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

Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002.

Biochemistry - 24 Aug 2010

Scott Nancy L, Xu Yu, Shen Gaozhong, Vuletich David A, Falzone Christopher J, Li Zhongkui, Ludwig Marcus, Pond Matthew P, Preimesberger Matthew R, Bryant Donald A, Lecomte Juliette T J

Abstract excerpt

Cyanobacterium Synechococcus sp. PCC 7002 contains a single gene (glbN) coding for GlbN, a protein of the 2/2 hemoglobin lineage. The precise function of GlbN is not known, but comparison to similar 2/2 hemoglobins suggests that reversible dioxygen binding is not its main activity. In this report, the results of in vitro and in vivo experiments probing the role of GlbN are presented. Transcription profiling...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli
Share to Gene Expression Regulation, Bacterial

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

Share to Hemoglobins

Share to Models, Molecular

Share to Protein Conformation

Share to Synechococcus

Share to Transcription, Genetic

Source

Identifiers

PMID: 20669934
DOI: 10.1021/bi100463d

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

Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002.PMID 20669934Read ↗

NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo.Semantic proximity Read ↗

The mechanism of iron homeostasis in the unicellular cyanobacterium synechocystis sp. PCC 6803 and its relationship to oxidative stress.Semantic proximity Read ↗

The AbrB2 autorepressor, expressed from an atypical promoter, represses the hydrogenase operon to regulate hydrogen production in Synechocystis strain PCC6803.Semantic proximity Read ↗

The search for new chlorophyll-binding proteins in the cyanobacterium Synechocystis sp. PCC 6803.Semantic proximity Read ↗

Stability and Folding of the Unusually Stable Hemoglobin from Synechocystis is Subtly Optimized and Dependent on the Key Heme Pocket Residues.Semantic proximity Read ↗

An AbrB-like transcriptional regulator, Sll0822, is essential for the activation of nitrogen-regulated genes in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

CyAbrB2 Contributes to the Transcriptional Regulation of Low CO2 Acclimation in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

A heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. PCC 6803: modes of differential operation of two isoforms/enzymes to adapt to low oxygen environments in cyanobacteria.Semantic proximity Read ↗

Expression and mutational analysis of the glnB genomic region in the heterocyst-forming Cyanobacterium Anabaena sp. strain PCC 7120.Semantic proximity Read ↗

A membrane-associated Mn-superoxide dismutase protects the photosynthetic apparatus and nitrogenase from oxidative damage in the Cyanobacterium Anabaena sp. PCC 7120.Semantic proximity Read ↗

Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress.Semantic proximity Read ↗

Free fatty acid production in the cyanobacterium Synechocystis sp. PCC 6803 is enhanced by deletion of the cyAbrB2 transcriptional regulator.Semantic proximity Read ↗

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