Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.

@article{Zhang2013MonothiolGC,
  title={Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.},
  author={Bo Zhang and Sibali Bandyopadhyay and Priyanka Shakamuri and Sunil G. Naik and Boi Hanh Huynh and J{\'e}r{\'e}my Couturier and Nicolas Rouhier and Michael K. Johnson},
  journal={Journal of the American Chemical Society},
  year={2013},
  volume={135 40},
  pages={
          15153-64
        }
}
Saccharomyces cerevisiae mitochondrial glutaredoxin 5 (Grx5) is the archetypical member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site sequence that has been shown to function in biological [Fe2S2](2+) cluster trafficking. In this work, we show that recombinant S. cerevisiae Grx5 purified aerobically, after prolonged exposure of the cell-free extract to air or after anaerobic reconstitution in the presence of glutathione, predominantly contains a… 

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The Arabidopsis Mitochondrial Glutaredoxin GRXS15 Provides [2Fe-2S] Clusters for ISCA-Mediated [4Fe-4S] Cluster Maturation

A detailed characterization of the interactions between Arabidopsis thaliana GRXS15 and ISCA proteins using both in vivo and in vitro approaches is reported, providing new insights into the roles of GRXs15 andISCA1a/2 in effecting [2Fe-2S]2+ to [4Fe-4S] 2+ cluster conversions for the maturation of client [4 Fe-4s] cluster-containing proteins in plants.

Mössbauer spectroscopy of Fe/S proteins.

Mitochondrial [4Fe-4S] protein assembly involves reductive [2Fe-2S] cluster fusion on ISCA1–ISCA2 by electron flow from ferredoxin FDX2

This study reconstituted the maturation of mitochondrial [4Fe-4S] aconitase without artificial reductants and verified the [2Fe-2S]-containing GLRX5 as cluster donor.

A multidisciplinary analysis of the as-isolated Escherichia coli SufBC2D complex reveals the presence of two new iron-sulfur clusters

The first characterization of the native Fe-S cluster of the anaerobically purified SufBC2D scaffold from Escherichia coli is described by XAS, Mössbauer, UV-visible absorption and EPR spectroscopy, supporting the hypothesis that both SufB and SufD are involved in Fe-sulfur cluster ligation.

Real-Time Kinetic Probes Support Monothiol Glutaredoxins As Intermediate Carriers in Fe-S Cluster Biosynthetic Pathways.

Testing whether the monothiol glutaredoxin, Grx4, functions as an obligate [2Fe-2S] carrier protein in the Fe-S cluster distribution network shows the power of chemically conjugated fluorophore reporters for unraveling mechanistic details of biological metal cofactor assembly and distribution networks.

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