ArticleFEBS letters2013
Calmodulin-induced structural changes in endothelial nitric oxide synthase.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Glutamine Substitution at LysineACS omega · 2026Article
- Conformational states and fluctuations in endothelial nitric oxide synthase under calmodulin regulation.Biophysical journal · 2021Article
- Use of Computational Biochemistry for Elucidating Molecular Mechanisms of Nitric Oxide Synthase.Computational and structural biotechnology journal · 2019Review
- A docked state conformational dynamics model to explain the ionic strength dependence of FMN - heme electron transfer in nitric oxide synthase.Journal of inorganic biochemistry · 2018Article
- Role of an isoform-specific residue at the calmodulin-heme (NO synthase) interface in the FMN - heme electron transfer.FEBS letters · 2018Article
- Exploring the conformations of nitric oxide synthase with fluorescence.Frontiers in bioscience (Landmark edition) · 2018Review
- Deciphering mechanism of conformationally controlled electron transfer in nitric oxide synthases.Frontiers in bioscience (Landmark edition) · 2018Review
- Nitric oxide synthase and structure-based inhibitor design.Nitric oxide : biology and chemistry · 2017Review
- Correlating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic Trap.ACS catalysis · 2016Article
- Elucidating nitric oxide synthase domain interactions by molecular dynamics.Protein science : a publication of the Protein Society · 2016Article
- Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics study.Journal of inorganic biochemistry · 2015Article
- Solving Kinetic Equations for the Laser Flash Photolysis Experiment on Nitric Oxide Synthases: Effect of Conformational Dynamics on the Interdomain Electron Transfer.The journal of physical chemistry. A · 2015Article
- Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Fluorescence quenching studies of structure and dynamics in calmodulin-eNOS complexes.FEBS letters · 2015Article
- Article
- Potential role of nitric oxide synthase isoforms in pathophysiology of neuropathic pain.Inflammopharmacology · 2014Review
- Holoenzyme structures of endothelial nitric oxide synthase - an allosteric role for calmodulin in pivoting the FMN domain for electron transfer.Journal of structural biology · 2014Article
- Molecular architecture of mammalian nitric oxide synthases.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Pulsed electron paramagnetic resonance study of domain docking in neuronal nitric oxide synthase: the calmodulin and output state perspective.The journal of physical chemistry. A · 2014Article
- Energy landscapes and catalysis in nitric-oxide synthase.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
We have derived structures of intact calmodulin (CaM)-free and CaM-bound endothelial nitric oxide synthase (eNOS) by reconstruction from cryo-electron micrographs. The CaM-free reconstruction is well fitted by the oxygenase domain dimer, but the reductase domains are not visible, suggesting they are mobile and thus delocalized. Additional protein is visible in the CaM-bound reconstruction, concentrated in volumes near two basic patches on each oxygenase domain. One of these corresponds with a presumptive docking site for the reductase domain FMN-binding module. The other is proposed to correspond with a docking site for CaM. A model is suggested in which CaM binding and docking position the reductase domains near the oxygenase domains and promote docking of the FMN-binding modules required for electron transfer.
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