De Novo Design of Iron–Sulfur Proteins

Zahra B. Dizicheh, Nicholas Halloran, William Asma, Giovanna Ghirlanda

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

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.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc
Pages33-53
Number of pages21
DOIs
Publication statusPublished - Jan 1 2017

Publication series

NameMethods in Enzymology
Volume595
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

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Keywords

  • Hydrogen production
  • Iron–sulfur cluster
  • Metalloproteins
  • Protein design
  • Secondary coordination sphere

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Dizicheh, Z. B., Halloran, N., Asma, W., & Ghirlanda, G. (2017). De Novo Design of Iron–Sulfur Proteins. In Methods in Enzymology (pp. 33-53). (Methods in Enzymology; Vol. 595). Academic Press Inc. https://doi.org/10.1016/bs.mie.2017.07.014