Sample treatment in Mössbauer spectroscopy for protein-related analyses: Nondestructive possibilities to look inside metal-containing biosystems.

In this review, the unique possibilities are considered of the 57 Fe transmission (TMS) and 57 Co emission (EMS) variants of Mössbauer (nuclear γ-resonance) spectroscopy as nondestructive techniques with minimal sample preparation/treatment and a significant analytical potential, with a focus on the analysis of cation-binding sites in metalloproteins. The techniques are shown to provide unique structural and quantitative information on the coordination microenvironment, the chemical state and transformations of the Mössbauer nuclides in sophisticated metal-containing proteins, including those within complicated supramolecular structures, and in microbial cells or tissues. Recent representative examples of analyses of Fe-containing proteins by 57 Fe TMS are briefly discussed, along with the newly emerging data on using 57 Co EMS for probing the structural organisation of 57 Co-doped cation-binding sites in sophisticated biocomplexes including metalloenzymes. Finally, some rare or exotic applications of Mössbauer spectroscopy (including the synchrotron-based methodology) in protein-related studies are outlined.