{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T23:27:31Z","timestamp":1785886051055,"version":"3.56.0"},"reference-count":59,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2022,8,6]],"date-time":"2022-08-06T00:00:00Z","timestamp":1659744000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Science Foundation","award":["IOS-2110017"],"award-info":[{"award-number":["IOS-2110017"]}]},{"name":"National Science Foundation","award":["IOS-1353886"],"award-info":[{"award-number":["IOS-1353886"]}]},{"name":"National Science Foundation","award":["MCB-1936590"],"award-info":[{"award-number":["MCB-1936590"]}]},{"name":"National Science Foundation","award":["IOS-1932639"],"award-info":[{"award-number":["IOS-1932639"]}]},{"name":"National Science Foundation","award":["MCB-2224839"],"award-info":[{"award-number":["MCB-2224839"]}]},{"name":"Bond Life Sciences Early Concept Grant","award":["IOS-2110017"],"award-info":[{"award-number":["IOS-2110017"]}]},{"name":"Bond Life Sciences Early Concept Grant","award":["IOS-1353886"],"award-info":[{"award-number":["IOS-1353886"]}]},{"name":"Bond Life Sciences Early Concept Grant","award":["MCB-1936590"],"award-info":[{"award-number":["MCB-1936590"]}]},{"name":"Bond Life Sciences Early Concept Grant","award":["IOS-1932639"],"award-info":[{"award-number":["IOS-1932639"]}]},{"name":"Bond Life Sciences Early Concept Grant","award":["MCB-2224839"],"award-info":[{"award-number":["MCB-2224839"]}]},{"name":"Interdisciplinary Plant Group","award":["IOS-2110017"],"award-info":[{"award-number":["IOS-2110017"]}]},{"name":"Interdisciplinary Plant Group","award":["IOS-1353886"],"award-info":[{"award-number":["IOS-1353886"]}]},{"name":"Interdisciplinary Plant Group","award":["MCB-1936590"],"award-info":[{"award-number":["MCB-1936590"]}]},{"name":"Interdisciplinary Plant Group","award":["IOS-1932639"],"award-info":[{"award-number":["IOS-1932639"]}]},{"name":"Interdisciplinary Plant Group","award":["MCB-2224839"],"award-info":[{"award-number":["MCB-2224839"]}]},{"name":"University of Missouri","award":["IOS-2110017"],"award-info":[{"award-number":["IOS-2110017"]}]},{"name":"University of Missouri","award":["IOS-1353886"],"award-info":[{"award-number":["IOS-1353886"]}]},{"name":"University of Missouri","award":["MCB-1936590"],"award-info":[{"award-number":["MCB-1936590"]}]},{"name":"University of Missouri","award":["IOS-1932639"],"award-info":[{"award-number":["IOS-1932639"]}]},{"name":"University of Missouri","award":["MCB-2224839"],"award-info":[{"award-number":["MCB-2224839"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>NEET proteins are conserved 2Fe-2S proteins that regulate the levels of iron and reactive oxygen species in plant and mammalian cells. Previous studies of seedlings with constitutive expression of AtNEET, or its dominant-negative variant H89C (impaired in 2Fe-2S cluster transfer), revealed that disrupting AtNEET function causes oxidative stress, chloroplast iron overload, activation of iron-deficiency responses, and cell death. Because disrupting AtNEET function is deleterious to plants, we developed an inducible expression system to study AtNEET function in mature plants using a time-course proteomics approach. Here, we report that the suppression of AtNEET cluster transfer function results in drastic changes in the expression of different members of the ferredoxin (Fd), Fd-thioredoxin (TRX) reductase (FTR), and TRX network of Arabidopsis, as well as in cytosolic cluster assembly proteins. In addition, the expression of Yellow Stripe-Like 6 (YSL6), involved in iron export from chloroplasts was elevated. Taken together, our findings reveal new roles for AtNEET in supporting the Fd-TFR-TRX network of plants, iron mobilization from the chloroplast, and cytosolic 2Fe-2S cluster assembly. In addition, we show that the AtNEET function is linked to the expression of glutathione peroxidases (GPXs), which play a key role in the regulation of ferroptosis and redox balance in different organisms.