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

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

The Journal of biological chemistry - 2 Oct 1998

Aono S, Ohkubo K, Matsuo T, Nakajima H

Abstract excerpt

The transcriptional activator CooA from Rhodospirillum rubrum contains a b-type heme that acts as a CO sensor in vivo. CooA is the first example of a transcriptional regulator containing a heme as a prosthetic group and of a hemeprotein in which CO plays a physiological role. In this study, we constructed an in vivo reporter system to measure the transcriptional activator activity of CooA and prepared some CooA...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Genes, Reporter
Share to Ligands

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Oxidation-Reduction

Share to Recombinant Proteins

Share to Trans-Activators

Share to Transcriptional Activation

Source

Identifiers

PMID: 9748246
DOI: 10.1074/jbc.273.40.25757

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA.PMID 9748246Read ↗

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

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

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 ↗

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

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

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

Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli.Semantic proximity Read ↗

Molecular structure of redox metal centers of the cytochrome bo complex from Escherichia coli. Spectroscopic characterizations of the subunit I histidine mutant oxidases.Semantic proximity Read ↗

New insights into the mechanism of nickel insertion into carbon monoxide dehydrogenase: analysis of Rhodospirillum rubrum carbon monoxide dehydrogenase variants with substituted ligands to the [Fe3S4] portion of the active-site C-cluster.Semantic proximity Read ↗

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

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