Developing metalloprotein models for diagnostic and sensing applications (original) (raw)
Abstract
Metalloproteins were selected by nature to mediate a great and extraordinarily heterogeneous class of processes, which are very important in biology. This class of biomolecules consists of protein scaffolds and prosthetic groups, which contain one or more metal ions linked to the polypeptide chain by different types of interaction, either covalent or noncovalent. A mutual relation between metal cofactors and polypeptide chains is estabilished, since (i) metal ions can impart a particular trimensional folding to the protein, thus influencing its function/s, and (ii) the protein matrix is able to modulate the chemical reactivity of metal ions, thus selecting one or few functions among all potential activities. In this contest, an interesting example is the heme-protein family, in which a single prosthetic group, the heme, plays a variety of functions, such as dioxygen storage and transport, electron transfer, hydroxylation and oxidation of organic substrates, disproportionation of hydrogen peroxide, etc.. Through the study of natural proteins and model systems, it is becoming increasingly clear that different proteins are able to optimize the environment surrounding the heme-cofactor for the acquisition of specific functions.
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