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

Mutational analysis of the Qi-site proton pathway in yeast cytochrome bc1 complex.

Biochemical and biophysical research communications - 12 Mar 2020

Song Zehua, Hu Yangfeng, Iorga Bogdan I, Vallières Cindy, Fisher Nicholas, Meunier Brigitte

Abstract excerpt

The respiratory cytochrome bc1 complex functions as a protonmotive ubiquinol:cytochrome c oxidoreductase. Lysine 228 (K228) located within the quinol reduction (Qi) site of the bc1 complex, has been reported as a key residue for proton transfer during the redox chemistry cycle to substrate quinone at Qi. In yeast, while single mutations had no effect, the combination of K228L and F225L resulted in a severe...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes b
Share to Electron Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Oxygen

Share to Proton-Motive Force

Share to Protons

Share to Saccharomyces cerevisiae Proteins

Share to Ubiquinone

Source

Identifiers

PMID: 31941609
DOI: 10.1016/j.bbrc.2019.12.102

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

Mutational analysis of the Qi-site proton pathway in yeast cytochrome bc1 complex.PMID 31941609Read ↗

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

QO site deficiency can be compensated by extragenic mutations in the hinge region of the iron-sulfur protein in the bc1 complex of Saccharomyces cerevisiae.Semantic proximity Read ↗

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

Disease-related mutations in cytochrome c oxidase studied in yeast and bacterial models.Semantic proximity Read ↗

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

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

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

Disruption of the interaction between the Rieske iron-sulfur protein and cytochrome b in the yeast bc1 complex owing to a human disease-associated mutation within cytochrome b.Semantic proximity Read ↗

Functional effects of mutations in cytochrome c oxidase related to prostate cancer.Semantic proximity Read ↗

Mitochondrial disease-related mutations at the cytochrome b-iron-sulfur protein (ISP) interface: Molecular effects on the large-scale motion of ISP and superoxide generation studied in Rhodobacter capsulatus cytochrome bc1.Semantic proximity Read ↗

Analysis of suppressor mutation reveals long distance interactions in the bc(1) complex of Saccharomyces cerevisiae.Semantic proximity Read ↗

Critical structural role of R481 in cytochrome c oxidase from Rhodobacter sphaeroides.Semantic proximity Read ↗

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