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

Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.

Proceedings of the National Academy of Sciences of the United States of America - 6 Jun 2017

Liang Ruibin, Swanson Jessica M J, Wikström Mårten, Voth Gregory A

Abstract excerpt

Cytochrome c oxidase (CcO) catalyzes the reduction of oxygen to water and uses the released free energy to pump protons against the transmembrane proton gradient. To better understand the proton-pumping mechanism of the wild-type (WT) CcO, much attention has been given to the mutation of amino acid residues along the proton translocating D-channel that impair, and sometimes decouple, proton pumping from the...

Read the complete abstract on PubMed

Topics

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

Share to Biochemical Phenomena
Share to Computer Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Transport Complex IV

Share to Ion Transport

Share to Molecular Dynamics Simulation

Share to Oxidation-Reduction

Share to Proton Pumps

Share to Protons

Source

Open in PubMed Open full text

Identifiers

PMID: 28536198
DOI: 10.1073/pnas.1703654114
PMCID: PMC5468613

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

Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.PMID 28536198Read ↗

Kinetic gating of the proton pump in cytochrome c oxidase.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 ↗

A carboxylate switch point controls long-range energy transduction in respiratory Complex I.Semantic proximity Read ↗

Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping.Semantic proximity Read ↗

Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump.Semantic proximity Read ↗

Insights into proton translocation in cbb3 oxidase from MD simulations.Semantic proximity Read ↗

Subunit III-depleted cytochrome c oxidase provides insight into the process of proton uptake by proteins.Semantic proximity Read ↗

A Carboxylate Switch Point Controls Long-Range Energy Transduction in Respiratory Complex ISemantic proximity Read ↗

Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides cytochrome c oxidase.Semantic proximity Read ↗

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

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

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