Evidence map›Paper›PMID 25342121›Full record

ArticleNature communications2014

The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll proteins.

Md Wahadoszamen, Iris Margalit, Anjue Mane Ara, Rienk van Grondelle, Dror Noy

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 60 citations in OpenAlex.

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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 3 institutions in 2 countries.

Md Wahadoszamen1] Section of Biophysics, Department of Physics and Astronomy, VU University Amsterdam, Amsterdam 1081 HV, The Netherlands [2] Department of Physics, University of Dhaka, Dhaka 1000, Bangladesh.
Iris Margalit1] Plant Sciences Department, Weizmann Institute of Science, Rehovot 7610001, Israel [2] Migal-Galilee Research Institute, Kiryat-Shmona 1101602, Israel.
Anjue Mane Ara1] Section of Biophysics, Department of Physics and Astronomy, VU University Amsterdam, Amsterdam 1081 HV, The Netherlands [2] Department of Physics, Jagannath University, Dhaka 1100, Bangladesh.
Rienk van GrondelleSection of Biophysics, Department of Physics and Astronomy, VU University Amsterdam, Amsterdam 1081 HV, The Netherlands.
Dror NoyMigal-Galilee Research Institute, Kiryat-Shmona 1101602, Israel.
Vrije Universiteit Amsterdam · NLMigal - Galilee Technology Center · ILWeizmann Institute of Science · IL

Funding

European Research Council 267333
6 · The paper itself

Abstract

Understanding how specific protein environments affect the mechanisms of non-radiative energy dissipation within densely assembled chlorophylls in photosynthetic protein complexes is of great interest to the construction of bioinspired solar energy conversion devices. Mixing of charge-transfer and excitonic states in excitonically interacting chlorophylls was implicated in shortening excited states' lifetimes, but its relevance to active control of energy dissipation in natural systems is under considerable debate. Here we show that the degree of fluorescence quenching in two similar pairs of excitonically interacting bacteriochlorophyll derivatives is directly associated with increasing charge-transfer character in the excited state, and that the protein environment may control non-radiative dissipation by affecting the mixing of charge-transfer and excitonic states. The capability of local protein environments to determine the fate of excited states, and thereby to confer different functionalities to excitonically coupled dimers substantiates the dimer as the basic functional element of photosynthetic enzymes.

Indexed as

ElectronsEnergy TransferAbsorption, PhysicochemicalBacterial ProteinsBacteriochlorophyllsMutant ProteinsSpectrometry, FluorescenceZincBacterial ProteinsBacteriochlorophyllsMutant ProteinsZinc

Identifiers

PMID25342121
PMCPMC4255223
OpenAlexW2083019335

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.