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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eraa578
|2 doi
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|a pubmed24n1062.xml
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|a (DE-627)NLM318669439
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|a (NLM)33301571
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Przybyla-Toscano, Jonathan
|e verfasserin
|4 aut
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|a Iron-sulfur proteins in plant mitochondria
|b roles and maturation
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| 264 |
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1 |
|c 2021
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 21.05.2021
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|a Date Revised 31.05.2022
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a Iron-sulfur (Fe-S) clusters are prosthetic groups ensuring electron transfer reactions, activating substrates for catalytic reactions, providing sulfur atoms for the biosynthesis of vitamins or other cofactors, or having protein-stabilizing effects. Hence, metalloproteins containing these cofactors are essential for numerous and diverse metabolic pathways and cellular processes occurring in the cytoplasm. Mitochondria are organelles where the Fe-S cluster demand is high, notably because the activity of the respiratory chain complexes I, II, and III relies on the correct assembly and functioning of Fe-S proteins. Several other proteins or complexes present in the matrix require Fe-S clusters as well, or depend either on Fe-S proteins such as ferredoxins or on cofactors such as lipoic acid or biotin whose synthesis relies on Fe-S proteins. In this review, we have listed and discussed the Fe-S-dependent enzymes or pathways in plant mitochondria including some potentially novel Fe-S proteins identified based on in silico analysis or on recent evidence obtained in non-plant organisms. We also provide information about recent developments concerning the molecular mechanisms involved in Fe-S cluster synthesis and trafficking steps of these cofactors from maturation factors to client apoproteins
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Biogenesis
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|a electron transfer
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|a enzyme catalysis
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|a iron–sulfur proteins
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|a mitochondria
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|a photosynthetic organisms
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|a respiratory complexes
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|a Apoproteins
|2 NLM
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|a Iron-Sulfur Proteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Sulfur
|2 NLM
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|a 70FD1KFU70
|2 NLM
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|a Iron
|2 NLM
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| 650 |
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|a E1UOL152H7
|2 NLM
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| 700 |
1 |
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|a Christ, Loïck
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Keech, Olivier
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Rouhier, Nicolas
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 72(2021), 6 vom: 17. März, Seite 2014-2044
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:72
|g year:2021
|g number:6
|g day:17
|g month:03
|g pages:2014-2044
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|u http://dx.doi.org/10.1093/jxb/eraa578
|3 Volltext
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