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Glutaredoxins and iron-sulfur protein biogenesis at the interface of redox biology and iron metabolism

Authors
  • Mühlenhoff, Ulrich1, 2
  • Braymer, Joseph J.1, 2
  • Christ, Stefan1
  • Rietzschel, Nicole1
  • Uzarska, Marta A.1, 3
  • Weiler, Benjamin D.1
  • Lill, Roland1, 2
  • 1 Philipps-Universität Marburg, Robert-Koch-Str. 6 , (Germany)
  • 2 Philipps-Universität Marburg, Hans-Meerwein-Str. , (Germany)
  • 3 University of Gdansk, Abrahama 58 , (Poland)
Type
Published Article
Journal
Biological Chemistry
Publisher
Walter de Gruyter GmbH
Publication Date
Oct 08, 2020
Volume
401
Issue
12
Pages
1407–1428
Identifiers
DOI: 10.1515/hsz-2020-0237
Source
De Gruyter
Keywords
License
Green

Abstract

The physiological roles of the intracellular iron and redox regulatory systems are intimately linked. Iron is an essential trace element for most organisms, yet elevated cellular iron levels are a potent generator and amplifier of reactive oxygen species and redox stress. Proteins binding iron or iron-sulfur (Fe/S) clusters, are particularly sensitive to oxidative damage and require protection from the cellular oxidative stress protection systems. In addition, key components of these systems, most prominently glutathione and monothiol glutaredoxins are involved in the biogenesis of cellular Fe/S proteins. In this review, we address the biochemical role of glutathione and glutaredoxins in cellular Fe/S protein assembly in eukaryotic cells. We also summarize the recent developments in the role of cytosolic glutaredoxins in iron metabolism, in particular the regulation of fungal iron homeostasis. Finally, we discuss recent insights into the interplay of the cellular thiol redox balance and oxygen with that of Fe/S protein biogenesis in eukaryotes.

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