Evidence map›Paper›PMID 21714528›Full record

ArticleJournal of the American Chemical Society2011

Proton coupled electron transfer and redox-active tyrosine Z in the photosynthetic oxygen-evolving complex.

James M Keough, David L Jenson, Ashley N Zuniga, Bridgette A Barry

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

12 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Calcium, conformational selection, and redox-active tyrosine YZ in the photosynthetic oxygen-evolving cluster.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. Detection of an intermediary, protonated water cluster in photosynthetic oxygen evolution.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  8. Article
  9. Article
  10. A hydrogen-bonding network plays a catalytic role in photosynthetic oxygen evolution.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  11. Article
  12. Proton-coupled electron transfer.Chemical reviews · 2007
    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

4 authors at 1 institution in 1 country.

James M KeoughSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
David L Jenson
Ashley N Zuniga
Bridgette A Barry
Georgia Institute of Technology · US

Funding

SPECTROSCOPIC STUDIES OF LIGHT-DRIVEN ELECTRON TRANSFERR01GM043273 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BARRY, BRIDGETTE ANNE · 1990 to 2010
$3.0M
NIGMS NIH HHS GM43273NIGMS NIH HHS R01 GM043273
6 · The paper itself

Abstract

Proton coupled electron transfer (PCET) reactions play an essential role in many enzymatic processes. In PCET, redox-active tyrosines may be involved as intermediates when the oxidized phenolic side chain deprotonates. Photosystem II (PSII) is an excellent framework for studying PCET reactions, because it contains two redox-active tyrosines, YD and YZ, with different roles in catalysis. One of the redox-active tyrosines, YZ, is essential for oxygen evolution and is rapidly reduced by the manganese-catalytic site. In this report, we investigate the mechanism of YZ PCET in oxygen-evolving PSII. To isolate YZ(•) reactions, but retain the manganese-calcium cluster, low temperatures were used to block the oxidation of the metal cluster, high microwave powers were used to saturate the YD(•) EPR signal, and YZ(•) decay kinetics were measured with EPR spectroscopy. Analysis of the pH and solvent isotope dependence was performed. The rate of YZ(•) decay exhibited a significant solvent isotope effect, and the rate of recombination and the solvent isotope effect were pH independent from pH 5.0 to 7.5. These results are consistent with a rate-limiting, coupled proton electron transfer (CPET) reaction and are contrasted to results obtained for YD(•) decay kinetics at low pH. This effect may be mediated by an extensive hydrogen-bond network around YZ. These experiments imply that PCET reactions distinguish the two PSII redox-active tyrosines.

Indexed as

Electron Spin Resonance SpectroscopyElectron TransportModels, MolecularOxidation-ReductionPhotosystem II Protein ComplexProtonsSynechococcusTyrosinePhotosystem II Protein ComplexProtonsTyrosine

Identifiers

PMID21714528
PMCPMC3246746
OpenAlexW2018216381

What OpenQuestion holds

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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.