The Fourier Transform Infrared Spectroscopy facility at the CEA Paris-Saclay is located at the Laboratory of Fundamental Mechanisms in Bioenergetics (UMR 9198). It provides the users with advanced FTIR spectrometry and responds to most of the needs of FTIR analyses.
The FTIR platform includes 4 spectrometers with many accessories: Transmission cell, ATR accessories, thermostatable liquid cells, cryostat for low temperature studies … It enables the analysis of various samples under different physical forms (see below). The laboratory has a specialization in FTIR difference spectroscopy, time-resolved FTIR, low temperature FTIR, and an expertise in the investigation of biochemical reactions and photo-induced reactions.
- Bruker Vertex 80V (under vacuum – to reduce noise and water vapor contamination; cryostat option; detectors: Bolometer, DTGS, MCT; spectral range between 100 and 6000 cm-1). It is interfaced with a pulsed laser Continuum Surelite+OPO (tunable between 440 and 670 nm) to investigate photoinduced processes. The instrument is especially devoted to time-resolved FTIR measurements (rapid-scan, step-scan) with a time resolution down to 100 ns.
- Bruker IFS88 (cryostat and ATR accessories; detectors: MCT, DTGS, Si. Spectral range between 800 and 6000 cm-1). It is interfaced with a pulsed laser Quantel Nd:YAG - 266 / 532 nm - and with Vis lamp and LEDs). The instrument can perform time-resolved rapid scan FTIR (time resolution down to 5 ms). FT-Vis-NIR experiments are also possible.
- Thermo-Nicolet 6700 (ATR accessory; detectors: MCT, InSb, DTGS. Spectral range between 600 and 10000 cm-1). Possibility of investigating electrochemically-induced reactions.
- Bruker Vector 22 (ATR accessory, DTGS detector, Spectral range between 800 and 4000 cm-1).
Samples that can be studied: liquids, powders, solutions, proteins. The large number of detectors makes it possible to investigate also metal-metal and metal-protein (or metal-ligand) bonds.
In particular, reaction mechanisms (in protein and in solutions) can be investigated. Recent measurements include also the study of biochemical reactions in integral bioenergetic membranes and whole microorganisms.
1. Mezzetti A., Leibl W. (2008), Proton and electron transfer in wild-type and mutant reaction centers from Rhodobacter sphaeroides followed by rapid-scan FTIR spectroscopy. Vibr. Spectroscopy 48, 126–134.
2. Mezzetti A., Blanchet L., de Juan A., Leibl W., Ruckebusch C. (2010), Ubiquinol formation in isolated photosynthetic reaction centers monitored by time-resolved differential FTIR in combination with 2D correlation spectroscopy and multivariate curve resolution. Anal. Bioanal. Chemistry, 399, 1999-2014.
3. Avenier F., Herrero C., Leibl W., Desbois A., Guillot R., Mahy JP., Aukauloo A. (2013), Photoassisted Generation of a Dinuclear Iron(III) Peroxo Species Leading to Oxygen Atom Transfer Reaction. Angew. Chemie Int. Ed. 52, 3634-3637.
4. Malferrari M.; Turina P., Francia F., Mezzetti A., Leibl W., Venturoli G. (2015), Dehydration affects the electronic structure of the primary electron donor in bacterial photosynthetic reaction centers: evidence from optical and light-induced difference FTIR spectroscopy. Photochem. Photobiol. Sci. 14, 238-251.
5. Le Caër S., Klein G., Ortiz D., Lima M., Devineau S., Pin S., Brubach J.-B., Roy P., Pommeret S., Leibl W., Righini R., Renault J.-P. (2014), Effect of myoglobin crowding on the dynamics of water: an infrared study. Phys. Chem. Chem. Phys.16: 22841-22852.
6. Valéry C., Deville-Foillard S., Lefebvre C., Taberner N., Legrand P., Meneau F., Meriadec C., Delvaux C., Bizien T., Kasotakis E., Lopez-Iglesias C., Gall A., Bressanelli S., Le Du M. - H., Paternostre M., and Artzner F. (2015) Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins, Nature Communications, 6: 7771.
7. Mezzetti A., Leibl W. (2017), Time-resolved infrared spectroscopy in the study of photosynthetic systems. Photosynth. Res., 131, 121-144