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

ABSTRACT 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...

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Bibliographic Details
Published in:Biopolymers 2015-07, Vol.104 (4), p.412-418
Main Authors: Sommer, Dayn Joseph, Roy, Anindya, Astashkin, Andrei, Ghirlanda, Giovanna
Format: Article
Language:English
Subjects:
Binding
Biopolymers
Clusters
coiled coil
de novo design
Electron Transport
Enzymes
Iron - chemistry
iron-sulfur clusters
Iron-Sulfur Proteins - chemistry
Ligands
metalloproteins
Modulation
Modules
Peptides - chemistry
Proteins
redox proteins
Sulfur - chemistry
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Summary:ABSTRACT 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.
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.22635