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

Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.

Biophysical journal - 1 Apr 2005

Zhang Wei, Olson John S, Phillips George N

Abstract excerpt

HemAT from Bacillus subtilis is a new type of heme protein responsible for sensing oxygen. The structural and functional properties of the full-length HemAT protein, the sensor domain (1-178), and Tyr-70 mutants have been characterized. Kinetic and equilibrium measurements reveal that both full-length HemAT and the sensor domain show two distinct O(2) binding components. The high-affinity component has a...

Read the complete abstract on PubMed

Topics

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

Share to Biophysics
Share to Carbon Monoxide
Share to Heme

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Spectrophotometry

Share to Spectrophotometry, Infrared

Share to Spectroscopy, Fourier Transform Infrared

Share to Tryptophan

Share to Ultracentrifugation

Source

Open in PubMed Open full text

Identifiers

PMID: 15653746
DOI: 10.1529/biophysj.104.047936
PMCID: PMC1305375

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

Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.PMID 15653746Read ↗

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

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

Minimal requirements for oxygen sensing by the aerotaxis receptor Aer.Semantic proximity Read ↗

Conservation and diversity of ancient hemoglobins in Bacteria.Semantic proximity Read ↗

Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.Semantic proximity Read ↗

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

Functional properties of human hemoglobins synthesized from recombinant mutant beta-globins.Semantic proximity Read ↗

Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure.Semantic proximity Read ↗

The Five Near-iron Transporter (NEAT) Domain Anthrax Hemophore, IsdX2, Scavenges Heme from Hemoglobin and Transfers Heme to the Surface Protein IsdCSemantic proximity Read ↗

Hemoglobin Dallas (alpha 97(G4)Asn-->Lys): functional characterization of a high oxygen affinity natural mutant.Semantic proximity Read ↗

Bacterial Nitric-oxide Synthases Operate without a Dedicated Redox PartnerSemantic proximity Read ↗

Control of Oxygen Affinity in Mammalian Hemoglobins: Implications for a System Biology Description of the Respiratory Properties of the Red Blood Cell.Semantic proximity Read ↗

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