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

Interaction of nitric oxide with human heme oxygenase-1.

The Journal of biological chemistry - 24 Jan 2003

Wang Jinling, Lu Shen, Moënne-Loccoz Pierre, Ortiz de Montellano Paul R

Abstract excerpt

NO and CO may complement each other as signaling molecules in some physiological situations. We have examined the binding of NO to human heme oxygenase-1 (hHO-1), an enzyme that oxidizes heme to biliverdin, CO, and free iron, to determine whether inhibition of hHO-1 by NO can contribute to the signaling interplay of NO and CO. An Fe(3+)-NO hHO-1-heme complex is formed with NO or the NO donors NOC9 or...

Read the complete abstract on PubMed

Topics

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

Share to Bilirubin
Share to Heme
Share to Heme Oxygenase-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heme Oxygenase (Decyclizing)

Share to Nitric Oxide

Share to Spectrophotometry

Share to Spectroscopy, Fourier Transform Infrared

Share to Spectrum Analysis, Raman

Source

Identifiers

PMID: 12433915
DOI: 10.1074/jbc.M211131200

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

Interaction of nitric oxide with human heme oxygenase-1.PMID 12433915Read ↗

Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins.Semantic proximity Read ↗

The Gasotransmitter Trio (NO, CO, H₂S) in Cardiovascular Health and Disease: From Molecular Crosstalk to Precision Gas MedicineSemantic proximity Read ↗

Dr. NO and Mr. Toxic – the versatile role of nitric oxideSemantic proximity Read ↗

Distal-to-proximal NO conversion in hemoproteins: the role of the proximal pocket.Semantic proximity Read ↗

Cross-talk between NO and oxyradicals, a supersystem that regulates energy metabolism and survival of animals.Semantic proximity Read ↗

Oxygen activation in neuronal NO synthase: resolving the consecutive mono-oxygenation steps.Semantic proximity Read ↗

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

Regulation of the properties of the heme-NO complexes in nitric-oxide synthase by hydrogen bonding to the proximal cysteine.Semantic proximity Read ↗

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

Investigation of Cyanide Ligand as an Active Site Probe of Human Heme Oxygenase.Semantic proximity Read ↗

NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism.Semantic proximity Read ↗

Trans effects in nitric oxide binding to myoglobin cavity mutant H93G.Semantic proximity Read ↗

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