ArticleProtein science : a publication of the Protein Society2024
Structural dynamics and functional cooperativity of human NQO1 by ambient temperature serial crystallography and simulations.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 15 citations in OpenAlex.
- Tyrosine residues at the substrate binding site in human NQO1 homodimer: Protein conformational dynamics and optimization of substrate binding geometry.The FEBS journal · 2026Article
- Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.Free radical biology & medicine · 2026Review
- Article
- Minimized sample consumption for time-resolved serial crystallography applied to the redox cycle of human NQO1.Communications chemistry · 2026Article
- Mechanism of cyanobacterial ferredoxin-dependent flavin thioredoxin reductase reveals thiolate-FAD charge transfer and catalytic asymmetry in a homodimer.The FEBS journal · 2026Article
- Matrine Alleviates Sepsis-Induced Acute Lung Injury by Reinforcing NQO1/SLC7A11/GPX4-Associated Anti-Ferroptotic Defenses and Attenuating NF-κB-Driven Inflammation.Drug design, development and therapy · 2026Article
- Monoammonium glycyrrhizinate ameliorates mitochondrial dysfunction-mediated oxidative stress and neuroinflammation via the NRF2/NQO1 axis after spinal cord injury.Redox report : communications in free radical research · 2025Article
- Application of signal separation to diffraction image compression and serial crystallography.Journal of applied crystallography · 2025Article
- Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.Communications chemistry · 2025Article
- Cyclic Olefin Copolymer-Based Fixed-Target Sample Delivery Device for Protein X-ray Crystallography.Analytical chemistry · 2024Article
- Sheet-on-sheet fixed target data collection devices for serial crystallography at synchrotron and XFEL sources.Journal of applied crystallography · 2024Article
- Evolutionary analysis of Quinone Reductases 1 and 2 suggests that NQO2 evolved to function as a pseudoenzyme.Protein science : a publication of the Protein Society · 2024Article
- Innovative Strategies in X-ray Crystallography for Exploring Structural Dynamics and Reaction Mechanisms in Metabolic Disorders.Journal of personalized medicine · 2024Review
- Structural dynamics and functional cooperativity of human NQO1 by ambient temperature serial crystallography and simulations.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
9 authors at 5 institutions in 4 countries.
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Abstract
The human NQO1 (hNQO1) is a flavin adenine nucleotide (FAD)-dependent oxidoreductase that catalyzes the two-electron reduction of quinones to hydroquinones, being essential for the antioxidant defense system, stabilization of tumor suppressors, and activation of quinone-based chemotherapeutics. Moreover, it is overexpressed in several tumors, which makes it an attractive cancer drug target. To decipher new structural insights into the flavin reductive half-reaction of the catalytic mechanism of hNQO1, we have carried serial crystallography experiments at new ID29 beamline of the ESRF to determine, to the best of our knowledge, the first structure of the hNQO1 in complex with NADH. We have also performed molecular dynamics simulations of free hNQO1 and in complex with NADH. This is the first structural evidence that the hNQO1 functional cooperativity is driven by structural communication between the active sites through long-range propagation of cooperative effects across the hNQO1 structure. Both structural results and MD simulations have supported that the binding of NADH significantly decreases protein dynamics and stabilizes hNQO1 especially at the dimer core and interface. Altogether, these results pave the way for future time-resolved studies, both at x-ray free-electron lasers and synchrotrons, of the dynamics of hNQO1 upon binding to NADH as well as during the FAD cofactor reductive half-reaction. This knowledge will allow us to reveal unprecedented structural information of the relevance of the dynamics during the catalytic function of hNQO1.
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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.