Evidence map›Paper›PMID 26946088›Full record

ArticleBiochimica et biophysica acta2016

Photocurrents from photosystem II in a metal oxide hybrid system: Electron transfer pathways.

Katharina Brinkert, Florian Le Formal, Xiaoe Li, James Durrant, A William Rutherford, Andrea Fantuzzi

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2016. 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
1.9field-weighted citation impact, top 14% 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, 40 citations in OpenAlex.

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  9. Review
  10. LPA2 protein is involved in photosystem II assembly in Chlamydomonas reinhardtii.The Plant journal : for cell and molecular biology · 2021
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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

6 authors at 1 institution in 1 country.

Katharina BrinkertDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Florian Le FormalDepartment of Chemistry, Imperial College London, London SW7 2AZ, UK.
Xiaoe LiDepartment of Chemistry, Imperial College London, London SW7 2AZ, UK.
James DurrantDepartment of Chemistry, Imperial College London, London SW7 2AZ, UK.
A William RutherfordDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK. Electronic address: a.rutherford@imperial.ac.uk.
Andrea FantuzziDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK. Electronic address: a.fantuzzi@imperial.ac.uk.
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K002627/1
6 · The paper itself

Abstract

We have investigated the nature of the photocurrent generated by Photosystem II (PSII), the water oxidizing enzyme, isolated from Thermosynechococcus elongatus, when immobilized on nanostructured titanium dioxide on an indium tin oxide electrode (TiO2/ITO). We investigated the properties of the photocurrent from PSII when immobilized as a monolayer versus multilayers, in the presence and absence of an inhibitor that binds to the site of the exchangeable quinone (QB) and in the presence and absence of exogenous mobile electron carriers (mediators). The findings indicate that electron transfer occurs from the first quinone (QA) directly to the electrode surface but that the electron transfer through the nanostructured metal oxide is the rate-limiting step. Redox mediators enhance the photocurrent by taking electrons from the nanostructured semiconductor surface to the ITO electrode surface not from PSII. This is demonstrated by photocurrent enhancement using a mediator incapable of accepting electrons from PSII. This model for electron transfer also explains anomalies reported in the literature using similar and related systems. The slow rate of the electron transfer step in the TiO2 is due to the energy level of electron injection into the semiconducting material being below the conduction band. This limits the usefulness of the present hybrid electrode. Strategies to overcome this kinetic limitation are discussed.

Indexed as

ElectrodesElectron TransportPhotosystem II Protein ComplexQuinonesTin CompoundsTitaniumindium tin oxidePhotosystem II Protein ComplexQuinonesTin CompoundsTitaniumtitanium dioxidePhotosynthesisPhotosynthetic reaction centreProtein electrode interfaceProtein film photoelectrochemistryQuinoneWater oxidizing enzyme

Identifiers

PMID26946088
PMCPMC4990130
OpenAlexW2290896840

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.