Evidence map›Paper›PMID 18281389›Full record

ArticleBiophysical journal2008

Time-resolved FTIR difference spectroscopy in combination with specific isotope labeling for the study of A1, the secondary electron acceptor in photosystem 1.

Gary Hastings, K M Priyangika Bandaranayake, Enrique Carrion

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Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 31 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

3 authors at 1 institution in 1 country.

Gary HastingsDepartment of Physics and Astronomy, Georgia State University, Atlanta, Georgia 30303, USA. ghastings@gsu.edu
K M Priyangika Bandaranayake
Enrique Carrion
Georgia State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A phylloquinone molecule (2-methyl, 3-phytyl, 1, 4-naphthoquinone) occupies the A(1) binding site in photosystem 1 particles from Synechocystis sp. 6803. In menB mutant photosystem 1 particles from the same species, plastoquinone-9 occupies the A(1) binding site. By incubation of menB mutant photosystem 1 particles in the presence of phylloquinone, it was shown in another study that phylloquinone will displace plastoquinone-9 in the A(1) binding site. We describe the reconstitution of unlabeled ((16)O) and (18)O-labeled phylloquinone back into the A(1) binding site in menB photosystem 1 particles. We then produce time-resolved A(1)(-)/A(1) Fourier transform infrared (FTIR) difference spectra for these menB photosystem 1 particles that contain unlabeled and (18)O-labeled phylloquinone. By specifically labeling only the phylloquinone oxygen atoms we are able to identify bands in A(1)(-)/A(1) FTIR difference spectra that are due to the carbonyl (C=O) modes of neutral and reduced phylloquinone. A positive band at 1494 cm(-1) in the A(1)(-)/A(1) FTIR difference spectrum is found to downshift 14 cm(-1) and decreases in intensity on (18)O labeling. Vibrational mode frequency calculations predict that an antisymmetric vibration of both C=O groups of the phylloquinone anion should display exactly this behavior. In addition, phylloquinone that has asymmetrically hydrogen bonded carbonyl groups is also predicted to display this behavior. The positive band at 1494 cm(-1) in the A(1)(-)/A(1) FTIR difference spectrum is therefore due to the antisymmetric vibration of both C=O groups of one electron reduced phylloquinone. Part of a negative band at 1654 cm(-1) in the A(1)(-)/A(1) FTIR difference spectrum downshifts 28 cm(-1) on (18)O labeling. Again, vibrational mode frequency calculations predict this behavior for a C=O mode of neutral phylloquinone. The negative band at 1654 cm(-1) in the A(1)(-)/A(1) FTIR difference spectrum is therefore due to a C=O mode of neutral phylloquinone. More specifically, calculations on a phylloquinone model molecule with the C(4)=O group hydrogen bonded predict that the 1654 cm(-1) band is due to the non hydrogen bonded C(1)=O mode of neutral phylloquinone.

Indexed as

Models, ChemicalComputer SimulationElectron TransportIsotope LabelingLightPhotosystem I Protein ComplexSpectroscopy, Fourier Transform InfraredPhotosystem I Protein Complex

Identifiers

PMID18281389
PMCPMC2480661
OpenAlexW2063009106

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.