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

Role of conformational change and K-path ligands in controlling cytochrome c oxidase activity.

Biochemical Society transactions - 15 Oct 2017

Liu Jian, Hiser Carrie, Ferguson-Miller Shelagh

Abstract excerpt

Given the central role of cytochrome c oxidase (CcO) in health and disease, it is an increasingly important question as to how the activity and efficiency of this key enzyme are regulated to respond to a variety of metabolic states. The present paper summarizes evidence for two modes of regulation of activity: first, by redox-induced conformational changes involving the K-proton uptake path; and secondly, by...

Read the complete abstract on PubMed

Topics

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

Share to Bacteria
Share to Binding Sites
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Electron Transport Complex IV

Share to Ligands

Share to Potassium

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 28842531
DOI: 10.1042/BST20160138
PMCID: PMC6103453

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

Role of conformational change and K-path ligands in controlling cytochrome c oxidase activity.PMID 28842531Read ↗

The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.Semantic proximity Read ↗

Conformational coupling between the active site and residues within the K(C)-channel of the Vibrio cholerae cbb3-type (C-family) oxygen reductase.Semantic proximity Read ↗

A universal coupling mechanism of respiratory complex I.Semantic proximity Read ↗

Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase.Semantic proximity Read ↗

On the role of the K-proton transfer pathway in cytochrome c oxidase.Semantic proximity Read ↗

Variable proton-pumping stoichiometry in structural variants of cytochrome c 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 ↗

Exploring the ubiquinone binding cavity of respiratory complex I.Semantic proximity Read ↗

Proton transfer in uncoupled variants of cytochrome c oxidase.Semantic proximity Read ↗

Allosteric interactions and proton conducting pathways in proton pumping aa(3) oxidases: heme a as a key coupling element.Semantic proximity Read ↗

Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects.Semantic proximity Read ↗

Intricate role of water in proton transport through cytochrome c oxidase.Semantic proximity Read ↗

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