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

Re-emerging structures: continuing crystallography of the bacterial reaction centre.

Biochimica et biophysica acta - 15 Aug 2000

Fyfe P K, Jones M R

Abstract excerpt

The reaction centre is nature's solar battery, and is found in a number of variations on a common theme in plants, algae and photosynthetic bacteria. During the last 20 years, a combination of X-ray crystallography, spectroscopy and mutagenesis has provided increasingly detailed insights into the mechanism of light energy transduction in the bacterial reaction centre. This mini-review looks at the application of...

Read the complete abstract on PubMed

Topics

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

Share to Energy Metabolism
Share to Herbicides
Share to Oxidation-Reduction

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

Share to Photosynthesis

Share to Photosynthetic Reaction Center Complex Proteins

Share to Rhodobacter sphaeroides

Share to Ubiquinone

Source

Identifiers

PMID: 11004458
DOI: 10.1016/s0005-2728(00)00179-1

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

Re-emerging structures: continuing crystallography of the bacterial reaction centre.PMID 11004458Read ↗

Protein-lipid interactions in the purple bacterial reaction centre.Semantic proximity Read ↗

The binding of cofactors to photosystem I analyzed by spectroscopic and mutagenic methods.Semantic proximity Read ↗

Expression, purification, crystallization and preliminary X-ray structure analysis of wild-type and L(M196)H-mutant Rhodobacter sphaeroides reaction centres.Semantic proximity Read ↗

A carboxylate switch point controls long-range energy transduction in respiratory Complex I.Semantic proximity Read ↗

A Carboxylate Switch Point Controls Long-Range Energy Transduction in Respiratory Complex ISemantic proximity Read ↗

Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center.Semantic proximity Read ↗

Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria.Semantic proximity Read ↗

X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways.Semantic proximity Read ↗

A comparative look at structural variation among RC-LH1 'Core' complexes present in anoxygenic phototrophic bacteria.Semantic proximity Read ↗

Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules.Semantic proximity Read ↗

Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography.Semantic proximity Read ↗

Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses.Semantic proximity Read ↗

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