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

On the role of basic residues in adapting the reaction centre-LH1 complex for growth at elevated temperatures in purple bacteria.

Photosynthesis research - 1 Nov 2005

Watson Ashley J, Hughes Arwel V, Fyfe Paul K, Wakeham Marion C, Holden-Dye Kate, Heathcote Peter, Jones Michael R

Abstract excerpt

The purple photosynthetic bacterium Thermochromatium tepidum is a moderate thermophile, with a growth optimum of 48-50 degrees C. The X-ray crystal structure of the reaction centre from this organism has been determined, and compared with that from mesophilic bacteria such as Blastochloris viridis and Rhodobacter sphaeroides (Nogi T et al. (2000) Proc Natl Acad Sci USA 97: 13561-13566). Structural features that...

Read the complete abstract on PubMed

Topics

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

Share to Cell Proliferation
Share to Enzyme Stability

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

Share to Photosynthetic Reaction Center Complex Proteins

Share to Protein Denaturation

Share to Protein Structure, Tertiary

Share to Proteobacteria

Share to Spectroscopy, Near-Infrared

Share to Temperature

Source

Identifiers

PMID: 16172928
DOI: 10.1007/s11120-005-4047-x

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

On the role of basic residues in adapting the reaction centre-LH1 complex for growth at elevated temperatures in purple bacteria.PMID 16172928Read ↗

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

The PufX quinone channel enables the light-harvesting 1 antenna to bind more carotenoids for light collection and photoprotection.Semantic proximity Read ↗

Assembly of light-harvesting bacteriochlorophyll in a model transmembrane helix in its natural environment.Semantic proximity Read ↗

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

Opposing structural changes in two symmetrical polypeptides bring about opposing changes to the thermal stability of a complex integral membrane protein.Semantic proximity Read ↗

A reaction center-light-harvesting 1 complex (RC-LH1) from a Rhodospirillum rubrum mutant with altered esterifying pigments: characterization by optical spectroscopy and cryo-electron microscopy.Semantic proximity Read ↗

Fine tuning of the spectral properties of LH2 by single amino acid residues.Semantic proximity Read ↗

Mutation-Induced Changes in the Protein Environment and Site Energies in the (M)L214G Mutant of the Rhodobacter sphaeroides Bacterial Reaction Center.Semantic proximity Read ↗

Hydrogen bonding in a model bacteriochlorophyll-binding site drives assembly of light harvesting complex.Semantic proximity Read ↗

Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactors.Semantic proximity Read ↗

Functions of conserved tryptophan residues of the core light-harvesting complex of Rhodobacter sphaeroides.Semantic proximity Read ↗

Re-emerging structures: continuing crystallography of the bacterial reaction centre.Semantic proximity Read ↗

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