Iron-sulfur proteins in plant mitochondria : roles and maturation
© 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.
Veröffentlicht in: | Journal of experimental botany. - 1985. - 72(2021), 6 vom: 17. März, Seite 2014-2044 |
---|---|
1. Verfasser: | |
Weitere Verfasser: | , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2021
|
Zugriff auf das übergeordnete Werk: | Journal of experimental botany |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Review Biogenesis electron transfer enzyme catalysis iron–sulfur proteins mitochondria photosynthetic organisms respiratory complexes mehr... |
Zusammenfassung: | © 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. 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 |
---|---|
Beschreibung: | Date Completed 21.05.2021 Date Revised 31.05.2022 published: Print Citation Status MEDLINE |
ISSN: | 1460-2431 |
DOI: | 10.1093/jxb/eraa578 |