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

Modeling the quinone-B binding site of the photosystem-II reaction center using notions of complementarity and contact-surface between atoms.

Proteins - 1 Mar 1995

Sobolev V, Edelman M

Abstract excerpt

Functional identity and significant similarities in cofactors and sequence exist between the L and M reaction center proteins of the photosynthetic bacteria and the D1 and D2 photosystem-II reaction center proteins of cyanobacteria, algae, and plants. A model of the quinone (QB) binding site of the D1 protein is presented based upon the resolved structure of the QB binding pocket of the L subunit, and introducing...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to Binding Sites
Share to Herbicides

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

Share to Mathematics

Share to Models, Molecular

Share to Phenotype

Share to Photosynthetic Reaction Center Complex Proteins

Share to Protein Conformation

Source

Identifiers

PMID: 7784425
DOI: 10.1002/prot.340210304

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

Modeling the quinone-B binding site of the photosystem-II reaction center using notions of complementarity and contact-surface between atoms.PMID 7784425Read ↗

Many combinations of amino acid sequences in a conserved region of the D1 protein satisfy photosystem II function.Semantic proximity Read ↗

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

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

Phe265 of the D1 protein is required to stabilize plastoquinone binding in the QB-binding site of photosystem II in Synechocystis sp. PCC 6803.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 ↗

Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.Semantic proximity Read ↗

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

Arg24 and 26 of the D2 protein are important for photosystem II assembly and plastoquinol exchange in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

Structure of donor side components in photosystem II predicted by computer modelling.Semantic proximity Read ↗

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

Engagement of specific sites in the plastoquinone niche regulates degradation of the D1 protein in photosystem II.Semantic proximity Read ↗

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

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