The field of bioinorganic chemistry is at a propitious stage of development. Ever more
complex metallobiomolecules are isolated and purified, physical methodologies and …

Several major advances in our understanding of the structure, function and properties of
biological iron-sulfur clusters have occurred in the past year. These include a new structural …

Lipoyl synthase (LipA) catalyzes the insertion of two sulfur atoms at the unactivated C6 and
C8 positions of a protein-bound octanoyl chain to produce the lipoyl cofactor. To activate its …

Ferredoxins are a group of iron–sulfur proteins for which a wealth of structural and
mutational data have recently become available. Previously unknown structures of …

Cuboidal [Fe4S4] clusters are ubiquitous cofactors in biological redox chemistry. In the
[Fe4S4] 1+ state, pairwise spin coupling gives rise to six arrangements of the Fe valences …

Various types of interactions involving the sulfhydryl group of free cysteine residues have
been analyzed using known protein structures. In a hydrogen bond the-SH group is more …

Substrate reduction by nitrogenase requires electron transfer from a [4Fe-4S] cluster in the
iron (Fe) protein component to an FeMo cofactor in the molybdenum− iron (MoFe) protein …

Publisher Summary This chapter reviews the various applications of electron paramagnetic
resonance (EPR) spectroscopy developed in the field of iron–sulfur research. As the …

Biological nitrogen fixation catalyzed by nitrogenase requires the participation of two
component proteins called the Fe protein and the MoFe protein. Each αβ catalytic unit of the …

The aim of this article is to critically discuss the information available on the influence of the
protein environment on the electron transfer properties of Fe-S proteins. First, the intrinsic …