Alternative FeS cluster ligands: tuning redox potentials and chemistry.
A subset of biological Fe-S clusters contain protein-based ligands other than cysteine (Cys). The most common alternative ligand is histidine, while aspartate, arginine, and threonine ligation have also been identified. With the exception of the 2-Cys, 2-His ligated Rieske clusters, the functions of these uniquely ligated clusters are, in general, poorly understood. Recent functional studies of a set of 3-Cys, 1-His ligated [2Fe-2S] clusters have begun to highlight the importance of non-Cys ligation in controlling both the redox and chemical properties of these clusters as well as their physiological stability. Here, a survey of non-Cys ligation motifs is examined along with the possible biological roles of these clusters.
Program in Molecular and Cellular Biology and Biochemistry, Boston University, Boston, MA 02215, United States.
Daniel W
DW
Bak
Program in Molecular and Cellular Biology and Biochemistry, Boston University, Boston, MA 02215, United States; Department of Chemistry, Boston University, Boston, MA 02215, United States. Electronic address: elliott@bu.edu.
Sean J
SJ
Elliott
D006801:Humans; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D010084:Oxidation-Reduction; D020836:Protein Structure, Quaternary
D007506:Iron-Sulfur Proteins; D008024:Ligands; D007501:Iron