ArticleProceedings of the National Academy of Sciences of the United States of America2014
[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 135 citations in OpenAlex.
- Review
- Shedding Light on the Electron Delocalization Pathway at the [FeInorganic chemistry · 2025Article
- Isa2p is essential inJournal of biosciences · 2025Article
- Defects in the Maturation of Mitochondrial Iron-Sulfur Proteins: Biophysical Investigation of the MMDS3 Causing Gly104Cys Variant of IBA57.International journal of molecular sciences · 2024Article
- Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction.Nature communications · 2024Article
- Multiple Rounds ofACS synthetic biology · 2023Article
- Structural Plasticity of NFU1 Upon Interaction with Binding Partners: Insights into the Mitochondrial [4Fe-4S] Cluster Pathway.Journal of molecular biology · 2023Article
- Understanding the Molecular Basis of the Multiple Mitochondrial Dysfunctions Syndrome 2: The Disease-Causing His96Arg Mutation of BOLA3.International journal of molecular sciences · 2023Article
- The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes.Antioxidants (Basel, Switzerland) · 2023Review
- New Perspectives on BolA: A Still Mysterious Protein Connecting Morphogenesis, Biofilm Production, Virulence, Iron Metabolism, and Stress Survival.Microorganisms · 2023Review
- Glutathione-Related Enzymes and Proteins: A Review.Molecules (Basel, Switzerland) · 2023Review
- The Intriguing mitoNEET: Functional and Spectroscopic Properties of a Unique [2Fe-2S] Cluster Coordination Geometry.Molecules (Basel, Switzerland) · 2022Review
- In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1.ACS bio & med chem Au · 2022Article
- Molecular Basis of Rare Diseases Associated to the Maturation of Mitochondrial [4Fe-4S]-Containing Proteins.Biomolecules · 2022Review
- Identification ofFrontiers in immunology · 2022Article
- Modulation of MagR magnetic properties via iron-sulfur cluster binding.Scientific reports · 2021Article
- Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021Review
- Environment and coordination of FeMo-co in the nitrogenase metallochaperone NafY.RSC chemical biology · 2021Article
- The function of glutaredoxin GRXS15 is required for lipoyl-dependent dehydrogenases in mitochondria.Plant physiology · 2021Article
- Glutaredoxin: Discovery, redox defense and much more.Redox biology · 2021Review
3 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monothiol glutaredoxins play a crucial role in iron-sulfur (Fe/S) protein biogenesis. Essentially all of them can coordinate a [2Fe-2S] cluster and have been proposed to mediate the transfer of [2Fe-2S] clusters from scaffold proteins to target apo proteins, possibly by acting as cluster transfer proteins. The molecular basis of [2Fe-2S] cluster transfer from monothiol glutaredoxins to target proteins is a fundamental, but still unresolved, aspect to be defined in Fe/S protein biogenesis. In mitochondria monothiol glutaredoxin 5 (GRX5) is involved in the maturation of all cellular Fe/S proteins and participates in cellular iron regulation. Here we show that the structural plasticity of the dimeric state of the [2Fe-2S] bound form of human GRX5 (holo hGRX5) is the crucial factor that allows an efficient cluster transfer to the partner proteins human ISCA1 and ISCA2 by a specific protein-protein recognition mechanism. Holo hGRX5 works as a metallochaperone preventing the [2Fe-2S] cluster to be released in solution in the presence of physiological concentrations of glutathione and forming a transient, cluster-mediated protein-protein intermediate with two physiological protein partners receiving the [2Fe-2S] cluster. The cluster transfer mechanism defined here may extend to other mitochondrial [2Fe-2S] target proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.