<\/jats:p>","DOI":"10.3390\/antiox11081533","type":"journal-article","created":{"date-parts":[[2022,8,7]],"date-time":"2022-08-07T21:03:50Z","timestamp":1659906230000},"page":"1533","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["The Cluster Transfer Function of AtNEET Supports the Ferredoxin\u2013Thioredoxin Network of Plant Cells"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1256-9371","authenticated-orcid":false,"given":"Sara I.","family":"Zandalinas","sequence":"first","affiliation":[{"name":"Department of Biology, Biochemistry and Environmental Sciences, University Jaume I. Av. de Vicent Sos Baynat, s\/n, 12071 Castell\u00f3 de la Plana, Spain"},{"name":"Division of Plant Sciences and Technology, College of Agriculture Food and Natural Resources and Interdisciplinary Plant Group, Christopher S. Bond Life Sciences Center University of Missouri, 1201 Rollins St, Columbia, MO 65211, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luhua","family":"Song","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of North Texas, Denton, TX 76203, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachel","family":"Nechushtai","sequence":"additional","affiliation":[{"name":"The Alexander Silberman Institute of Life Science, The Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David G.","family":"Mendoza-Cozatl","sequence":"additional","affiliation":[{"name":"Division of Plant Sciences and Technology, College of Agriculture Food and Natural Resources and Interdisciplinary Plant Group, Christopher S. Bond Life Sciences Center University of Missouri, 1201 Rollins St, Columbia, MO 65211, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ron","family":"Mittler","sequence":"additional","affiliation":[{"name":"Division of Plant Sciences and Technology, College of Agriculture Food and Natural Resources and Interdisciplinary Plant Group, Christopher S. Bond Life Sciences Center University of Missouri, 1201 Rollins St, Columbia, MO 65211, USA"},{"name":"Department of Surgery, University of Missouri School of Medicine, Christopher S. Bond Life Sciences Center University of Missouri, 1201 Rollins St, Columbia, MO 65211, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,8,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2139","DOI":"10.1105\/tpc.112.097634","article-title":"Characterization of Arabidopsis NEET Reveals an Ancient Role for NEET Proteins in Iron Metabolism","volume":"24","author":"Nechushtai","year":"2012","journal-title":"Plant Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"118805","DOI":"10.1016\/j.bbamcr.2020.118805","article-title":"The Balancing Act of NEET Proteins: Iron, ROS, Calcium and Metabolism","volume":"1867","author":"Nechushtai","year":"2020","journal-title":"Biochim. Biophys. Acta-Mol. Cell Res."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"42571","DOI":"10.1038\/srep42571","article-title":"Phylogenetic Analysis of Eukaryotic NEET Proteins Uncovers a Link between a Key Gene Duplication Event and the Evolution of Vertebrates","volume":"7","author":"Inupakutika","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"4840","DOI":"10.1038\/s41598-018-23305-6","article-title":"Phylogenetic Analysis of the CDGSH Iron-Sulfur Binding Domain Reveals Its Ancient Origin","volume":"8","author":"Sengupta","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"e49019","DOI":"10.15252\/embr.201949019","article-title":"Chemical Targeting of NEET Proteins Reveals Their Function in Mitochondrial Morphodynamics","volume":"21","author":"Molino","year":"2020","journal-title":"EMBO Rep."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1089\/ars.2018.7502","article-title":"NEET Proteins: A New Link between Iron Metabolism, Reactive Oxygen Species, and Cancer","volume":"30","author":"Mittler","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.plantsci.2013.09.001","article-title":"Purification and Biochemical Characterization of Arabidopsis At-NEET, an Ancient Iron-Sulfur Protein, Reveals a Conserved Cleavage Motif for Subcellular Localization","volume":"213","author":"Su","year":"2013","journal-title":"Plant Sci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"14676","DOI":"10.1073\/pnas.1313198110","article-title":"NAF-1 and MitoNEET Are Central to Human Breast Cancer Proliferation by Maintaining Mitochondrial Homeostasis and Promoting Tumor Growth","volume":"110","author":"Sohn","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1111\/tpj.14581","article-title":"Expression of a Dominant-negative AtNEET-H89C Protein Disrupts Iron\u2013Sulfur Metabolism and Iron Homeostasis in Arabidopsis","volume":"101","author":"Zandalinas","year":"2020","journal-title":"Plant J."