Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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 - 1 Jun 2012

Li Wenbing, Fan Weihong, Chen Li, Elmore Bradley O, Piazza Mike, Guillemette J Guy, Feng Changjian

Abstract excerpt

In the crystal structure of a calmodulin (CaM)-bound FMN domain of human inducible nitric oxide synthase (NOS), the CaM-binding region together with CaM forms a hinge, and pivots on an R536(NOS)/E47(CaM) pair (Xia et al. J Biol Chem 284:30708-30717, 2009). Notably, isoform-specific human inducible NOS S562 and C563 residues form hydrogen bonds with the R536 residue through their backbone oxygens. In this study,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Calmodulin
Share to Electron Transport

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Flavin Mononucleotide

Share to Hydrogen Bonding

Share to Nitric Oxide Synthase Type II

Share to Protein Isoforms

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 22407542
DOI: 10.1007/s00775-012-0887-y
PMCID: PMC3526944

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase.PMID 22407542Read ↗

An isoform-specific pivot modulates the electron transfer between the flavin mononucleotide and heme centers in inducible nitric oxide synthase.Semantic proximity Read ↗

Intra- and inter-molecular effects of a conserved arginine residue of neuronal and inducible nitric oxide synthases on FMN and calmodulin binding.Semantic proximity Read ↗

Structural Basis of Electron Transfer by the Human Nitric Oxide Synthase Holoenzyme ComplexSemantic proximity Read ↗

Structural Mechanism of Electron Shuttling in Inducible Nitric Oxide SynthaseSemantic proximity Read ↗

Molecular dynamics study of in silico mutations in the auto-inhibitory loop of human endothelial nitric oxide synthase FMN sub-domain.Semantic proximity Read ↗

Lobe-specific calcium binding in calmodulin regulates endothelial nitric oxide synthase activation.Semantic proximity Read ↗

A cross-domain charge interaction governs the activity of NO synthase.Semantic proximity Read ↗

Domain interactions in neuronal nitric oxide synthase identified by time-resolved fluorescence.Semantic proximity Read ↗

Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.Semantic proximity Read ↗

The role of a conserved serine residue within hydrogen bonding distance of FAD in redox properties and the modulation of catalysis by Ca2+/calmodulin of constitutive nitric-oxide synthases.Semantic proximity Read ↗

Intra-subunit and inter-subunit electron transfer in neuronal nitric-oxide synthase: effect of calmodulin on heterodimer catalysis.Semantic proximity Read ↗

Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.