Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of <i>Chlamydomonas reinhardtii</i> Glutaredoxin 2

Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of <i>Chlamydomonas reinhardtii</i> Glutaredoxin 2

Glutaredoxins (GRXs) are thioredoxin superfamily members exhibiting thiol-disulfide oxidoreductase activity and/or iron-sulfur (Fe-S) cluster binding capacities. These properties are determined by specific structural factors. In this study, we examined the capacity of the class I <i>Chlamydomo...

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Bibliographic Details
Main Authors: Thomas Roret, Bo Zhang, Anna Moseler, Tiphaine Dhalleine, Xing-Huang Gao, Jérémy Couturier, Stéphane D. Lemaire, Claude Didierjean, Michael K. Johnson, Nicolas Rouhier
Format: Article
Language:English
Published: MDPI AG 2021-05-01
Series:Antioxidants
Subjects:
glutaredoxin
glutathione
glutathionylation
iron-sulfur cluster
oxidoreductase
green alga
Online Access:https://www.mdpi.com/2076-3921/10/5/803

Internet

https://www.mdpi.com/2076-3921/10/5/803

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