ReviewArchives of biochemistry and biophysics2012
NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
54 citing papers in PubMed, 116 citations in OpenAlex.
- 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
- 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
- Recent Advances in Elucidating the Mechanism of the NADPH-Cytochrome P450 Reductase-Mediated Electron Transfer Cycle: Experimental and Computational Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Catalytic Dioxygen Activation Using a Diketopiperazine and a Manganese Catalyst for Selective C(spJACS Au · 2025Article
- 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
- Effects of aflatoxin B1 on subacute exposure of hybrid groupers (Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2024Article
- Modulating Nitric Oxide: Implications for Cytotoxicity and Cytoprotection.Antioxidants (Basel, Switzerland) · 2024Review
- Allosteric modulation of cytochrome P450 enzymes by the NADPH cytochrome P450 reductase FMN-containing domain.The Journal of biological chemistry · 2023Article
- Metabolic Engineering of Model Microorganisms for the Production of Xanthophyll.Microorganisms · 2023Review
- Self-cleaving guide RNAs enable pharmacological selection of precise gene editing events in vivo.Nature communications · 2022Article
- Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Review
- Confrontation of AlphaFold models with experimental structures enlightens conformational dynamics supporting CYP102A1 functions.Scientific reports · 2022Article
- A disease-associated missense mutation in CYP4F3 affects the metabolism of leukotriene B4 via disruption of electron transfer.Journal of cachexia, sarcopenia and muscle · 2022Article
- Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase.Biophysical journal · 2022Article
- The FMN "140s Loop" of Cytochrome P450 Reductase Controls Electron Transfer to Cytochrome P450.International journal of molecular sciences · 2021Article
- Therapeutic liver repopulation by transient acetaminophen selection of gene-modified hepatocytes.Science translational medicine · 2021Article
- Structural and kinetic investigations of the carboxy terminus of NADPH-cytochrome P450 oxidoreductase.Archives of biochemistry and biophysics · 2021Article
- Sterol regulatory element-binding protein Sre1 regulates carotenogenesis in the red yeastJournal of lipid research · 2020Article
- Reconsidering Aromatase for Breast Cancer Treatment: New Roles for an Old Target.Molecules (Basel, Switzerland) · 2020Review
- Conformational Equilibrium of NADPH-Cytochrome P450 Oxidoreductase Is Essential for Heme Oxygenase Reaction.Antioxidants (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
NADPH-cytochrome P450 oxidoreductase (CYPOR) and nitric oxide synthase (NOS), two members of the diflavin oxidoreductase family, are multi-domain enzymes containing distinct FAD and FMN domains connected by a flexible hinge. FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 or NOS oxygenase domain. Structural analysis of CYPOR, the prototype of this enzyme family, has revealed the exact nature of the domain arrangement and the role of residues involved in cofactor binding. Recent structural and biophysical studies of CYPOR have shown that the two flavin domains undergo large domain movements during catalysis. NOS isoforms contain additional regulatory elements within the reductase domain that control electron transfer through Ca(2+)-dependent calmodulin (CaM) binding. The recent crystal structure of an iNOS Ca(2+)/CaM-FMN construct, containing the FMN domain in complex with Ca(2+)/CaM, provided structural information on the linkage between the reductase and oxgenase domains of NOS, making it possible to model the holo iNOS structure. This review summarizes recent advances in our understanding of the dynamics of domain movements during CYPOR catalysis and the role of the NOS diflavin reductase domain in the regulation of NOS isozyme activities.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.