The competition between chemistry and biology in assembling iron-sulfur derivatives. Molecular structures and electrochemistry. Part IV. {[Fe3S4](SγCys)3} proteins
| Autor: | Piero Zanello, Fabrizia Fabrizi de Biani |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Materials Chemistry2506 Metals and Alloys
0301 basic medicine Stereochemistry chemistry.chemical_element 010402 general chemistry Electrochemistry 01 natural sciences Synthetic [Fe3S4](LS3) complexes Redox Activity Inorganic Chemistry 03 medical and health sciences Electron transfer Rubredoxin Materials Chemistry Redox active Organic chemistry Physical and Theoretical Chemistry Ferredoxin Molecular structures biology Chemistry biology.organism_classification Sulfur 0104 chemical sciences 030104 developmental biology [Fe3S4](SγCys)3 proteins Bacteria |
| Zdroj: | Inorganica Chimica Acta. 455:319-328 |
| ISSN: | 0020-1693 |
| Popis: | Since iron–sulfur clusters are often involved in the electron transfer activity of redox active proteins, following our previous review on {Fe(SγCys)4}proteins (i.e. rubredoxins and related species; Coord. Chem. Rev. 257 (2013) 1777–1805), we focus here on molecular structures and electrochemistry of {[Fe2S2](SγCys)4}proteins (i.e. [2Fe-2S] ferredoxins). The present survey highlights the extended presence of such proteins in natural organisms such as bacteria, plants, fungi, algae, mammals and human parasites. In addition we put in evidence those structurally characterized [2Fe-2S] ferredoxins which have not yet received attention with respect to their redox activity, which is a fundamental aspect of their role in different biological processes. We will conclude with electrochemical and structural aspects of synthetic complexes possessing a [Fe2S2] core linked to four sulfur ligands in order to judge about their biomimetic reliability. |
| Databáze: | OpenAIRE |
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