ArticleThe Journal of biological chemistry2015
Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c.
Article in The Journal of biological chemistry, 2015. 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.
- Impairing the interaction between Erg11 and cytochrome P450 reductase Ncp1 enhances azoles' antifungal activities.Nature communications · 2025Article
- Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of Human Cytochrome P450 1A2-Mediated Caffeine Metabolism.Biomolecules · 2023Article
- Electron transfer between cytochrome c and microsomal monooxygenase generates reactive oxygen species that accelerates apoptosis.Redox biology · 2022Article
- Differential effects on human cytochromes P450 by CRISPR/Cas9-induced genetic knockout of cytochrome P450 reductase and cytochrome b5 in HepaRG cells.Scientific reports · 2021Article
- Interaction Modes of Microsomal Cytochrome P450s with Its Reductase and the Role of Substrate Binding.International journal of molecular sciences · 2020Article
- 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
- Substrate mediated redox partner selectivity of cytochrome P450.Chemical communications (Cambridge, England) · 2018Article
- Solution structure of the cytochrome P450 reductase-cytochromeThe Journal of biological chemistry · 2018Article
- Application of methyl-TROSY to a large paramagnetic membrane protein without perdeuteration:Journal of biomolecular NMR · 2018Article
- Kinetic and Structural Characterization of the Effects of Membrane on the Complex of Cytochrome bScientific reports · 2017Article
- Correlation of Cytochrome P450 Oxidoreductase Expression with the Expression of 10 Isoforms of Cytochrome P450 in Human Liver.Drug metabolism and disposition: the biological fate of chemicals · 2016Article
- Recent Structural Insights into Cytochrome P450 Function.Trends in pharmacological sciences · 2016Review
- Selective Targeting of Heme Protein in Cytochrome P450 and Nitric Oxide Synthase by Diphenyleneiodonium.Toxicological sciences : an official journal of the Society of Toxicology · 2016Article
- Designed multi-stranded heme binding β-sheet peptides in membrane.Chemical science · 2016Article
- Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome c.The FEBS journal · 2015Article
- Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.PLoS biology · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Cytochrome P450 reductase (CPR) is a diflavin enzyme that transfers electrons to many protein partners. Electron transfer from CPR to cyt c has been extensively used as a model reaction to assess the redox activity of CPR. CPR is composed of multiple domains, among which the FMN binding domain (FBD) is the direct electron donor to cyt c. Here, electron transfer and complex formation between FBD and cyt c are investigated. Electron transfer from FBD to cyt c occurs at distinct rates that are dependent on the redox states of FBD. When compared with full-length CPR, FBD reduces cyt c at a higher rate in both the semiquinone and hydroquinone states. The NMR titration experiments reveal the formation of dynamic complexes between FBD and cyt c on a fast exchange time scale. Chemical shift mapping identified residues of FBD involved in the binding interface with cyt c, most of which are located in proximity to the solvent-exposed edge of the FMN cofactor along with other residues distributed around the surface of FBD. The structural model of the FBD-cyt c complex indicates two possible orientations of complex formation. The major complex structure shows a salt bridge formation between Glu-213/Glu-214 of FBD and Lys-87 of cyt c, which may be essential for the formation of the complex, and a predicted electron transfer pathway mediated by Lys-13 of cyt c. The findings provide insights into the function of CPR and CPR-cyt c interaction on a structural basis.
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