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

Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells.

Photochemistry and photobiology - 1 Feb 2004

Lupínková Lenka, Komenda Josef

Abstract excerpt

Action of reactive oxygen species (ROS) on the isolated D1 protein, a key component of Photosystem II (PSII) complex, was studied and compared with the effect of high irradiance on this protein in mildly solubilized photosynthetic membranes and cells of the cyanobacterium Synechocystis. Whereas s...

Read the complete abstract on PubMed

Topics

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

Share to Cyanobacteria
Share to Heme
Share to Hydrogen Peroxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Photosystem II Protein Complex

Share to Superoxides

Share to Thylakoids

Source

Identifiers

PMID: 15068028
DOI: 10.1562/0031-8655(2004)079<0152:omotpi>2.0.co;2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15068028-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells.PMID 15068028Read ↗

Irreversible photoinhibition of photosystem II is caused by exposure of Synechocystis cells to strong light for a prolonged period.Semantic proximity Read ↗

The exposed N-terminal tail of the D1 subunit is required for rapid D1 degradation during photosystem II repair in Synechocystis sp PCC 6803.Semantic proximity Read ↗

Photosystem II characteristics of a constructed Synechocystis 6803 mutant lacking synthesis of the D1 polypeptide.Semantic proximity Read ↗

Role of the PSII-H subunit in photoprotection: novel aspects of D1 turnover in Synechocystis 6803.Semantic proximity Read ↗

Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II.Semantic proximity Read ↗

Arabidopsis thaliana plants lacking the PSI-D subunit of photosystem I suffer severe photoinhibition, have unstable photosystem I complexes, and altered redox homeostasis in the chloroplast stroma.Semantic proximity Read ↗

A sequential two-step proteolytic process in the carboxyl-terminal truncation of precursor D1 protein in Synechocystis sp. PCC6803.Semantic proximity Read ↗

Degradation of the Photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocytis PCC 6803 varying with respect to the type and level of psbA transcript.Semantic proximity Read ↗

Dissecting a cyanobacterial proteolytic system: efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants.Semantic proximity Read ↗

Synechocystis 6803 mutants expressing distinct forms of the Photosystem II D1 protein from Synechococcus 7942: relationship between the psbA coding region and sensitivity to visible and UV-B radiation.Semantic proximity Read ↗

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

Low unsaturation level of thylakoid membrane lipids limits turnover of the D1 protein of photosystem II at high irradiance.Semantic proximity Read ↗

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