Evidence map›Paper›PMID 18483777›Full record

ReviewPhotosynthesis research2008

Computational insights into the O2-evolving complex of photosystem II.

Eduardo M Sproviero, James P McEvoy, José A Gascón, Gary W Brudvig, Victor S Batista

Open access · greenAbstract readReview
In one paragraph

Review in Photosynthesis research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Non-heme manganese catalase--the 'other' catalase.Archives of biochemistry and biophysics · 2012
    Review
  6. Article
  7. Article
  8. Article
  9. Proton-coupled electron transfer.Chemical reviews · 2007
    Review
  10. Review
  11. Density functional theory.Photosynthesis research
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Eduardo M SprovieroDepartment of Chemistry, Yale University, New Haven, CT 06520-8107, USA.
James P McEvoy
José A Gascón
Gary W Brudvig
Victor S Batista
Yale University · US

Funding

STRUCTURE/FUNCTION RELATIONS IN MEMBRANE PROTEINSR01GM032715 · NIGMS · YALE UNIVERSITY · PI BRUDVIG, GARY W · 1985 to 2010
$2.7M
ELECTRONIC STRUCTURE OF FE-OXO AND MN-OXO COMPLEXESR01GM043278 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI NOODLEMAN, LOUIS · 1991 to 2010
$2.7M
NIGMS NIH HHS 2R01-GM043278-14NIGMS NIH HHS GM32715NIGMS NIH HHS R01 GM032715
6 · The paper itself

Abstract

Mechanistic investigations of the water-splitting reaction of the oxygen-evolving complex (OEC) of photosystem II (PSII) are fundamentally informed by structural studies. Many physical techniques have provided important insights into the OEC structure and function, including X-ray diffraction (XRD) and extended X-ray absorption fine structure (EXAFS) spectroscopy as well as mass spectrometry (MS), electron paramagnetic resonance (EPR) spectroscopy, and Fourier transform infrared spectroscopy applied in conjunction with mutagenesis studies. However, experimental studies have yet to yield consensus as to the exact configuration of the catalytic metal cluster and its ligation scheme. Computational modeling studies, including density functional (DFT) theory combined with quantum mechanics/molecular mechanics (QM/MM) hybrid methods for explicitly including the influence of the surrounding protein, have proposed chemically satisfactory models of the fully ligated OEC within PSII that are maximally consistent with experimental results. The inorganic core of these models is similar to the crystallographic model upon which they were based, but comprises important modifications due to structural refinement, hydration, and proteinaceous ligation which improve agreement with a wide range of experimental data. The computational models are useful for rationalizing spectroscopic and crystallographic results and for building a complete structure-based mechanism of water-splitting in PSII as described by the intermediate oxidation states of the OEC. This review summarizes these recent advances in QM/MM modeling of PSII within the context of recent experimental studies.

Indexed as

Computer SimulationModels, MolecularOxygenPhotosystem II Protein ComplexProtein BindingWaterOxygenPhotosystem II Protein ComplexWater

Identifiers

PMID18483777
PMCPMC2728911
OpenAlexW2065897065

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.