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

1H NMR studies of the paramagnetic CuA center of cytochrome oxidase.

FEBS letters - 7 Oct 1996

Dennison C, Berg A, de Vries S, Canters G W

Abstract excerpt

The dinuclear paramagnetic center of the soluble CuA domain of the cytochrome c oxidase from Bacillus subtilis has been studied using 1H NMR. The spectrum possesses remarkably sharp shifted resonances. Comparison with the spectrum of the CuA amicyanin variant provides the spin density distribution in the CuA site of cytochrome c oxidase. This represents the first paramagnetic NMR study of the dinuclear CuA center...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Bacterial Proteins
Share to Binding Sites

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

Share to Electron Transport Complex IV

Share to Magnetic Resonance Spectroscopy

Share to Mutation

Share to Peptide Fragments

Share to Recombinant Proteins

Source

Identifiers

PMID: 8830670
DOI: 10.1016/0014-5793(96)00981-7

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.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

1H NMR studies of the paramagnetic CuA center of cytochrome oxidase.PMID 8830670Read ↗

1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.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 ↗

Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Semantic proximity Read ↗

Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts.Semantic proximity Read ↗

Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.Semantic proximity Read ↗

Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR.Semantic proximity Read ↗

Pulsed EPR/ENDOR characterization of perturbations of the Cu(A) center ground state by axial methionine ligand mutations.Semantic proximity Read ↗

EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.Semantic proximity Read ↗

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