Evidence map›Paper›PMID 23786399›Full record

ArticleBiochemistry2013

Functional roles of D2-Lys317 and the interacting chloride ion in the water oxidation reaction of photosystem II as revealed by fourier transform infrared analysis.

Hiroyuki Suzuki, Jianfeng Yu, Takashi Kobayashi, Hanayo Nakanishi, Peter J Nixon, Takumi Noguchi

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Functional Water Networks in Fully Hydrated Photosystem II.Journal of the American Chemical Society · 2022
    Article
  6. Review
  7. Article
  8. Article
  9. High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium,Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. The Photosystem II Assembly Factor Ycf48 from the CyanobacteriumInternational journal of molecular sciences · 2021
    Article
  11. Article
  12. Article
  13. Theoretical study of the EPR spectrum of the SPhotosynthesis research · 2016
    Article
  14. Quantum mechanics/molecular mechanics simulation of the ligand vibrations of the water-oxidizing MnProceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. 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

6 authors at 2 institutions in 2 countries.

Hiroyuki SuzukiDivision of Material Science, Graduate School of Science, Nagoya University , Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
Jianfeng Yu
Takashi Kobayashi
Hanayo Nakanishi
Peter J Nixon
Takumi Noguchi
Nagoya University · JPImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C507037Biotechnology and Biological Sciences Research Council BB/C507037/1
6 · The paper itself

Abstract

Photosynthetic water oxidation in plants and cyanobacteria is catalyzed by a Mn4CaO5 cluster within the photosystem II (PSII) protein complex. Two Cl(-) ions bound near the Mn4CaO5 cluster act as indispensable cofactors, but their functional roles remain to be clarified. We have investigated the role of the Cl(-) ion interacting with D2-K317 (designated Cl-1) by Fourier transform infrared spectroscopy (FTIR) analysis of the D2-K317R mutant of Synechocystis sp. PCC 6803 in combination with Cl(-)/NO3(-) replacement. The D2-K317R mutation perturbed the bands in the regions of the COO(-) stretching and backbone amide vibrations in the FTIR difference spectrum upon the S1 → S2 transition. In addition, this mutation altered the (15)N isotope-edited NO3(-) bands in the spectrum of NO3(-)-treated PSII. These results provide the first experimental evidence that the Cl-1 site is coupled with the Mn4CaO5 cluster and its interaction is affected by the S1 → S2 transition. It was also shown that a negative band at 1748 cm(-1) arising from COOH group(s) was altered to a positive intensity by the D2-K317R mutation as well as by NO3(-) treatment, suggesting that the Cl-1 site affects the pKa of COOH/COO(-) group(s) near the Mn4CaO5 cluster in a common hydrogen bond network. Together with the observation that the efficiency of the S3 → S0 transition significantly decreased in the core complexes of D2-K317R upon moderate dehydration, it is suggested that D2-K317 and Cl-1 are involved in a proton transfer pathway from the Mn4CaO5 cluster to the lumen, which functions in the S3 → S0 transition.

Indexed as

ChloridesCrystallography, X-RayLysineOxidation-ReductionPhotosystem II Protein ComplexSpectroscopy, Fourier Transform InfraredWaterChloridesLysinePhotosystem II Protein ComplexWater

Identifiers

PMID23786399
PMCPMC3777104
OpenAlexW2006375321

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.