ArticleDalton transactions (Cambridge, England : 2003)2009
Regulation of interdomain electron transfer in the NOS output state for NO production.
Article in Dalton transactions (Cambridge, England : 2003), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- 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
- Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Journal of inorganic biochemistry · 2014Review
- Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.The FEBS journal · 2013Article
- Regulatory role of Glu546 in flavin mononucleotide-heme electron transfer in human inducible nitric oxide synthase.Inorganic chemistry · 2013Article
- Construction and analysis of the protein-protein interaction network related to essential hypertension.BMC systems biology · 2013Article
- The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.The Journal of biological chemistry · 2012Article
- Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Coordination chemistry reviews · 2012Article
- Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins.FEBS letters · 2012Article
- Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme.Biochimica et biophysica acta · 2011Article
- Pulsed ENDOR determination of relative orientation of g-frame and molecular frame of imidazole-coordinated heme center of iNOS.The journal of physical chemistry. A · 2011Article
- Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase.FEBS letters · 2011Article
- Mutation in the flavin mononucleotide domain modulates magnetic circular dichroism spectra of the iNOS ferric cyano complex in a substrate-specific manner.Inorganic chemistry · 2011Article
- Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin.FEBS letters · 2010Article
- Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase.Journal of the American Chemical Society · 2010Article
- A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
There is still much that is unknown about how nitric oxide (NO) biosynthesis by NO synthase (NOS) isoform is tightly regulated at the molecular level. This is remarkable because deviated NO production in vivo has been implicated in an increasing number of diseases that currently lack effective treatments, including stroke and cancer. Given the significant public health burden of these diseases, the NOS enzyme family is a key target for development of new pharmaceuticals. Three NOS isoforms, inducible, endothelial and neuronal NOS (iNOS, eNOS and nNOS, respectively), achieve their key biological functions via stringent regulations of interdomain electron transfer (IET) processes. Unlike iNOS, eNOS and nNOS isoforms are controlled by calmodulin (CaM) binding through facilitating catalytically significant IET processes. The CaM-modulated NOS output state is an IET-competent complex between the flavin mononucleotide (FMN) domain and the catalytic heme domain. The output state facilitates the catalytically essential FMN-heme IET, and thereby enables NO production by NOS. Due to lack of reliable techniques for specifically determining the inter-domain FMN-heme interactions and their direct effects on the catalytic heme center, the molecular mechanism that underlies the output state formation remains elusive. The recent developments in our understanding of mechanisms of the NOS output state formation that are driven by a combination of molecular biology, laser flash photolysis, and spectroscopic techniques are the subject of this perspective.
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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.