Evidence map›Paper›PMID 21790179›Full record

ArticleBiochemistry2011

Ligation of D1-His332 and D1-Asp170 to the manganese cluster of photosystem II from Synechocystis assessed by multifrequency pulse EPR spectroscopy.

Troy A Stich, Gregory J Yeagle, Rachel J Service, Richard J Debus, R David Britt

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Assignment of the slowly exchanging substrate water of nature's water-splitting cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Water oxidation in photosystem II.Photosynthesis research · 2019
    Review
  7. Article
  8. An Mn(V)-oxo role in splitting water?Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
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 2 institutions in 1 country.

Troy A StichDepartment of Chemistry, University of California at Davis, Davis, California 95616, United States.
Gregory J Yeagle
Rachel J Service
Richard J Debus
R David Britt
University of California, Davis · USUniversity of California, Riverside · US

Funding

PULSED EPR STUDIES OF BIOLOGICAL MANGANESE CLUSTERSR01GM048242 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI BRITT, R DAVID · 1997 to 2010
$2.5M
EPR STUDIES OF METAL/NUCLEI ACID INTERACTIONSR01GM061211 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI BRITT, R DAVID · 2000 to 2003
$915k
FTIR Studies of Photosynthetic Oxygen EvolutionR01GM076232 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI DEBUS, RICHARD J · 2006 to 2009
$854k
MULTIFREQUENCY EPR/ENDOR SPECTROMETER: TSE, PRIONS10RR021075 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI BRITT, R DAVID · 2005 to 2005
$500k
PULSED EPR STUDIES OF BIOLOGICAL MANGANESE CLUSTERSR29GM048242 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI BRITT, R DAVID · 1992 to 1996
–
NCRR NIH HHS S10 RR021075NCRR NIH HHS S10-RR021075NIGMS NIH HHS GM-048242NIGMS NIH HHS GM-061211NIGMS NIH HHS GM-076232NIGMS NIH HHS R01 GM048242NIGMS NIH HHS R01 GM061211NIGMS NIH HHS R01 GM076232NIGMS NIH HHS R29 GM048242
6 · The paper itself

Abstract

Multifrequency electron spin-echo envelope modulation (ESEEM) spectroscopy is used to ascertain the nature of the bonding interactions of various active site amino acids with the Mn ions that compose the oxygen-evolving cluster (OEC) in photosystem II (PSII) from the cyanobacterium Synechocystis sp. PCC 6803 poised in the S(2) state. Spectra of natural isotopic abundance PSII ((14)N-PSII), uniformly (15)N-labeled PSII ((15)N-PSII), and (15)N-PSII containing (14)N-histidine ((14)N-His/(15)N-PSII) are compared. These complementary data sets allow for a precise determination of the spin Hamiltonian parameters of the postulated histidine nitrogen interaction with the Mn ions of the OEC. These results are compared to those from a similar study on PSII isolated from spinach. Upon mutation of His332 of the D1 polypeptide to a glutamate residue, all isotopically sensitive spectral features vanish. Additional K(a)- and Q-band ESEEM experiments on the D1-D170H site-directed mutant give no indication of new (14)N-based interactions.

Indexed as

Aspartic AcidElectron Spin Resonance SpectroscopyHistidineManganeseModels, MolecularMutagenesis, Site-DirectedMutationOxygenPhotosystem II Protein ComplexProtein ConformationSynechocystisAspartic AcidHistidineManganeseOxygenPhotosystem II Protein Complex

Identifiers

PMID21790179
PMCPMC3418060
OpenAlexW2061961108

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Registered trials

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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.