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

Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.

Biochemistry - 11 Oct 2005

Sawai Hitomi, Makino Masatomo, Mizutani Yasuhisa, Ohta Takehiro, Sugimoto Hiroshi, Uno Tadayuki, Kawada Norifumi, Yoshizato Katsutoshi, Kitagawa Teizo, Shiro Yoshitsugu

Abstract excerpt

Cytoglobin (Cgb) and neuroglobin (Ngb) are the first examples of hexacoordinated globins from humans and other vertebrates in which a histidine (His) residue at the sixth position of the heme iron is an endogenous ligand in both the ferric and ferrous forms. Static and time-resolved resonance Raman and FT-IR spectroscopic techniques were applied in examining the structures in the heme environment of these...

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 Crystallography

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

Share to Globins

Share to Nitric Oxide

Share to Photolysis

Share to Spectroscopy, Fourier Transform Infrared

Share to Spectrum Analysis, Raman

Source

Identifiers

PMID: 16201751
DOI: 10.1021/bi050997o

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

Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.PMID 16201751Read ↗

Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps.Semantic proximity Read ↗

Roles of N- and C-terminal domains in the ligand-binding properties of cytoglobin.Semantic proximity Read ↗

Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance.Semantic proximity Read ↗

Dynamic features of carboxy cytoglobin distal mutants investigated by molecular dynamics simulations.Semantic proximity Read ↗

Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism.Semantic proximity Read ↗

A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin.Semantic proximity Read ↗

Human neuroglobin and H64A distal variant: How mutation and pH affect the heme pocket.Semantic proximity Read ↗

The structure of murine neuroglobin: Novel pathways for ligand migration and binding.Semantic proximity Read ↗

Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: implications for nitric oxide sensors.Semantic proximity Read ↗

EPR investigation of the role of B10 phenylalanine in neuroglobin - evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation.Semantic proximity Read ↗

Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobinSemantic proximity Read ↗

Cytoglobin: A Novel Globin Type Ubiquitously Expressed inVertebrate TissuesSemantic proximity Read ↗

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