ReviewJournal of inorganic biochemistry2014
Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.
Review in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Glutamine Substitution at LysineACS omega · 2026Article
- Interdomain Interactions Modulate the Active Site Dynamics of Human Inducible Nitric Oxide Synthase.The journal of physical chemistry. B · 2022Article
- Conformational states and fluctuations in endothelial nitric oxide synthase under calmodulin regulation.Biophysical journal · 2021Article
- Tetrahydrobiopterin redox cycling in nitric oxide synthase: evidence supports a through-heme electron delivery.The FEBS journal · 2016Article
- The tetrahydrobiopterin radical interacting with high- and low-spin heme in neuronal nitric oxide synthase - A new indicator of the extent of NOS coupling.Free radical biology & medicine · 2016Article
- Elucidating nitric oxide synthase domain interactions by molecular dynamics.Protein science : a publication of the Protein Society · 2016Article
- Neuronal Nitric Oxide Synthase in Vascular Physiology and Diseases.Frontiers in physiology · 2016Review
- 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
- Comparison of oxygen-induced radical intermediates in iNOS oxygenase domain with those from nNOS and eNOS.Journal of inorganic biochemistry · 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
- Molecular mechanisms of neuronal nitric oxide synthase in cardiac function and pathophysiology.The Journal of physiology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nitric oxide synthase (NOS), a flavo-hemoprotein, is responsible for biosynthesis of nitric oxide (NO) in mammals. Three NOS isoforms, iNOS, eNOS and nNOS (inducible, endothelial, and neuronal NOS), achieve their biological functions by tight control of interdomain electron transfer (IET) process through interdomain interactions. In particular, the FMN-heme IET is essential in coupling electron transfer in the reductase domain with NO synthesis in the heme domain by delivery of electrons required for O2 activation at the catalytic heme site. Emerging evidence indicates that calmodulin (CaM) activates NO synthesis in eNOS and nNOS by a conformational change of the FMN domain from its shielded electron-accepting (input) state to a new electron-donating (output) state, and that CaM is also required for proper alignment of the FMN and heme domains in the three NOS isoforms. In the absence of a structure of full-length NOS, an integrated approach of spectroscopic, rapid kinetic and mutagenesis methods is required to unravel regulation mechanism of the FMN-heme IET process. This is to investigate the roles of the FMN domain motions and the docking between the primary functional FMN and heme domains in regulating NOS activity. The recent developments in this area that are driven by the combined approach are the focuses of this review. A better understanding of the roles of interdomain FMN/heme interactions and CaM binding may serve as a basis for the rational design of new selective modulators of the NOS enzymes.
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