Evidence map›Paper›PMID 19513810›Full record

ReviewPhotosynthesis research

Fourier transform infrared (FTIR) spectroscopy.

Catherine Berthomieu, Rainer Hienerwadel

Abstract readReview
PubMed Publisher
In one paragraph

Review in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
–field-weighted citation impact
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

119 citing papers in PubMed.

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  18. Optimized histidine-specific isotopic labeling in proteins overproduced in Escherichia coli.Protein science : a publication of the Protein Society · 2026
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  19. Article
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59 more citing papers are in PubMed but not listed here.

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

2 authors.

Catherine BerthomieuCommissariat à l' Energie Atomique, Laboratoire des Interactions Protéine Métal, DSV/Institut de Biologie Environnementale et Biotechnologie, CNRS-CEA-Université Aix-Marseille II, Saint Paul-lez-Durance Cedex, France. catherine.berthomieu@cea.fr
Rainer Hienerwadel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fourier transform infrared (FTIR) spectroscopy probes the vibrational properties of amino acids and cofactors, which are sensitive to minute structural changes. The lack of specificity of this technique, on the one hand, permits us to probe directly the vibrational properties of almost all the cofactors, amino acid side chains, and of water molecules. On the other hand, we can use reaction-induced FTIR difference spectroscopy to select vibrations corresponding to single chemical groups involved in a specific reaction. Various strategies are used to identify the IR signatures of each residue of interest in the resulting reaction-induced FTIR difference spectra. (Specific) Isotope labeling, site-directed mutagenesis, hydrogen/deuterium exchange are often used to identify the chemical groups. Studies on model compounds and the increasing use of theoretical chemistry for normal modes calculations allow us to interpret the IR frequencies in terms of specific structural characteristics of the chemical group or molecule of interest. This review presents basics of FTIR spectroscopy technique and provides specific important structural and functional information obtained from the analysis of the data from the photosystems, using this method.

Indexed as

Hydrogen BondingLigandsMetalsPhotosynthetic Reaction Center Complex ProteinsPlant ProteinsSpectroscopy, Fourier Transform InfraredLigandsMetalsPhotosynthetic Reaction Center Complex ProteinsPlant Proteins

Identifiers

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.