Cited by 84Enzyme Structure and FunctionMetal-Catalyzed Oxygenation MechanismsPharmacogenetics and Drug Metabolism

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Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase

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Aigrain, Louise, Pompon, Denis, Moréra, Solange, Truan, Gilles·2009·The EMBO Reports

DOI 10.1038/embor.2009.82PMC PMC2727436

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Abstract

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.

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Authors: Aigrain, L., Pompon, D., Moréra, S., & Truan, G.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Truan, Gilles
ORCID: Aigrain, Louise
Pompon, Denis
Moréra, Solange
Truan, Gilles
Venue: The EMBO Reports
Publisher: Springer Science and Business Media LLC
Published: 2009-05-29
Volume: 10
Issue: 7
Pages: 742-747
ISSN: 1469-221X (ISSN-L)
1469-3178
DOI: 10.1038/embor.2009.82
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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

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Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase

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