@inbook{8968d2e0d7694466999ef36c60e28bbf,
title = "De Novo Design of Iron–Sulfur Proteins",
abstract = "Iron–sulfur proteins are one of the most abundant and functionally pliable redox proteins found in all living organisms. Because of their crucial role in mediating electron transfer processes, minimalist model systems have been developed as a proxy to study natural Fe–S redox proteins and to dissect rules to enable tuning of their redox and electron transfer activities. This goal has been pursued through computational design, mutagenesis in the first and second coordination sphere, metal substitution, cofactor replacement, and the use of unnatural amino acids to stabilize a given cluster. In this chapter, we discuss the most recent design strategies to introduce various Fe–S clusters into natural and artificial protein scaffolds. Practical approaches for the cluster reconstitution, hydrogen production, and electrochemical characterization are mentioned.",
keywords = "Hydrogen production, Iron–sulfur cluster, Metalloproteins, Protein design, Secondary coordination sphere",
author = "Dizicheh, {Zahra B.} and Nicholas Halloran and William Asma and Giovanna Ghirlanda",
year = "2017",
doi = "10.1016/bs.mie.2017.07.014",
language = "English (US)",
volume = "595",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "33--53",
booktitle = "Methods in Enzymology",
address = "United States",
}