ArticleScientific reports2015
Insights into the role of substrates on the interaction between cytochrome b5 and cytochrome P450 2B4 by NMR.
Article in Scientific reports, 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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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.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Redox partner exchanges between spatially confined complexes control the coupling effect of cytochrome bScientific reports · 2025Article
- Direct interaction between the transmembrane helices stabilize cytochrome P450 2B4 and cytochrome b5 redox complex.Biophysical chemistry · 2023Article
- Optimization of Multiparameters for Increased Yields of Cytochrome B5 in Bioreactors.Molecules (Basel, Switzerland) · 2021Article
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- Expression, purification, and functional reconstitution ofBiochimica et biophysica acta. Biomembranes · 2020Article
- Probing protein-protein and protein-substrate interactions in the dynamic membrane-associated ternary complex of cytochromes P450, bChemical communications (Cambridge, England) · 2019Article
- Specificity of the Redox Complex between Cytochrome P450 24A1 and Adrenodoxin Relies on Carbon-25 Hydroxylation of Vitamin-D Substrate.Drug metabolism and disposition: the biological fate of chemicals · 2019Article
- Probing the Role of the Hinge Segment of Cytochrome P450 Oxidoreductase in the Interaction with Cytochrome P450.International journal of molecular sciences · 2018Article
- Effect of polymer charge on functional reconstitution of membrane proteins in polymer nanodiscs.Chemical communications (Cambridge, England) · 2018Article
- Substrate mediated redox partner selectivity of cytochrome P450.Chemical communications (Cambridge, England) · 2018Article
- The cytochrome P450 24A1 interaction with adrenodoxin relies on multiple recognition sites that vary among species.The Journal of biological chemistry · 2018Article
- Structural and functional effects of cytochromeThe Journal of biological chemistry · 2017Article
- Kinetic and Structural Characterization of the Effects of Membrane on the Complex of Cytochrome bScientific reports · 2017Article
- The catalytic function of cytochrome P450 is entwined with its membrane-bound nature.F1000Research · 2017Review
- Designed multi-stranded heme binding β-sheet peptides in membrane.Chemical science · 2016Article
- Molecular Basis of MgATP Selectivity of the Mitochondrial SCaMC Carrier.Structure (London, England : 1993) · 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
7 authors at 2 institutions in 1 country.
Funding
Abstract
Mammalian cytochrome b5 (cyt b5) is a membrane-bound protein capable of donating an electron to cytochrome P450 (P450) in the P450 catalytic cycle. The interaction between cyt b5 and P450 has been reported to be affected by the substrates of P450; however, the mechanism of substrate modulation on the cyt b5-P450 complex formation is still unknown. In this study, the complexes between full-length rabbit cyt b5 and full-length substrate-free/substrate-bound cytochrome P450 2B4 (CYP2B4) are investigated using NMR techniques. Our findings reveal that the population of complexes is ionic strength dependent, implying the importance of electrostatic interactions in the complex formation process. The observation that the cyt b5-substrate-bound CYP2B4 complex shows a weaker dependence on ionic strength than the cyt b5-substrate-free CYP2B4 complex suggests the presence of a larger fraction of steoreospecific complexes when CYP2B4 is substrate-bound. These results suggest that a CYP2B4 substrate likely promotes specific interactions between cyt b5 and CYP2B4. Residues D65, V66, T70, D71 and A72 are found to be involved in specific interactions between the two proteins due to their weak response to ionic strength change. These findings provide insights into the mechanism underlying substrate modulation on the cyt b5-P450 complexation process.
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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.