guidance for optimization of Adx-dependent P450 reactions.
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