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"10890","DOI":"10.1073\/pnas.1612736113","article-title":"Breast Cancer Tumorigenicity Is Dependent on High Expression Levels of NAF-1 and the Lability of Its Fe-S Clusters","volume":"113","author":"Pozniak","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.freeradbiomed.2021.09.013","article-title":"Disrupting CISD2 Function in Cancer Cells Primarily Impacts Mitochondrial Labile Iron Levels and Triggers TXNIP Expression","volume":"176","author":"Karmi","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1046\/j.1365-313X.1997.11030605.x","article-title":"A Glucocorticoid-Mediated Transcriptional Induction System in Transgenic Plants","volume":"11","author":"Aoyama","year":"1997","journal-title":"Plant J."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2125","DOI":"10.1093\/jxb\/eraa425","article-title":"Ferroptosis in Plants: Triggers, Proposed Mechanisms, and the Role of Iron in Modulating Cell Death","volume":"72","author":"Setzes","year":"2021","journal-title":"J. Exp. Bot."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1038\/nprot.2006.97","article-title":"Agrobacterium-Mediated Transformation of Arabidopsis Thaliana Using the Floral Dip Method","volume":"1","author":"Zhang","year":"2006","journal-title":"Nat. Protoc."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2445","DOI":"10.1021\/acs.jproteome.5b01120","article-title":"Quantitative Proteomics of Zea Mays Hybrids Exhibiting Different Levels of Heterosis","volume":"15","author":"Dahal","year":"2016","journal-title":"J. Proteome Res."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"13810","DOI":"10.1073\/pnas.2005077117","article-title":"Systemic Signaling during Abiotic Stress Combination in Plants","volume":"117","author":"Zandalinas","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"5381","DOI":"10.1093\/jxb\/erw299","article-title":"ABA Is Required for the Accumulation of APX1 and MBF1c during a Combination of Water Deficit and Heat Stress","volume":"67","author":"Zandalinas","year":"2016","journal-title":"J. Exp. Bot."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1104\/pp.105.068254","article-title":"The Zinc-Finger Protein Zat12 Plays a Central Role in Reactive Oxygen and Abiotic Stress Signaling in Arabidopsis","volume":"139","author":"Davletova","year":"2005","journal-title":"Plant Physiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1105\/tpc.104.026971","article-title":"Cytosolic Ascorbate Peroxidase 1 Is a Central Component of the Reactive Oxygen Gene Network of Arabidopsis","volume":"17","author":"Davletova","year":"2005","journal-title":"Plant Cell"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/nature08301","article-title":"Function and Biogenesis of Iron\u2013Sulphur Proteins","volume":"460","author":"Lill","year":"2009","journal-title":"Nature"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5569","DOI":"10.1128\/MCB.00642-08","article-title":"Dre2, a Conserved Eukaryotic Fe\/S Cluster Protein, Functions in Cytosolic Fe\/S Protein Biogenesis","volume":"28","author":"Zhang","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.tplants.2010.12.006","article-title":"Ancient and Essential: The Assembly of Iron-Sulfur Clusters in Plants","volume":"16","author":"Balk","year":"2011","journal-title":"Trends Plant Sci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"118863","DOI":"10.1016\/j.bbamcr.2020.118863","article-title":"Mechanistic Concepts of Iron-Sulfur Protein Biogenesis in Biology","volume":"1868","author":"Braymer","year":"2021","journal-title":"Biochim. Biophys. Acta-Mol. Cell Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1105\/tpc.112.107672","article-title":"The Arabidopsis YELLOW STRIPE LIKE4 and 6 Transporters Control Iron Release from the Chloroplast","volume":"25","author":"Divol","year":"2013","journal-title":"Plant Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3389\/fpls.2013.00283","article-title":"Arabidopsis Thaliana Yellow Stripe1-Like4 and Yellow Stripe1-Like6 Localize to Internal Cellular Membranes and Are Involved in Metal Ion Homeostasis","volume":"4","author":"Conte","year":"2013","journal-title":"Front. Plant Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1709","DOI":"10.1104\/pp.110.170233","article-title":"The Chloroplast Permease PIC1 Regulates Plant Growth and Development by Directing Homeostasis and Transport of Iron","volume":"155","author":"Duy","year":"2011","journal-title":"Plant Physiol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1105\/tpc.106.047407","article-title":"PIC1, an Ancient Permease in Arabidopsis Chloroplasts, Mediates Iron Transport","volume":"19","author":"Duy","year":"2007","journal-title":"Plant Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"410","DOI":"10.3389\/fpls.2018.00410","article-title":"FdC1 and Leaf-Type Ferredoxins Channel Electrons from Photosystem i to Different Downstream Electron Acceptors","volume":"9","author":"Guan","year":"2018","journal-title":"Front. Plant Sci."