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

Redesign of the Chlamydomonas reinhardtii QB binding niche reveals photosynthesis works in the absence of a driving force for QA-QB electron transfer.

Physiologia plantarum - 1 Jan 2024

Lambreva Maya D, Zobnina Veranika, Antal Taras K, Peeva Violeta N, Giardi Maria Teresa, Bertalan Ivo, Johanningmeier Udo, Virtanen Olli, Ray Mithila, Mulo Paula, Polticelli Fabio, Tyystjärvi Esa, Rea Giuseppina

Abstract excerpt

An in silico redesign of the secondary quinone electron acceptor (QB) binding pocket of the D1 protein of Photosystem II (PSII) suggested that mutations of the F265 residue would affect atrazine binding. Chlamydomonas reinhardtii mutants F265T and F265S were produced to obtain atrazine-hypersensitive strains for biosensor applications, and the mutants were indeed found to be more atrazine-sensitive than the...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Chlamydomonas reinhardtii

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

Share to Electron Transport

Share to Mutation

Share to Photosynthesis

Share to Photosystem II Protein Complex

Share to Quinones

Source

Open in PubMed Open full text

Identifiers

PMID: 39673282
DOI: 10.1111/ppl.70008
PMCID: PMC11645544

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 16 Oct 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

Redesign of the Chlamydomonas reinhardtii QB binding niche reveals photosynthesis works in the absence of a driving force for QA-QB electron transfer.PMID 39673282Read ↗

Structure-based design of novel Chlamydomonas reinhardtii D1-D2 photosynthetic proteins for herbicide monitoring.Semantic proximity Read ↗

Redesigning the QA binding site of Photosystem II allows reduction of exogenous quinones.Semantic proximity Read ↗

Modification of the photosystem II acceptor side function in a D1 mutant (arginine-269-glycine) of Chlamydomonas reinhardti.Semantic proximity Read ↗

Requirement for Asn298 on D1 protein for oxygen evolution: analyses by exhaustive amino acid substitution in the green alga Chlamydomonas reinhardtii.Semantic proximity Read ↗

S1 destabilization and higher sensitivity to light in metribuzin-resistant mutants.Semantic proximity Read ↗

Chlamydomonas reinhardtii genetic variants as probes for fluorescence sensing system in detection of pollutants.Semantic proximity Read ↗

Mutations of photosystem II D1 protein that empower efficient phenotypes of Chlamydomonas reinhardtii under extreme environment in space.Semantic proximity Read ↗

A powerful molecular engineering tool provided efficient Chlamydomonas mutants as bio-sensing elements for herbicides detection.Semantic proximity Read ↗

D1-Tyr246 and D2-Tyr244 in photosystem II: Insights into bicarbonate binding and electron transfer from QA•- to QB.Semantic proximity Read ↗

Improved survival of very high light and oxidative stress is conferred by spontaneous gain-of-function mutations in Chlamydomonas.Semantic proximity Read ↗

Isolation and characterization of mutants corresponding to the MENA, MENB, MENC and MENE enzymatic steps of 5'-monohydroxyphylloquinone biosynthesis in Chlamydomonas reinhardtii.Semantic proximity Read ↗

Loss of inhibition by formate in newly constructed photosystem II D1 mutants, D1-R257E and D1-R257M, of Chlamydomonas reinhardtii.Semantic proximity Read ↗

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