ArticleScientific reports2013
Dynamic interaction between membrane-bound full-length cytochrome P450 and cytochrome b5 observed by solid-state NMR spectroscopy.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 58 citations in OpenAlex.
- Redox partner exchanges between spatially confined complexes control the coupling effect of cytochrome bScientific reports · 2025Article
- Shedding Light on the Electron Delocalization Pathway at the [FeInorganic chemistry · 2025Article
- Direct interaction between the transmembrane helices stabilize cytochrome P450 2B4 and cytochrome b5 redox complex.Biophysical chemistry · 2023Article
- Transmembrane helices mediate the formation of a stable ternary complex of bCommunications biology · 2022Article
- Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing.Chemical communications (Cambridge, England) · 2021Article
- Solution of a Puzzle: High-Level Quantum-Chemical Treatment of Pseudocontact Chemical Shifts Confirms Classic Semiempirical Theory.The journal of physical chemistry letters · 2020Article
- Expression, purification, and functional reconstitution ofBiochimica et biophysica acta. Biomembranes · 2020Article
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Mechanisms of Specific versus Nonspecific Interactions of Aggregation-Prone Inhibitors and Attenuators.Journal of medicinal chemistry · 2019Article
- Validation of protein backbone structures calculated from NMR angular restraints using Rosetta.Journal of biomolecular NMR · 2019Article
- Influence of Transmembrane Helix Mutations on Cytochrome P450-Membrane Interactions and Function.Biophysical journal · 2019Article
- Reconstituted Discoidal High-Density Lipoproteins: Bioinspired Nanodiscs with Many Unexpected Applications.Current atherosclerosis reports · 2018Review
- Cytochrome-P450-Induced Ordering of Microsomal Membranes Modulates Affinity for Drugs.Angewandte Chemie (International ed. in English) · 2018Article
- Application of methyl-TROSY to a large paramagnetic membrane protein without perdeuteration:Journal of biomolecular NMR · 2018Article
- Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-bScientific reports · 2017Article
- The catalytic function of cytochrome P450 is entwined with its membrane-bound nature.F1000Research · 2017Review
- Structure of the transmembrane domain of human nicastrin-a component of γ-secretase.Scientific reports · 2016Article
- Inhibition of cytochrome P450 2B4 by environmentally persistent free radical-containing particulate matter.Biochemical pharmacology · 2015Article
- Effects of membrane mimetics on cytochrome P450-cytochrome b5 interactions characterized by NMR spectroscopy.The Journal of biological chemistry · 2015Article
- Analysis of cytochrome P450 CYP119 ligand-dependent conformational dynamics by two-dimensional NMR and X-ray crystallography.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as xenobiotic, toxic and 70% of the drugs in clinical use. Full-length cytochrome-b5 has been shown to be important for the catalytic activity of cytochrome-P450. Despite the significance in understanding the interactions between these two membrane-associated proteins, only limited high-resolution structural information on the full-length cytochrome-P450 and the cytochromes-b5-P450 complex is available. Here, we report a structural study on a functional ~72-kDa cytochromes-b5-P450 complex embedded in magnetically-aligned bicelles without having to freeze the sample. Functional and solid-state NMR (Nuclear Magnetic Resonance) data reveal interactions between the proteins in fluid lamellar phase bilayers. In addition, our data infer that the backbone structure and geometry of the transmembrane domain of cytochrome-b5 is not significantly altered due to its interaction with cytochrome-P450, whereas the mobility of cytochrome-b5 is considerably reduced.
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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.