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"6315","DOI":"10.1093\/jxb\/ers283","article-title":"New Insights into the Reduction Systems of Plastidial Thioredoxins Point out the Unique Properties of Thioredoxin z from Arabidopsis","volume":"63","author":"Bohrer","year":"2012","journal-title":"J. Exp. Bot."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"20160474","DOI":"10.1098\/rstb.2016.0474","article-title":"Chloroplast Thioredoxin Systems: Prospects for Improving Photosynthesis","volume":"372","author":"Nikkanen","year":"2017","journal-title":"Philos. Trans. R. Soc. B Biol. Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.gene.2019.04.041","article-title":"Thioredoxins and Thioredoxin Reductase in Chloroplasts: A Review","volume":"706","author":"Kang","year":"2019","journal-title":"Gene"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.freeradbiomed.2019.03.003","article-title":"Evolution of the Thioredoxin System as a Step Enabling Adaptation to Oxidative Stress","volume":"140","author":"Balsera","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1093\/plphys\/kiaa062","article-title":"Redox Regulation of Chloroplast Metabolism","volume":"186","author":"Cejudo","year":"2021","journal-title":"Plant Physiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1093\/plphys\/kiab246","article-title":"A Chloroplast Redox Relay Adapts Plastid Metabolism to Light and Affects Cytosolic Protein Quality Control","volume":"187","author":"Ojeda","year":"2021","journal-title":"Plant Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"20130224","DOI":"10.1098\/rstb.2013.0224","article-title":"Thioredoxin-Dependent Regulatory Networks in Chloroplasts under Fluctuating Light Conditions","volume":"369","author":"Nikkanen","year":"2014","journal-title":"Philos. Trans. R. Soc. B Biol. Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1105\/tpc.112.097139","article-title":"A Chloroplast Light-Regulated Oxidative Sensor for Moderate Light Intensity in Arabidopsis","volume":"24","author":"Dangoor","year":"2012","journal-title":"Plant Cell"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"3866","DOI":"10.1105\/tpc.20.00304","article-title":"M-Type Thioredoxins Regulate the PGR5\/PGRL1-Dependent Pathway by Forming a Disulfide-Linked Complex with PGRL1","volume":"32","author":"Okegawa","year":"2020","journal-title":"Plant Cell"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1093\/jxb\/erw017","article-title":"Type-f Thioredoxins Have a Role in the Short-Term Activation of Carbon Metabolism and Their Loss Affects Growth under Short-Day Conditions in Arabidopsis Thaliana","volume":"67","author":"Naranjo","year":"2016","journal-title":"J. Exp. Bot."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"43821","DOI":"10.1074\/jbc.M404696200","article-title":"A Novel NADPH Thioredoxin Reductase, Localized in the Chloroplast, Which Deficiency Causes Hypersensitivity to Abiotic Stress in Arabidopsis Thaliana","volume":"279","author":"Serrato","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1515\/hsz-2020-0291","article-title":"Shifting Paradigms and Novel Players in Cys-Based Redox Regulation and ROS Signaling in Plants\u2014And Where to Go Next","volume":"402","author":"Meyer","year":"2020","journal-title":"Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1093\/jxb\/erz330","article-title":"On the Move: Redox-Dependent Protein Relocation in Plants","volume":"71","author":"Foyer","year":"2020","journal-title":"J. Exp. Bot."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1720","DOI":"10.1104\/pp.16.00420","article-title":"The ROS Wheel: Refining ROS Transcriptional Footprints","volume":"171","author":"Willems","year":"2016","journal-title":"Plant Physiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.freeradbiomed.2015.01.017","article-title":"Reduction of Mitochondrial Protein MitoNEET [2Fe-2S] Clusters by Human Glutathione Reductase","volume":"81","author":"Landry","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4307","DOI":"10.1074\/jbc.M113.542050","article-title":"Redox Control of Human Mitochondrial Outer Membrane Protein MitoNEET [2Fe-2S] Clusters by Biological Thiols and Hydrogen Peroxide","volume":"289","author":"Landry","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e2121491119","DOI":"10.1073\/pnas.2121491119","article-title":"A VDAC1-Mediated NEET Protein Chain Transfers [2Fe-2S] Clusters between the Mitochondria and the Cytosol and Impacts Mitochondrial Dynamics","volume":"119","author":"Karmi","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Karmi, O., Holt, S.H., Song, L., Tamir, S., Luo, Y., Bai, F., Adenwalla, A., Darash-Yahana, M., Sohn, Y.