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

Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy.

The Journal of biological chemistry - 14 Mar 2008

El-Mashtoly Samir F, Gu Yuzong, Yoshimura Hideaki, Yoshioka Shiro, Aono Shigetoshi, Kitagawa Teizo

Abstract excerpt

HemAT from Bacillus subtilis (HemAT-Bs) is a heme-based O2 sensor protein that acts as a signal transducer responsible for aerotaxis. HemAT-Bs discriminates its physiological effector (O2) from other gas molecules (CO and NO), although all of them bind to a heme. To monitor the conformational changes in the protein moiety upon binding of different ligands, we have investigated ultraviolet resonance Raman (UVRR)...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Heme

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemeproteins

Share to Hydrogen Bonding

Share to Molecular Conformation

Share to Oxygen

Share to Spectrophotometry, Ultraviolet

Share to Spectrum Analysis, Raman

Source

Identifiers

PMID: 18162468
DOI: 10.1074/jbc.M709209200

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

Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy.PMID 18162468Read ↗

Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis.Semantic proximity Read ↗

Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.Semantic proximity Read ↗

Resonance raman investigation of the specific sensing mechanism of a target molecule by gas sensory proteins.Semantic proximity Read ↗

Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS protein.Semantic proximity Read ↗

Unusually strong H-bonding to the heme ligand and fast geminate recombination dynamics of the carbon monoxide complex of Bacillus subtilis truncated hemoglobin.Semantic proximity Read ↗

Novel heme ligand displacement by CO in the soluble hemophore HasA and its proximal ligand mutants: implications for heme uptake and release.Semantic proximity Read ↗

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

Critical roles of Leu99 and Leu115 at the heme distal side in auto-oxidation and the redox potential of a heme-regulated phosphodiesterase from Escherichia coli.Semantic proximity Read ↗

The C-helix in CooA rolls upon CO binding to ferrous heme.Semantic proximity Read ↗

Heme pocket structural properties of a bacterial truncated hemoglobin from Thermobifida fusca.Semantic proximity Read ↗

Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA.Semantic proximity Read ↗

Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin.Semantic proximity Read ↗

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