Spectroscopy in Biological and Biomedical Research

Alexander A. Kamnev/ Krisztina KovAcs, Irina V. Alenkina, and Michael I. Oshtrakh  

Up to now, several thousand papers on various biological aspects of Mossbauer spectroscopy applications have been published (for some previous reviews see, for instance. Refs. 2-12), while only about 350—400 articles can be considered as biomedical from the narrower viewpoint (for reviews see Refs. 13-25). These studies were based mainly on Fe-containing subjects however, in a number of cases, Co, Sn, l, Sm, Tb, and Au containing species were used. Various objects, from molecules to tissues and organs, were studied in normal physiological conditions and in the case of pathologies. 

Mossbauer Spectroscopy Applications in Chemistry, Biology, and Nanotechnology, First Edition. Edited b/Virender K. Sharma, Gostar Kiingeihofer, and Tetsuaki Nishida. 

Note that in the case of tryptophan, no Fe(lll) reduction v/as observed within 15 min after mixing the reagents even at pH 2 [46], while the resulting Fe(ll) had earlier been detected in Mossbauer spectra after longer periods [49,50]. In particular, partial reduction of Fe(lll) to Fe(ll) vras detected by Mossbauer spectroscopy in the course of synthesis of ferric complexes with tryptophan and lysine, which included the procedures of precipitation and extraction with nonaqueous solvents [49]. 

Gradual Fe(lll) reduction to Fe(ll) by a series of auxins (indole-3-alkanoic acids with C1-C4 side chains) in weakly acidic aqueous solutions v/as evident from Mossbauer spectroscopic measurements [46,47] performed in rapidly frozen solutions after 15 min and 2 days of reaction at ambient temperature (Fig. 13.1). In that case, rapid freezing allows all the ongoing processes to be ceased at a certain time point, and Mossbauer measurements in the solidified frozen matrix become feasible. 

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MOSSB AUER SPECTROSCOPY IN BIOLOGICAL AND BIOMEDICAL RESEARCH... 

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