Mossbauer spectroscopy characteristics

Mosshauer effect The resonance fluorescence by y-radiation of an atomic nucleus, returning from an excited state to the ground state. The resonance energy is characteristic of the chemical environment of the nucleus and Mossbauer spectroscopy may be used to yield information about this chemical environment. Used particularly in the study of Fe. Sn and Sb compounds. 

Mossbauer spectroscopy is an analytical technique that, in archaeological ceramic studies, provides information on the condition and characteristics of the compounds of iron in pottery. Using the technique makes it possible to determine the relative amounts of the different (ferrous and ferric) ions of iron and hence to ascertain the firing conditions of the pottery at the time it was made. The technique involves irradiating a sample of pottery with gamma rays and then assessing the amount of radiation absorbed by the nuclei of the ions of iron within the pottery (Feathers et al. 1998 Bearat and Pradell 1997). 

As described above, the combination of EPR and Mossbauer spectroscopies, when applied to carefully prepared parallel samples, enables a detailed characterization of all the redox states of the clusters present in the enzyme. Once the characteristic spectroscopic properties of each cluster are identified, the determination of their midpoint redox potentials is an easy task. Plots of relative amounts of each species (or some characteristic intensive property) as a function of the potential can be fitted to Nernst equations. In the case of the D. gigas hydrogenase it was determined that those midpoint redox potentials (at pFi 7.0) were —70 mV for the [3Fe-4S] [3Fe-4S]° and —290 and —340mV for each of the [4Fe-4S]> [4Fe-4S] transitions. 

The [Fe =0(TMP+ )]+ complex exhibited a characteristic bright green color and corresponding visible absorbance in its UV-vis spectrum. In its NMR spectrum, the meta-proton doublet of the porphyrin mesityl groups were shifted more than 70 ppm downfield from tetramethylsilane (TMS) because they were in the presence of the cation radical, while the methyl protons shift between 10 and 20ppm downfield. In Mossbauer spectroscopy, the isomer shift, 5 of 0.06 mm/s, and A q value of 1.62mm/s were similar to those for other known Fe(IV) complexes. Electron paramagnetic resonance (EPR), resonance Raman (RR), and EXAFS spectroscopies provided additional indications of an Fe =0 n-cation radical intermediate. For instance,... 

The magnetic properties of iron oxides can be determined using Mossbauer spectroscopy, neutron powder diffraction and magnetometry (see Chap. 7). The characteristic parameters are the magnetic moment, the permeability, the saturation magnetization, the magnetic anisotropy constants and the Bhf (Tab. 6.2). 

In contrast to the above systems, where electronic support interactions were negligible, the work of Bowles and Cranshaw 198) points to the presence of such effects for tin on platinum. Tin was deposited on platinum electrodes at a potential high enough to ensure a fractional tin monolayer. Subsequent 119Sn Mossbauer spectroscopy showed a tin isomer shift characteristic of a Pt-Sn alloy, thereby evidencing the electronic interaction between these two metals. The possible modification by the support of the... 

Cytochromes from bacterial, yeast, and mammalian sources have been investigated by Mossbauer spectroscopy (114—117). Horseheart cytochrome c and the c-type cytochrome from T. utilis show spectra characteristic of low-spin Fe(III) in the oxidized form of the protein and low-spin Fe(II) for the reduced form of the protein. Lang et al. (115) have analyzed the Mossbauer data in terms of a low-spin Hamiltonian in some detail. Cooke and Debrunner (116) present quadrupole data on dehydrated forms of oxidized and reduced cytochrome c the quadrupole splittings for hydrated and dehydrated forms of the reduced protein are quite similar in contrast to a difference of the oxidized form. No spin-state change is reported for either form of cytochrome c. 

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