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

Electron-electron distances in spin-labeled low-spin metmyoglobin variants by relaxation enhancement.

Biophysical journal - 1 Dec 2008

Ulyanov Dmitriy, Bowler Bruce E, Eaton Gareth R, Eaton Sandra S

Abstract excerpt

Thirteen single-cysteine variants of myoglobin were prepared by overexpression of apoprotein, spin labeling, and reconstitution with hemin. This procedure resulted in a protein with fewer hemichrome impurities than was obtained by an overexpression of holo-protein followed by spin labeling. Coordination of cyanide to the met heme formed low-spin complexes. Iron-nitroxyl interspin distances in the range of 17-30 A...

Read the complete abstract on PubMed

Topics

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

Share to Electron Spin Resonance Spectroscopy
Share to Electrons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Mutation

Share to Spin Labels

Share to Temperature

Share to Time Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 18775958
DOI: 10.1529/biophysj.108.141887
PMCID: PMC2586584

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

Electron-electron distances in spin-labeled low-spin metmyoglobin variants by relaxation enhancement.PMID 18775958Read ↗

Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.Semantic proximity Read ↗

A General Model to Optimise Copper(II) Labelling Efficiency of Double-Histidine Motifs for Pulse Dipolar EPR ApplicationsSemantic proximity Read ↗

Alkylamine-ligated H93G myoglobin cavity mutant: a model system for endogenous lysine and terminal amine ligation in heme proteins such as nitrite reductase and cytochrome f.Semantic proximity Read ↗

Effect of Outer-Sphere Side Chain Substitutions on the Fate of the trans Iron-Nitrosyl Dimer in Heme/Nonheme Engineered Myoglobins (Fe(B)Mbs): Insights into the Mechanism of Denitrifying NO Reductases.Semantic proximity Read ↗

Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the alpha-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface.Semantic proximity Read ↗

Low microwave-amplitude ESR spectroscopy: measuring spin-relaxation interactions of moderately immobilized spin labels in proteins.Semantic proximity Read ↗

Ultrafast dynamics of resonance energy transfer in myoglobin: probing local conformation fluctuations.Semantic proximity Read ↗

Binding of histidine in the (Cys)3(His)1-coordinated [2Fe-2S] cluster of human mitoNEET.Semantic proximity Read ↗

Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant.Semantic proximity Read ↗

Protein ligand migration mapped by nonequilibrium 2D-IR exchange spectroscopy.Semantic proximity Read ↗

Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.Semantic proximity Read ↗

Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c.Semantic proximity Read ↗

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