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

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

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Dec 2020

Zheng Huayu, Li Jinghui, Feng Changjian

Abstract excerpt

Intraprotein interdomain electron transfer (IET) between the flavin mononucleotide (FMN) and heme centers is an obligatory step in nitric oxide synthase (NOS) enzymes. An isoform-specific pivotal region near Leu406 in the heme domain of human inducible NOS (iNOS) was proposed to mediate the FMN-heme domain-domain alignment (J Inorg Biochem 153:186-196, 2015). The FMN-heme IET rate is a measure of the interdomain...

Read the complete abstract on PubMed

Topics

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

Share to Electron Transport
Share to Flavin Mononucleotide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isoenzymes

Share to Kinetics

Share to Molecular Docking Simulation

Share to Nitric Oxide Synthase Type II

Share to Protein Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 33057871
DOI: 10.1007/s00775-020-01824-w
PMCID: PMC7669679

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An isoform-specific pivot modulates the electron transfer between the flavin mononucleotide and heme centers in inducible nitric oxide synthase.PMID 33057871Read ↗

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

Solving Kinetic Equations for the Laser Flash Photolysis Experiment on Nitric Oxide Synthases: Effect of Conformational Dynamics on the Interdomain Electron Transfer.Semantic proximity Read ↗

Mutations in the FMN domain modulate MCD spectra of the heme site in the oxygenase domain of inducible nitric oxide synthase.Semantic proximity Read ↗

Dynamic regulation of the inducible nitric-oxide synthase by NO: comparison with the endothelial isoform.Semantic proximity Read ↗

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

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

Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.Semantic proximity Read ↗

Distal Val346Ile mutation in inducible NO synthase promotes substrate-dependent NO confinement.Semantic proximity Read ↗

Critical role of the neuronal nitric-oxide synthase heme proximal side residue, Arg418, in catalysis and electron transfer.Semantic proximity Read ↗

A conserved tryptophan in nitric oxide synthase regulates heme-dioxy reduction by tetrahydrobiopterin.Semantic proximity Read ↗

Revisiting the Val/Ile Mutation in Mammalian and Bacterial Nitric Oxide Synthases: A Spectroscopic and Kinetic Study.Semantic proximity Read ↗

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

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