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

On the mechanism of quinol oxidation at the QP site in the cytochrome bc1 complex: studied using mutants lacking cytochrome bL or bH.

The Journal of biological chemistry - 17 Oct 2008

Yang Shaoqing, Ma He-Wen, Yu Linda, Yu Chang-An

Abstract excerpt

To elucidate the mechanism of bifurcated oxidation of quinol in the cytochrome bc1 complex, Rhodobacter sphaeroides mutants, H198N and H111N, lacking heme bL and heme bH, respectively, were constructed and characterized. Purified mutant complexes have the same subunit composition as that of the wild-type complex, but have only 9-11% of the electron transfer activity, which is sensitive to stigmatellin or...

Read the complete abstract on PubMed

Topics

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

Share to Antimycin A
Share to Cytochromes
Share to Cytochromes b

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

Share to Electron Transport

Share to Electron Transport Complex III

Share to Horses

Share to Rhodobacter sphaeroides

Source

Open in PubMed Open full text

Identifiers

PMID: 18713733
DOI: 10.1074/jbc.M803013200
PMCID: PMC2568935

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

On the mechanism of quinol oxidation at the QP site in the cytochrome bc1 complex: studied using mutants lacking cytochrome bL or bH.PMID 18713733Read ↗

The rate-limiting step in the cytochrome bc1 complex (Ubiquinol-Cytochrome c Oxidoreductase) is not changed by inhibition of cytochrome b-dependent deprotonation: implications for the mechanism of ubiquinol oxidation at center P of the bc1 complex.Semantic proximity Read ↗

ROS production by cytochrome bc1: Its mechanism as inferred from the effects of heme b cofactor mutants.Semantic proximity Read ↗

Functional flexibility of electron flow between quinol oxidation Qo site of cytochrome bc1 and cytochrome c revealed by combinatory effects of mutations in cytochrome b, iron-sulfur protein and cytochrome c1.Semantic proximity Read ↗

Mutations at the Qo Site of the Cytochrome bc1 Complex Strongly Affect Oxygen Binding.Semantic proximity Read ↗

ROS signaling capacity of cytochrome bc1: Opposing effects of adaptive and pathogenic mitochondrial mutations.Semantic proximity Read ↗

Cytochrome b6 arginine 214 of Synechococcus sp. PCC 7002, a key residue for quinone-reductase site function and turnover of the cytochrome bf complex.Semantic proximity Read ↗

A compilation of mutations located in the cytochrome b subunit of the bacterial and mitochondrial bc1 complex.Semantic proximity Read ↗

Modification of inhibitor binding sites in the cytochrome bf complex by directed mutagenesis of cytochrome b(6) in Synechococcus sp. PCC 7002.Semantic proximity Read ↗

Formation of engineered intersubunit disulfide bond in cytochrome bc1 complex disrupts electron transfer activity in the complex.Semantic proximity Read ↗

The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex.Semantic proximity Read ↗

Electron sweep across four b-hemes of cytochrome bc1 revealed by unusual paramagnetic properties of the Qi semiquinone intermediate.Semantic proximity Read ↗

The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex.Semantic proximity Read ↗

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