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

Reactions of isocytochrome c2 in the photosynthetic electron transfer chain of Rhodobacter sphaeroides.

Biochemistry - 28 Jan 1997

Witthuhn V C, Gao J, Hong S, Halls S, Rott M A, Wraight C A, Crofts A R, Donohue T J

Abstract excerpt

Rhodobacter sphaeroides strains lacking cytochrome c2 (cyt c2), the normal electron donor to P870+ in light-oxidized reaction center (RC) complexes, are unable to grow photosynthetically. However, spd mutations that suppress the photosynthetic deficiency of cyt c2 mutants elevate levels of the cyt c2 isoform, isocyt c2. We monitored photosynthetic electron transfer in whole cells, in chromatophores, and with...

Read the complete abstract on PubMed

Topics

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

Share to Cytochrome c Group
Share to Electron Transport
Share to Kinetics

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

Share to Mutation

Share to Oxidation-Reduction

Share to Photosynthesis

Share to Photosynthetic Reaction Center Complex Proteins

Share to Rhodobacter sphaeroides

Source

Identifiers

PMID: 9020790
DOI: 10.1021/bi961648k

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

Reactions of isocytochrome c2 in the photosynthetic electron transfer chain of Rhodobacter sphaeroides.PMID 9020790Read ↗

Genetic evidence for the role of isocytochrome c2 in photosynthetic growth of Rhodobacter sphaeroides Spd mutants.Semantic proximity Read ↗

Rhodobacter sphaeroides spd mutations allow cytochrome c2-independent photosynthetic growth.Semantic proximity Read ↗

Regulation of a cytochrome c2 isoform in wild-type and cytochrome c2 mutant strains of Rhodobacter sphaeroides.Semantic proximity Read ↗

Mobile cytochrome c2 and membrane-anchored cytochrome cy are both efficient electron donors to the cbb3- and aa3-type cytochrome c oxidases during respiratory growth of Rhodobacter sphaeroides.Semantic proximity Read ↗

The role of c-type cytochromes in the photosynthetic electron transport pathway of Rhodobacter capsulatus.Semantic proximity Read ↗

Initial characterization of site-directed mutants of tyrosine M210 in the reaction centre of Rhodobacter sphaeroides.Semantic proximity Read ↗

Interaction between cytochrome c2 and reaction centers from purple bacteria.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 ↗

Mutational analyses of the photosynthetic reaction center-bound triheme cytochrome subunit and cytochrome c2 in the purple bacterium Rhodovulum sulfidophilum.Semantic proximity Read ↗

Double mutant studies identify electrostatic interactions that are important for docking cytochrome c2 onto the bacterial reaction center.Semantic proximity Read ↗

Deletion of the cytochrome bc complex from Heliobacterium modesticaldum results in viable but non-phototrophic cells.Semantic proximity Read ↗

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 ↗

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