Evidence map›Paper›PMID 25617045›Full record

ArticlePlant physiology2015

Crystal structure and functional characterization of photosystem II-associated carbonic anhydrase CAH3 in Chlamydomonas reinhardtii.

Reyes Benlloch, Dmitriy Shevela, Tobias Hainzl, Christin Grundström, Tatyana Shutova, Johannes Messinger, Göran Samuelsson, A Elisabeth Sauer-Eriksson

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Regulatory logic of theFrontiers in plant science · 2026
    Review
  5. Review
  6. Article
  7. CAH3 fromCells · 2024
    Review
  8. Article
  9. Review
  10. α-CAs from Photosynthetic Organisms.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Review
  13. Water oxidation by photosystem II is the primary source of electrons for sustained HProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. Elucidation and genetic intervention of COJournal of biosciences · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Reyes BenllochDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden.ORCID http://orcid.org/0000-0002-0364-1589
Dmitriy ShevelaDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden.
Tobias HainzlDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden.
Christin GrundströmDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden.
Tatyana ShutovaDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden.
Johannes MessingerDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden.
Göran SamuelssonDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden goran.samuelsson@umu.se elisabeth.sauer-eriksson@umu.se.
A Elisabeth Sauer-ErikssonDepartment of Forest Genetics and Plant Physiology (R.B) and Department of Plant Physiology (T.S., G.S.), Umeå Plant Science Centre, and Department of Chemistry, Chemistry Biology Centre (D.S., T.H., C.G., J.M., A.E.S.-E.), Umeå University, SE-90187 Umea, Sweden goran.samuelsson@umu.se elisabeth.sauer-eriksson@umu.se.
Umeå Plant Science Centre · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In oxygenic photosynthesis, light energy is stored in the form of chemical energy by converting CO2 and water into carbohydrates. The light-driven oxidation of water that provides the electrons and protons for the subsequent CO2 fixation takes place in photosystem II (PSII). Recent studies show that in higher plants, HCO3 (-) increases PSII activity by acting as a mobile acceptor of the protons produced by PSII. In the green alga Chlamydomonas reinhardtii, a luminal carbonic anhydrase, CrCAH3, was suggested to improve proton removal from PSII, possibly by rapid reformation of HCO3 (-) from CO2. In this study, we investigated the interplay between PSII and CrCAH3 by membrane inlet mass spectrometry and x-ray crystallography. Membrane inlet mass spectrometry measurements showed that CrCAH3 was most active at the slightly acidic pH values prevalent in the thylakoid lumen under illumination. Two crystal structures of CrCAH3 in complex with either acetazolamide or phosphate ions were determined at 2.6- and 2.7-Å resolution, respectively. CrCAH3 is a dimer at pH 4.1 that is stabilized by swapping of the N-terminal arms, a feature not previously observed in α-type carbonic anhydrases. The structure contains a disulfide bond, and redox titration of CrCAH3 function with dithiothreitol suggested a possible redox regulation of the enzyme. The stimulating effect of CrCAH3 and CO2/HCO3 (-) on PSII activity was demonstrated by comparing the flash-induced oxygen evolution pattern of wild-type and CrCAH3-less PSII preparations. We showed that CrCAH3 has unique structural features that allow this enzyme to maximize PSII activity at low pH and CO2 concentration.

Indexed as

Carbonic Anhydrase InhibitorsCarbonic AnhydrasesCatalytic DomainChlamydomonas reinhardtiiCrystallography, X-RayCysteineDisulfidesHydrogen-Ion ConcentrationMass SpectrometryMutationOxidation-ReductionOxygenPhotosystem II Protein ComplexProtein Structure, SecondaryCarbonic Anhydrase InhibitorsCarbonic AnhydrasesCysteineDisulfidesOxygenPhotosystem II Protein Complex

Identifiers

PMID25617045
PMCPMC4348767
OpenAlexW2107137307

What OpenQuestion holds

Textmetadata
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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.