ArticlePhotosynthesis research2014
Molecular interactions of the quinone electron acceptors Q(A), Q(B), and Q(C) in photosystem II as studied by the fragment molecular orbital method.
Article in Photosynthesis research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Pathway(s) and distribution of photosystem II-cyclic electron flow.Biochemical Society transactions · 2026Review
- Review
- Regulation of Microalgal Photosynthetic Electron Transfer.Plants (Basel, Switzerland) · 2024Review
- Regulation of light energy conversion between linear and cyclic electron flow within photosystem II controlled by the plastoquinone/quinol redox poise.Photosynthesis research · 2023Article
- Redox properties and regulatory mechanism of the iron-quinone electron acceptor in photosystem II as revealed by FTIR spectroelectrochemistry.Photosynthesis research · 2022Review
- New Structural and Mechanistic Insights Into Functional Roles of CytochromeFrontiers in plant science · 2022Review
- Untangling the sequence of events during the SProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The study of conformational changes in photosystem II during a charge separation.Journal of molecular modeling · 2020Article
- Recognition of repulsive and attractive regions of selected serotonin receptor binding site using FMO-EDA approach.Journal of molecular modeling · 2019Article
- The plastoquinol-plastoquinone exchange mechanism in photosystem II: insight from molecular dynamics simulations.Photosynthesis research · 2017Article
- Towards an understanding of redox heterogeneity of the photosystem II cytochrome b559 in the native membrane.European biophysics journal : EBJ · 2016Article
- New interpretation of the redox properties of cytochrome b559 in photosystem II.Doklady. Biochemistry and biophysics · 2016Article
- Origin and Evolution of Water Oxidation before the Last Common Ancestor of the Cyanobacteria.Molecular biology and evolution · 2015Article
- Structure/function/dynamics of photosystem II plastoquinone binding sites.Current protein & peptide science · 2014Review
- Evidence for the involvement of loosely bound plastosemiquinones in superoxide anion radical production in photosystem II.PloS one · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular interactions of the three plastoquinone electron acceptors, Q(A), Q(B), and Q(C), in photosystem II (PSII) were studied by fragment molecular orbital (FMO) calculations. Calculations at the FMO-MP2/6-31G level using PSII models deduced from the X-ray structure of the PSII complexes from Thermosynechococcus elongatus provided the binding energies of Q(A), Q(B), and Q(C) as -56.1, -37.9, and -30.1 kcal/mol, respectively. The interaction energies with surrounding fragments showed that the contributions of lipids and cofactors were 0, 24 and 45 % of the total interaction energies for Q(A), Q(B), and Q(C), respectively. These results are consistent with the fact that Q(A) is strongly bound to the PSII protein, whereas Q(B) functions as a substrate and is exchangeable with other quinones and herbicides, and the presence of Q(C) is highly dependent on PSII preparations. It was further shown that the isoprenoid tail is more responsible for the binding than the head group in all the three quinones, and that dispersion forces rather than electrostatic interactions mainly contribute to the stabilization. The relevance of the stability and molecular interactions of Q(A), Q(B), and Q(C) to their physiological functions is discussed.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.