-S., and Jennings, P.A. (2017). Interactions between MitoNEET and NAF-1 in Cells. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0175796"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Lipper, C.H., Paddock, M.L., Onuchic, J.N., Mittler, R., Nechushtai, R., and Jennings, P.A. (2015). Cancer-Related NEET Proteins Transfer 2Fe-2S Clusters to Anamorsin, a Protein Required for Cytosolic Iron-Sulfur Cluster Biogenesis. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0139699"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1039\/c9mt00286c","article-title":"Defining the Mechanism of the Mitochondrial Atm1p [2Fe-2S] Cluster Exporter","volume":"12","author":"Pearson","year":"2020","journal-title":"Metallomics"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1515\/hsz-2020-0117","article-title":"From the Discovery to Molecular Understanding of Cellular Iron-Sulfur Protein Biogenesis","volume":"401","author":"Lill","year":"2020","journal-title":"Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"118847","DOI":"10.1016\/j.bbamcr.2020.118847","article-title":"Iron-Sulfur Cluster Biogenesis, Trafficking, and Signaling: Roles for CGFS Glutaredoxins and BolA Proteins","volume":"1868","author":"Talib","year":"2021","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Kroh, G.E., and Pilon, M. (2020). Regulation of Iron Homeostasis and Use in Chloroplasts. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21093395"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1093\/pcp\/pcz091","article-title":"Essential and Detrimental\u2014An Update on Intracellular Iron Trafficking and Homeostasis","volume":"60","author":"Vigani","year":"2019","journal-title":"Plant Cell Physiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1111\/pce.12046","article-title":"Plant Type Ferredoxins and Ferredoxin-Dependent Metabolism","volume":"36","author":"Hanke","year":"2013","journal-title":"Plant Cell Environ."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Mittler, R., Zandalinas, S.I., Fichman, Y., and Van Breusegem, F. (2022). Reactive Oxygen Species Signalling in Plant Stress Responses. Nat. Rev. Mol. Cell Biol., in press.","DOI":"10.1038\/s41580-022-00499-2"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.freeradbiomed.2015.02.017","article-title":"Understanding Mammalian Glutathione Peroxidase 7 in the Light of Its Homologs","volume":"83","author":"Maiorino","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1038\/s41580-020-00324-8","article-title":"Ferroptosis: Mechanisms, Biology and Role in Disease","volume":"22","author":"Jiang","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"13047","DOI":"10.1073\/pnas.1109986108","article-title":"Facile Transfer of [2Fe-2S] Clusters from the Diabetes Drug Target MitoNEET to an Apo-Acceptor Protein","volume":"108","author":"Zuris","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.freeradbiomed.2020.05.004","article-title":"Exploring the FMN Binding Site in the Mitochondrial Outer Membrane Protein MitoNEET","volume":"156","author":"Tasnim","year":"2020","journal-title":"Free Radic. Biol. Med."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.freeradbiomed.2018.04.569","article-title":"Electron Transfer Kinetics of the Mitochondrial Outer Membrane Protein MitoNEET","volume":"121","author":"Li","year":"2018","journal-title":"Free Radic. Biol. Med."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/11\/8\/1533\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:05:14Z","timestamp":1760141114000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/11\/8\/1533"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,8,6]]},"references-count":59,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2022,8]]}},"alternative-id":["antiox11081533"],"URL":"https:\/\/doi.org\/10.3390\/antiox11081533","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2022.05.12.491709","asserted-by":"object"}]},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,8,6]]}}}