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

The quantum mechanically mixed-spin state in a non-symbiotic plant hemoglobin: the effect of distal mutation on AHb1 from Arabidopsis thaliana.

Journal of inorganic biochemistry - 1 Nov 2007

Droghetti Enrica, Howes Barry D, Feis Alessandro, Dominici Paola, Fittipaldi Maria, Smulevich Giulietta

Abstract excerpt

Non-symbiotic hemoglobins are hexacoordinated heme proteins found in all plants. To gain insight into the importance of the heme hexacoordination and the coordinated distal histidine in general for the possible physiological functions of these proteins, the distal His(E7) of Arabidopsis thaliana hemoglobin (AHb1) was substituted by a leucine residue. The heme properties of the wild-type and mutant proteins have...

Read the complete abstract on PubMed

Topics

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

Share to Arabidopsis Proteins
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemeproteins

Share to Hemoglobins

Share to Mutagenesis, Site-Directed

Share to Plant Proteins

Share to Spectrum Analysis, Raman

Share to Temperature

Source

Identifiers

PMID: 17686524
DOI: 10.1016/j.jinorgbio.2007.06.035

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

The quantum mechanically mixed-spin state in a non-symbiotic plant hemoglobin: the effect of distal mutation on AHb1 from Arabidopsis thaliana.PMID 17686524Read ↗

Structural plasticity and functional implications of internal cavities in distal mutants of type 1 non-symbiotic hemoglobin AHb1 from Arabidopsis thaliana.Semantic proximity Read ↗

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

Chemical shift-based constraints for solution structure determination of paramagnetic low-spin heme proteins with bis-His and His-CN axial ligands: the cases of oxidized cytochrome b(5) and Met80Ala cyano-cytochrome c.Semantic proximity Read ↗

A new way to understand quaternary structure changes of hemoglobin upon ligand binding on the basis of UV-resonance Raman evaluation of intersubunit interactions.Semantic proximity Read ↗

Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy.Semantic proximity Read ↗

Static normal coordinate deformations of the heme group in mutants of ferrocytochrome c from Saccharomyces cerevisiae probed by resonance Raman spectroscopy.Semantic proximity Read ↗

Primary charge separation in the photosystem II core from Synechocystis: a comparison of femtosecond visible/midinfrared pump-probe spectra of wild-type and two P680 mutants.Semantic proximity Read ↗

The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase.Semantic proximity Read ↗

Influence of mutations at the proximal histidine position on the Fe-O2 bond in hemoglobin from density functional theory.Semantic proximity Read ↗

Intersubunit distances in full-length, dimeric, bacterial phytochrome Agp1, as measured by pulsed electron-electron double resonance (PELDOR) between different spin label positions, remain unchanged upon photoconversion.Semantic proximity Read ↗

Electron spin-lattice relaxation of the [Cu(1.5) ... Cu(1.5)] dinuclear copper center in nitrous oxide reductase.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 ↗

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