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- W3113208324 endingPage "2044" @default.
- W3113208324 startingPage "2014" @default.
- W3113208324 abstract "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." @default.
- W3113208324 created "2020-12-21" @default.
- W3113208324 creator A5041934645 @default.
- W3113208324 creator A5045124318 @default.
- W3113208324 creator A5051010750 @default.
- W3113208324 creator A5062432587 @default.
- W3113208324 date "2020-12-10" @default.
- W3113208324 modified "2023-10-16" @default.
- W3113208324 title "Iron–sulfur proteins in plant mitochondria: roles and maturation" @default.
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