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

Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli.

Biochimica et biophysica acta. Bioenergetics - 1 May 2017

Choi Sylvia K, Lin Myat T, Ouyang Hanlin, Gennis Robert B

Abstract excerpt

The cytochrome bo3 ubiquinol oxidase is one of three respiratory oxygen reductases in the aerobic respiratory chain of Escherichia coli. The generally accepted model of catalysis assumes that cyt bo3 contains two distinct ubiquinol binding sites: (i) a low affinity (QL) site which is the traditional substrate binding site; and (ii) a high affinity (QH) site where a "permanently" bound quinone acts as a cofactor,...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Cytochrome b Group
Share to Cytochromes

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

Share to Escherichia coli Proteins

Share to Oxidation-Reduction

Share to Structure-Activity Relationship

Share to Ubiquinone

Source

Identifiers

PMID: 28235459
DOI: 10.1016/j.bbabio.2017.02.008

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

Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli.PMID 28235459Read ↗

The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli.Semantic proximity Read ↗

Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.Semantic proximity Read ↗

Characterization of mutants that change the hydrogen bonding of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli.Semantic proximity Read ↗

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

Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.Semantic proximity Read ↗

Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.Semantic proximity Read ↗

Ubiquinol-binding site in the alternative oxidase: mutagenesis reveals features important for substrate binding and inhibition.Semantic proximity Read ↗

Electron transfer processes in subunit I mutants of cytochrome bo quinol oxidase in Escherichia coli.Semantic proximity Read ↗

Molecular structure of redox metal centers of the cytochrome bo complex from Escherichia coli. Spectroscopic characterizations of the subunit I histidine mutant oxidases.Semantic proximity Read ↗

Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Semantic proximity Read ↗

Mutation analysis of the interaction of B-type cytochrome c oxidase with its natural substrate cytochrome c-551.Semantic proximity Read ↗

Computational characterization of the substrate-binding mode in coproporphyrinogen III oxidase.Semantic proximity Read ↗

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