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

Modification of the pheophytin redox potential in Thermosynechococcus elongatus Photosystem II with PsbA3 as D1.

Biochimica et biophysica acta - 1 Jan 2014

Sugiura Miwa, Azami Chizuko, Koyama Kazumi, Rutherford A William, Rappaport Fabrice, Boussac Alain

Abstract excerpt

In Photosystem II (PSII) of the cyanobacterium Thermosynechococcus elongatus, glutamate 130 in the high-light variant of the D1-subunit (PsbA3) was changed to glutamine in a strain lacking the two other genes for D1, psbA1 and psbA2. The resulting PSII (PsbA3/Glu130Gln) was compared with those from the "native" high-light (PsbA3-PSII) and low-light (PsbA1-PSII) variants, which differ by 21 amino acid including...

Read the complete abstract on PubMed

Topics

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

Share to Cyanobacteria
Share to Electron Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutamic Acid

Share to Glutamine

Share to Mutation

Share to Oxidation-Reduction

Share to Photosystem II Protein Complex

Source

Identifiers

PMID: 24060528
DOI: 10.1016/j.bbabio.2013.09.009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modification of the pheophytin redox potential in Thermosynechococcus elongatus Photosystem II with PsbA3 as D1.PMID 24060528Read ↗

D1 protein variants in Photosystem II from Thermosynechococcus elongatus studied by low temperature optical spectroscopy.Semantic proximity Read ↗

The D1-173 amino acid is a structural determinant of the critical interaction between D1-Tyr161 (TyrZ) and D1-His190 in Photosystem II.Semantic proximity Read ↗

Mutations in the CD-loop region of the D2 protein in Synechocystis sp. PCC 6803 modify charge recombination pathways in photosystem II in vivo.Semantic proximity Read ↗

Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803.Semantic proximity Read ↗

Site-directed mutations at D1-Thr179 of photosystem II in Synechocystis sp. PCC 6803 modify the spectroscopic properties of the accessory chlorophyll in the D1-branch of the reaction center.Semantic proximity Read ↗

Modulating the redox potential of the stable electron acceptor, Q(B), in mutagenized photosystem II reaction centers.Semantic proximity Read ↗

D1' centers are less efficient than normal photosystem II centers.Semantic proximity Read ↗

The PsbP-like protein (sll1418) of Synechocystis sp. PCC 6803 stabilises the donor side of Photosystem II.Semantic proximity Read ↗

Spectroscopic and functional characterization of cyanobacterium Synechocystis PCC 6803 mutants on the cytoplasmic-side of cytochrome b559 in photosystem II.Semantic proximity Read ↗

Engineering of an alternative electron transfer path in photosystem II.Semantic proximity Read ↗

Photosynthetic water oxidation in Synechocystis sp. PCC6803: mutations D1-E189K, R and Q are without influence on electron transfer at the donor side of photosystem II.Semantic proximity Read ↗

Double mutation in photosystem II reaction centers and elevated CO2 grant thermotolerance to mesophilic cyanobacterium.Semantic proximity Read ↗

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