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Modulation of cluster incorporation specificity in a de novo iron‐sulfur cluster binding peptide
Author(s) -
Sommer Dayn Joseph,
Roy Anindya,
Astashkin Andrei,
Ghirlanda Giovanna
Publication year - 2015
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22635
Subject(s) - chemistry , redox , cluster (spacecraft) , iron–sulfur cluster , metalloprotein , sulfur , electron transfer , enzyme , peptide , biochemistry , stereochemistry , inorganic chemistry , organic chemistry , computer science , programming language
iron‐sulfur cluster binding proteins perform an astounding variety of functions, and represent one of the most abundant classes of metalloproteins. Most often, they constitute pairs or chains and act as electron transfer modules either within complex redox enzymes or within small diffusible proteins. We have previously described the design of a three‐helix bundle that can bind two clusters within its hydrophobic core. Here, we use single‐point mutations to exchange one of the Cys ligands coordinating the cluster to either Leu or Ser. We show that the mutants modulate the redox potential of the clusters and stabilize the [3Fe‐4S] form over the [4Fe‐4S] form, supporting the use of model iron‐sulfur cluster proteins as modules in the design of complex redox enzymes. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 412–418, 2015.