How does iron–sulfur cluster coordination regulate the activity of human glutaredoxin 2?

C Berndt, C Hudemann, EM Hanschmann… - Antioxidants & redox …, 2007 - liebertpub.com
Human mitochondrial glutaredoxin (Grx2) was described as the first iron–sulfur protein from
the thioredoxin superfamily of proteins. The [2Fe–2S] cluster was proposed to serve as …

[HTML][HTML] Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis

A Kumánovics, OS Chen, L Li, D Bagley… - Journal of Biological …, 2008 - ASBMB
The nature of the connection between mitochondrial Fe-S cluster synthesis and the iron-
sensitive transcription factor Aft1 in regulating the expression of the iron transport system in …

Plant glutaredoxins: still mysterious reducing systems

N Rouhier, E Gelhaye, JP Jacquot - Cellular and Molecular Life Sciences …, 2004 - Springer
Glutaredoxins are ubiquitous oxidoreductases which are similar to thioredoxins and possess
a typical glutathione-reducible CxxC or CxxS active site. We present here the current …

[HTML][HTML] Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae

L Ojeda, G Keller, U Muhlenhoff, JC Rutherford… - Journal of Biological …, 2006 - ASBMB
The transcription factors Aft1 and Aft2 from Saccharomyces cerevisiae regulate the
expression of genes involved in iron homeostasis. These factors induce the expression of …

The E. coli Monothiol Glutaredoxin GrxD Forms Homodimeric and Heterodimeric FeS Cluster Containing Complexes

N Yeung, B Gold, NL Liu, R Prathapam, HJ Sterling… - Biochemistry, 2011 - ACS Publications
Monothiol glutaredoxins (mono-Grx) represent a highly evolutionarily conserved class of
proteins present in organisms ranging from prokaryotes to humans. Mono-Grxs have been …

A Novel Group of Glutaredoxins in the cis-Golgi Critical for Oxidative Stress Resistance

N Mesecke, A Spang, M Deponte… - Molecular biology of the …, 2008 - Am Soc Cell Biol
Glutaredoxins represent a ubiquitous family of proteins that catalyze the reduction of
disulfide bonds in their substrate proteins by use of reduced glutathione. In an attempt to …

Thioredoxins and glutaredoxins: unifying elements in redox biology

Y Meyer, BB Buchanan, F Vignols… - Annual review of …, 2009 - annualreviews.org
Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of
thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory …

[HTML][HTML] Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins

L Liedgens, J Zimmermann, L Wäschenbach… - Nature …, 2020 - nature.com
Class I glutaredoxins are enzymatically active, glutathione-dependent oxidoreductases,
whilst class II glutaredoxins are typically enzymatically inactive, Fe-S cluster-binding …

Structural Insight into Poplar Glutaredoxin C1 with a Bridging Iron−Sulfur Cluster at the Active Site,

Y Feng, N Zhong, N Rouhier, T Hase, M Kusunoki… - Biochemistry, 2006 - ACS Publications
Glutaredoxins are glutathione-dependent enzymes that function to reduce disulfide bonds in
vivo. Interestingly, a recent discovery indicates that some glutaredoxins can also exist in …

Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae

MT Rodríguez-Manzaneque, J Ros… - … and cellular biology, 1999 - Am Soc Microbiol
Glutaredoxins are members of a superfamily of thiol disulfide oxidoreductases involved in
maintaining the redox state of target proteins. In Saccharomyces cerevisiae, two …