ArticleScientific reports2021
Modulation of MagR magnetic properties via iron-sulfur cluster binding.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
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- Hypomagnetic Fields Influence the Developmental Duration, Fecundity and Temperature Stress Resistance ofBiology · 2026Article
- Quantum Effects in Evolution: Terrestrial Fine-Tuning of Magnetic Parameters.Computational and structural biotechnology journal · 2026Article
- Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins.Nature communications · 2025Article
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- The physiology of plants in the context of space exploration.Communications biology · 2024Review
- Filamentous morphology engineering of bacteria by iron metabolism modulation through MagR expression.Synthetic and systems biotechnology · 2024Article
- On the evolutionary trail of MagRs.Zoological research · 2024Article
- Mitochondrial targeting sequence of magnetoreceptor MagR: More than just targeting.Zoological research · 2024Article
- Neuroprotective effects of repetitive transcranial magnetic stimulation on Alzheimer's disease: Undetermined therapeutic protocols and mechanisms.Neuroprotection (Chichester, England) · 2024Review
- Unexpected divergence in magnetoreceptor MagR from robin and pigeon linked to two sequence variations.Zoological research · 2024Article
- Probing Transcriptional Crosstalk betweenInternational journal of molecular sciences · 2023Article
- Towards magnetism in pigeon MagR: Iron- and iron-sulfur binding work indispensably and synergistically.Zoological research · 2023Article
- A redox-sensitive iron-sulfur cluster in murine FAM72A controls its ability to degrade the nuclear form of uracil-DNA glycosylase.DNA repair · 2022Article
- Searching for unity in diversity of animal magnetoreception: From biology to quantum mechanics and back.Innovation (Cambridge (Mass.)) · 2022Review
- The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Iron-sulfur clusters are essential cofactors found in all kingdoms of life and play essential roles in fundamental processes, including but not limited to respiration, photosynthesis, and nitrogen fixation. The chemistry of iron-sulfur clusters makes them ideal for sensing various redox environmental signals, while the physics of iron-sulfur clusters and its host proteins have been long overlooked. One such protein, MagR, has been proposed as a putative animal magnetoreceptor. It forms a rod-like complex with cryptochromes (Cry) and possesses intrinsic magnetic moment. However, the magnetism modulation of MagR remains unknown. Here in this study, iron-sulfur cluster binding in MagR has been characterized. Three conserved cysteines of MagR play different roles in iron-sulfur cluster binding. Two forms of iron-sulfur clusters binding have been identified in pigeon MagR and showed different magnetic properties: [3Fe-4S]-MagR appears to be superparamagnetic and has saturation magnetization at 5 K but [2Fe-2S]-MagR is paramagnetic. While at 300 K, [2Fe-2S]-MagR is diamagnetic but [3Fe-4S]-MagR is paramagnetic. Together, the different types of iron-sulfur cluster binding in MagR attribute distinguished magnetic properties, which may provide a fascinating mechanism for animals to modulate the sensitivity in magnetic sensing.
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Registered trials
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.