Sulfur Administration in Fe–S Cluster Homeostasis

Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters. The newly formed cluster can be utilized by mitochondrial Fe–S protein sy...

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Autores principales:	Leszek Rydz, Maria Wróbel, Halina Jurkowska
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Fe–S cluster iron–sulfur protein rhodanese 3-mercaptopyruvate sulfurtransferase oxidative stress Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/9be952f9097042628f4cedda45edb1c2
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id	oai:doaj.org-article:9be952f9097042628f4cedda45edb1c2
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spelling	oai:doaj.org-article:9be952f9097042628f4cedda45edb1c22021-11-25T16:27:33ZSulfur Administration in Fe–S Cluster Homeostasis10.3390/antiox101117382076-3921https://doaj.org/article/9be952f9097042628f4cedda45edb1c22021-10-01T00:00:00Zhttps://www.mdpi.com/2076-3921/10/11/1738https://doaj.org/toc/2076-3921Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters. The newly formed cluster can be utilized by mitochondrial Fe–S protein synthesis or undergo further transformation. Mitochondrial Fe–S cluster biogenesis components are required in the cytosolic iron–sulfur cluster assembly machinery for cytosolic and nuclear cluster supplies. Clusters that are the key components of Fe–S proteins are vulnerable and prone to degradation whenever exposed to oxidative stress. However, once degraded, the Fe–S cluster can be resynthesized or repaired. It has been proposed that sulfurtransferases, rhodanese, and 3-mercaptopyruvate sulfurtransferase, responsible for sulfur transfer from donor to nucleophilic acceptor, are involved in the Fe–S cluster formation, maturation, or reconstitution. In the present paper, we attempt to sum up our knowledge on the involvement of sulfurtransferases not only in sulfur administration but also in the Fe–S cluster formation in mammals and yeasts, and on reconstitution-damaged cluster or restoration of enzyme’s attenuated activity.Leszek RydzMaria WróbelHalina JurkowskaMDPI AGarticleFe–S clusteriron–sulfur proteinrhodanese3-mercaptopyruvate sulfurtransferaseoxidative stressTherapeutics. PharmacologyRM1-950ENAntioxidants, Vol 10, Iss 1738, p 1738 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Fe–S cluster iron–sulfur protein rhodanese 3-mercaptopyruvate sulfurtransferase oxidative stress Therapeutics. Pharmacology RM1-950
spellingShingle	Fe–S cluster iron–sulfur protein rhodanese 3-mercaptopyruvate sulfurtransferase oxidative stress Therapeutics. Pharmacology RM1-950 Leszek Rydz Maria Wróbel Halina Jurkowska Sulfur Administration in Fe–S Cluster Homeostasis
description	Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters. The newly formed cluster can be utilized by mitochondrial Fe–S protein synthesis or undergo further transformation. Mitochondrial Fe–S cluster biogenesis components are required in the cytosolic iron–sulfur cluster assembly machinery for cytosolic and nuclear cluster supplies. Clusters that are the key components of Fe–S proteins are vulnerable and prone to degradation whenever exposed to oxidative stress. However, once degraded, the Fe–S cluster can be resynthesized or repaired. It has been proposed that sulfurtransferases, rhodanese, and 3-mercaptopyruvate sulfurtransferase, responsible for sulfur transfer from donor to nucleophilic acceptor, are involved in the Fe–S cluster formation, maturation, or reconstitution. In the present paper, we attempt to sum up our knowledge on the involvement of sulfurtransferases not only in sulfur administration but also in the Fe–S cluster formation in mammals and yeasts, and on reconstitution-damaged cluster or restoration of enzyme’s attenuated activity.
format	article
author	Leszek Rydz Maria Wróbel Halina Jurkowska
author_facet	Leszek Rydz Maria Wróbel Halina Jurkowska
author_sort	Leszek Rydz
title	Sulfur Administration in Fe–S Cluster Homeostasis
title_short	Sulfur Administration in Fe–S Cluster Homeostasis
title_full	Sulfur Administration in Fe–S Cluster Homeostasis
title_fullStr	Sulfur Administration in Fe–S Cluster Homeostasis
title_full_unstemmed	Sulfur Administration in Fe–S Cluster Homeostasis
title_sort	sulfur administration in fe–s cluster homeostasis
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/9be952f9097042628f4cedda45edb1c2
work_keys_str_mv	AT leszekrydz sulfuradministrationinfesclusterhomeostasis AT mariawrobel sulfuradministrationinfesclusterhomeostasis AT halinajurkowska sulfuradministrationinfesclusterhomeostasis
_version_	1718413153333673984

Sulfur Administration in Fe–S Cluster Homeostasis

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