Vibrational spectroscopy background

The book has been written as an introductory text, not as an exhaustive review. It is meant for students at the start of their Ph.D. projects and for anyone else who needs a concise introduction to catalyst characterization. Each chapter describes the physical background and principles of a technique, a few recent applications to illustrate the type of information that can be obtained, and an evaluation of possibilities and limitations. A chapter on case studies highlights a few important catalyst systems and illustrates how powerful combinations of techniques are. The appendix on the surface theory of metals and on chemical bonding at surfaces is included to provide better insight in the results of photoemission, vibrational spectroscopy and thermal desorption. 

In this section we give a simple and qualitative description of chemisorption in terms of molecular orbital theory. It should provide a feeling for why some atoms such as potassium or chlorine acquire positive or negative charge upon adsorption, while other atoms remain more or less neutral. We explain qualitatively why a molecule adsorbs associatively or dissociatively, and we discuss the role of the work function in dissociation. The text is meant to provide some elementary background for the chapters on photoemission, thermal desorption and vibrational spectroscopy. We avoid theoretical formulae and refer for thorough treatments of chemisorption to the literature [2,6-8],... 

This appendix begins with a brief introduction to the physics of metal surfaces. We limit ourselves to those properties of surfaces that play a role in catalysis or in catalyst characterization. The second part includes an introduction to the theory of chemisorption, and is intended to serve as a theoretical background for the chapters on vibrational spectroscopy, photoemission, and the case study on promoter effects. General textbooks on the physics and chemistry of surfaces are listed in [1-8]. 

The secondary structure of proteins may also be assessed using vibrational spectroscopy, fourier transform infrared spectroscopy (FTIR), and Raman spectroscopy both provide information on the secondary structure of proteins. The bulk of the literature using vibrational spectroscopy to study protein structure has involved the use of FTIR. Water produces vibrational bands that interfere with the bands associated with proteins. For this reason, most of the FTIR literature focuses on the use of this technique to assess structure in the solid state or in the presence of non-aqueous environments. Recently, differential FTIR has been used in which a water background is subtracted from the FTIR spectrum. This workaround is limited to solutions containing relatively high protein concentrations. 

Ex situ IR data are collected on dried, diluted powder films in a low vacuum enviromnent or one purged with a dry gas such as N2. Attenuated total reflectance (ATR)-IR spectroscopy provides surface-sensitive IR measurements and can be used for in situ studies of sorption phenomena. Raman spectroscopy is a related vibrational spectroscopy that provides complimentary information to IR. It can also be used to collect vibrational spectra of aqueous samples. Typical data reduction for vibrational spectra involves subtraction of a background spectmm collected under identical conditions from the raw, averaged sample spectrum. Data analysis usually consists of an examination of changes in peak position and shape and peak fitting (Smith, 1996). These and other spectral parameters are tracked as a function of maaoscopic variables such as pH, adsorption density, and ionic strength. 

Theoretical interpretation of molecular vibration spectra is not a simple task. It requires knowledge of symmetry and mathematical group theory to assign all the vibration bands in a spectrum precisely. For applications of vibrational spectroscopy to materials characterization, we can still interpret the vibrational spectra with relatively simple methods without extensive theoretical background knowledge. Here, we introduce some simple methods of vibrational spectrum interpretations. 

A major difference between SFG and other surface vibrational spectroscopy techniques is the presence of a non-resonant background, because, in part, of the metal substrate. This background is usually treated as independent of the frequency and characterized as a constant ( nr). although this treatment is not always possible. In electrochemical systems, /nr is not usually independent of the applied potential. This is because of potential-dependent changes in the electronic state... 

Figure 2 Resonance Raman and SERBS spectra of rhoda-mine 6G with excitation at 514.5 nm, The high fiuorescence background is effectiveiy quenched in the SERRS spectrum due to adsorption of the rhodamine onto the surface of the siiver nanoparticies, (Reproduced with permission from Rodger C and Smith WE (2002) SERS. in Handbook of Vibrational Spectroscopy. New York Wiiey John Wiiey Sons Ltd.)...

The background on Brdneted acid hydroxyls Is discussed on the bases of quantum-chemical cluster calculations, and vibrational spectroscopy. Transition states of carbocalions on zeolites and their reactivity is rationalized. 

The chapter is roughly divided into three sections. In the first (Sections 6.2 and 6.3) we look at the background theory of vibrational spectroscopy, including the selection rules for IR and Raman spectroscopy. We can already use reducible representations and the reduction formula to determine the symmetry labels for the vibrational modes of any molecule. 

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