Abstract
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.
Highlights
Involvement in tRNA modification, threonylcarbamoyladenosine tRNA methylthiotransferase (CDKAL1), (E) participation of Fe–S cluster in genome integrity; RTEL, (F) molybdenum cofactor biosynthesis protein 1 (MOCS1A, a member of the S-adenosylmethionine (SAM)-dependent enzyme family) is an enzyme using the Fe–S cluster to generate a 50 -deoxyadenosyl radical, (G) glutaredoxins with Fe–S clusters are involved in Fe–S
Acid-labile sulfur is a part of the iron–sulfur clusters, which are included in different proteins where they can perform various tasks
The mitochondrial process can be divided into two steps: the [2Fe–2S] cluster synthesis and [4Fe–4S] cluster synthesis
Summary
The most important source of this chemical element are the sulfur-containing amino acids L-cysteine and L-methionine [3]. The sulfur pool can be divided into the stable form (for example L-cysteine and L-methionine) and the labile form. Hydrogen sulfide (H2 S) can be released from both labile pools of sulfur under specific conditions [5]. Sulfur, which is a part of metal–sulfur clusters, belongs to the acid-labile group [6]. Non-heme iron ions can be connected with inorganic sulfur in the polymetallic clusters of proteins, which are called the iron–sulfur (Fe–S) proteins [8]. It is possible that one or more coordinating ligands are changed from the original one to (1) other amino acids, (2) a non-sulfur-based ligand, or (3) another thiolate donating ligand [11].
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