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

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

Biochemistry - 2 Jun 1998

Saribaş A S, Valkova-Valchanova M, Tokito M K, Zhang Z, Berry E A, Daldal F

Abstract excerpt

Ubihydroquinone:cytochrome (cyt) c oxidoreductase (bc1 complex and its plant counterpart b6f complex) is a vital component of energy-transducing systems in most organisms from bacteria to eukaryotes. In the facultative phototrophic (Ps) bacterium Rhodobacter capsulatus, it is constituted by the cyt b, cyt c1, and Rieske Fe-S protein subunits and is essential for Ps growth. Of these subunits, cyt b has two...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Models, Molecular

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

Share to Mutagenesis, Site-Directed

Share to Oxidation-Reduction

Share to Phenotype

Share to Phenylalanine

Share to Suppression, Genetic

Share to Transcription, Genetic

Source

Identifiers

PMID: 9609705
DOI: 10.1021/bi973146s

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

Interactions between the cytochrome b, cytochrome c1, and Fe-S protein subunits at the ubihydroquinone oxidation site of the bc1 complex of Rhodobacter capsulatus.PMID 9609705Read ↗

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 ↗

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 ↗

Controlling the functionality of cytochrome c(1) redox potentials in the Rhodobacter capsulatus bc(1) complex through disulfide anchoring of a loop and a beta-branched amino acid near the heme-ligating methionine.Semantic proximity Read ↗

Consequences of structural modifications in cytochrome b559 on the electron acceptor side of Photosystem II.Semantic proximity Read ↗

Mutual relationships between structural and functional changes in a PsbM-deletion mutant of photosystem II.Semantic proximity Read ↗

Phe265 of the D1 protein is required to stabilize plastoquinone binding in the QB-binding site of photosystem II in Synechocystis sp. PCC 6803.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 ↗

Manipulating the Energetics and Rates of Electron Transfer in Rhodobacter capsulatus Reaction Centers with Asymmetric Pigment Content.Semantic proximity Read ↗

A robust genetic system for producing heterodimeric native and mutant cytochrome bc(1).Semantic proximity Read ↗

A native electrostatic environment near Q(B) is not sufficient to ensure rapid proton delivery in photosynthetic reaction centers.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 ↗

Recent advances in cytochrome bc(1): inter monomer electronic communication?Semantic proximity Read ↗

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