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.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 72(2021), 6 vom: 17. März, Seite 2014-2044
1. Verfasser: Przybyla-Toscano, Jonathan (VerfasserIn)
Weitere Verfasser: Christ, Loïck, Keech, Olivier, Rouhier, Nicolas
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... Apoproteins Iron-Sulfur Proteins Plant Proteins Sulfur 70FD1KFU70 Iron E1UOL152H7
Beschreibung
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