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

The involvement of threonine 160 of cytochrome b of Rhodobacter sphaeroides cytochrome bc1 complex in quinone binding and interaction with subunit IV.

The Journal of biological chemistry - 1 Dec 1995

Mather M W, Yu L, Yu C A

Abstract excerpt

The cytochrome b subunit (subunit I) of the ubiquinolcytochrome c reductase (bc1 complex) is thought to participate in the formation of two quinone/quinol reaction centers, an oxidizing center (Qo) and a reducing center, in accordance with the quinone cycle mechanism. Threonine 160 is a highly conserved residue in a segment of subunit I that was shown to bind quinone and is placed near the putative Qo site in...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cytochrome b Group
Share to Molecular Sequence Data

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

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Oligodeoxyribonucleotides

Share to Protein Binding

Share to Threonine

Source

Identifiers

PMID: 7499386
DOI: 10.1074/jbc.270.48.28668

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

The involvement of threonine 160 of cytochrome b of Rhodobacter sphaeroides cytochrome bc1 complex in quinone binding and interaction with subunit IV.PMID 7499386Read ↗

Interactions between the cytochrome b, cytochrome c1, and Fe-S protein subunits at the ubihydroquinone oxidation site of the bc1 complex of Rhodobacter capsulatus.Semantic proximity Read ↗

Tyrosine triad at the interface between the Rieske iron-sulfur protein, cytochrome c1 and cytochrome c2 in the bc1 complex of Rhodobacter capsulatus.Semantic proximity Read ↗

The role of extra fragment at the C-terminal of cytochrome b (Residues 421-445) in the cytochrome bc1 complex from Rhodobacter sphaeroides.Semantic proximity Read ↗

The role of an extra fragment of cytochrome b (residues 309-326) in the cytochrome bc1 complex from Rhodobacter sphaeroides.Semantic proximity Read ↗

Structure-function relationships of the mitochondrial bc1 complex in temperature-sensitive mutants of the cytochrome b gene, impaired in the catalytic center N.Semantic proximity Read ↗

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47.Semantic proximity Read ↗

The disulfide bridge in the head domain of rhodobacter sphaeroides cytochrome c1 is needed to maintain its structural integrity.Semantic proximity Read ↗

Electron transfer from the tetraheme cytochrome to the special pair in the Rhodopseudomonas viridis reaction center: effect of mutations of tyrosine L162.Semantic proximity Read ↗

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

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 ↗

A mutation in cytochrome oxidase subunit 2 restores respiration of the mutant pet ts1402.Semantic proximity Read ↗

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