Modulation of cluster incorporation specificity in a de novo iron‐sulfur cluster binding peptide

摘要: iron-sulfur cluster binding proteins perform an astounding variety of functions, and represent one the most abundant classes metalloproteins. Most often, they constitute pairs or chains act as electron transfer modules either within complex redox enzymes small diffusible proteins. We have previously described design a three-helix bundle that can bind two clusters its hydrophobic core. Here, we use single-point mutations to exchange Cys ligands coordinating Leu Ser. show mutants modulate potential stabilize [3Fe-4S] form over [4Fe-4S] form, supporting model in enzymes.