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

The C-helix in CooA rolls upon CO binding to ferrous heme.

The Journal of biological chemistry - 5 Nov 2004

Yamashita Taku, Hoashi Yohei, Tomisugi Yoshikazu, Ishikawa Yoshinobu, Uno Tadayuki

Abstract excerpt

CooA is a homodimeric transcriptional activator from Rhodospirillum rubrum containing one heme in each subunit. CO binding to the heme in its sensor domain activates CooA, facilitating the binding to DNA by its DNA-binding domain. The C-helix links the two domains and shapes an interface between...

Read the complete abstract on PubMed

Topics

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

Share to Carbon Monoxide
Share to Databases as Topic
Share to Heme

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemeproteins

Share to Leucine

Share to Oxidation-Reduction

Share to Spectrum Analysis, Raman

Source

Identifiers

PMID: 15326178
DOI: 10.1074/jbc.M407766200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15326178-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The C-helix in CooA rolls upon CO binding to ferrous heme.PMID 15326178Read ↗

The role of the hydrophobic distal heme pocket of CooA in ligand sensing and response.Semantic proximity Read ↗

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

CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2.Semantic proximity Read ↗

Mapping CooA.RNA polymerase interactions. Identification of activating regions 2 and 3 in CooA, the co-sensing transcriptional activator.Semantic proximity Read ↗

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

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

Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Semantic proximity Read ↗

Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.Semantic proximity Read ↗

Identification of Cys94 as the distal ligand to the Fe(III) heme in the transcriptional regulator RcoM-2 from Burkholderia xenovorans.Semantic proximity Read ↗

Metal sensing and signal transduction by CnrX from Cupriavidus metallidurans CH34: role of the only methionine assessed by a functional, spectroscopic, and theoretical study.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 ↗

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