The competition between chemistry and biology in assembling iron–sulfur derivatives. Molecular structures and electrochemistry. Part I. {Fe(SγCys)4} proteins

In the present review, we focus on the relationships between molecular geometry and electron transfer ability of the different classes of proteins bearing the {Fe(SγCys)4} core as active site. We will highlight the role played by the amino acid composition in determining the redox activity of rubredoxins, flavorubredoxins, rubrerythrins, nigerythrins, desulfoferrodoxins and desulforedoxins, including, when available, their mutants. We will conclude with the electrochemical and structural aspects of synthetic FeS4 derivatives able to mimic the above cited proteins (usually the rubredoxins).

Graphical abstractStructural consequences of the Fe(III)/Fe(II) reduction in the Leu41Ala mutant of Clostridium pasteurianum rubredoxin.Figure optionsDownload full-size imageDownload high-quality image (116 K)Download as PowerPoint slideHighlights► We illustrate structure and electrochemistry of proteins containing {Fe(SγCys)4}core(s). ► We present the structural changes consequent to Fe(III)/Fe(II) passage in {Fe(SγCys)4} proteins. ► We examine structure/electrochemistry of synthetic iron-tetrathiolate mimicking {Fe(SγCys)4} proteins.