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

Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.

Biochimica et biophysica acta. Bioenergetics - 1 Sept 2018

Maréchal Amandine, Hartley Andrew M, Warelow Thomas P, Meunier Brigitte, Rich Peter R

Abstract excerpt

Redox and CO photolysis FTIR spectra of yeast cytochrome c oxidase WT and mutants are compared to those from bovine and P. denitrificans CcOs in order to establish common functional features. All display changes that can be assigned to their E242 (bovine numbering) equivalent and to weakly H-bonded water molecules. The additional redox-sensitive band reported at 1736 cm-1 in bovine CcO and previously assigned to...

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 Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Transport Complex IV

Share to Oxidation-Reduction

Share to Photolysis

Share to Saccharomyces cerevisiae Proteins

Share to Spectroscopy, Fourier Transform Infrared

Source

Open in PubMed Open full text

Identifiers

PMID: 29852141
DOI: 10.1016/j.bbabio.2018.05.018
PMCID: PMC6094048

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.PMID 29852141Read ↗

Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy.Semantic proximity Read ↗

Yeast cytochrome c oxidase: a model system to study mitochondrial forms of the haem-copper oxidase superfamily.Semantic proximity Read ↗

Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe mutant enzymes.Semantic proximity Read ↗

ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase.Semantic proximity Read ↗

The Increase in the Peroxidase Activity of the Cytochrome C with Substitutions in the Universal Binding Site Is Associated with Changes in the Ability to Interact with External Ligands.Semantic proximity Read ↗

Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase.Semantic proximity Read ↗

Mutations in the Ca2+ binding site of the Paracoccus denitrificans cytochrome c oxidase.Semantic proximity Read ↗

Fine-tuning of the binding and dissociation of CO by the amino acids of the heme pocket of Coprinus cinereus peroxidase.Semantic proximity Read ↗

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

Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.Semantic proximity Read ↗

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47.Semantic proximity Read ↗

Interactions between the cytochrome b, cytochrome c1, and Fe-S protein subunits at the ubihydroquinone oxidation site of the bc1 complex of Rhodobacter capsulatus.Semantic proximity Read ↗

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