The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase
Open accessAbstract
Two catalytic domains, bearing FMN and FAD cofactors, joined by a connecting domain, compose the core of the NADPH cytochrome P450 reductase (CPR). The FMN domain of CPR mediates electron shuttling from the FAD domain to cytochromes P450. Together, both enzymes form the main mixed-function oxidase system that participates in the metabolism of endo- and xenobiotic compounds in mammals. Available CPR structures show a closed conformation, with the two cofactors in tight proximity, which is consistent with FAD-to-FMN, but not FMN-to-P450, electron transfer. Here, we report the 2.5 A resolution crystal structure of a functionally competent yeast-human chimeric CPR in an open conformation, compatible with FMN-to-P450 electron transfer. Comparison with closed structures shows a major conformational change separating the FMN and FAD cofactors from 86 A.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Kabsch, W. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889893005588 · Cited by 3,562
Cytochrome P450 and Chemical Toxicology
Guengerich, F. P. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700079z · Cited by 1,789
Cytochrome P450 systems—biological variations of electron transport chains
Hannemann, F., Bichet, A., Ewen, K. M., & Bernhardt, R. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.07.017 · Cited by 763
Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S. S., & Kim, J.-J. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8411 · Cited by 744
Structure of a cytochrome P450-redox partner electron-transfer complex
Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A., & Poulos, T. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1863 · Cited by 501
Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains.
Smith, G. C., Tew, D. G., & Wolf, C. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8710 · Cited by 137
Dodhia, V. R., Fantuzzi, A., & Gilardi, G. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0144-3 · Cited by 80
Lamb, D. C., Kim, Y., Yermalitskaya, L. V., Yermalitsky, V. N., Lepesheva, G. I., Kelly, S. L., Waterman, M. R., & Podust, L. M. (2006) · Structure · doi:10.1016/j.str.2005.09.015 · Cited by 60
Cited by
Sorted by citations
Insect CYP Genes and P450 Enzymes
Feyereisen, R. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384747-8.10008-x · Cited by 633
Esteves, F., Rueff, J., & Kranendonk, M. (2021) · Journal of Xenobiotics · doi:10.3390/jox11030007 · Cited by 561
NADPH P450 oxidoreductase: Structure, function, and pathology of diseases
Pandey, A. V., & Flück, C. E. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.010 · Cited by 279
Šrejber, M., Navrátilová, V., Paloncýová, M., Bazgier, V., Berka, K., Anzenbacher, P., & Otyepka, M. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.03.002 · Cited by 202
Domain Motion in Cytochrome P450 Reductase
Ellis, J., Gutierrez, A., Barsukov, I. L., Huang, W.-C., Grossmann, J. G., & Roberts, G. C. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054304 · Cited by 140
Metadata
- Authors
- Aigrain, L., Pompon, D., Moréra, S., & Truan, G.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Truan, Gilles
- Venue
- The EMBO Reports
- Published
- 2009-05-29
- Volume
- 10
- Issue
- 7
- Pages
- 742-747
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2727436
- OpenAlex
- W2094484494
- Semantic Scholar
- 7c1ff3af72968ecac7c1c0f53a79884af883a9db
- Cited by
- 84
- References
- 20
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 2 · 2023: 1 · 2022: 5 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 5 · 2017: 4 · 2016: 3 · 2015: 9 · 2014: 4 · 2013: 5 · 2012: 4
- FWCI
- 4.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Keywords
- NADPH-cytochrome P450 reductase, open conformation, FMN cofactor, FAD cofactor, mixed function oxidase, chimeric enzymes, conformational change, crystal structure, electron shuttling
- MeSH terms
- Humans, NADPH-Ferrihemoprotein Reductase, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Protein Structure, Secondary, Crystallography, X-Ray, Cytochromes c, Cytochrome P-450 CYP3A
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
