Iron–sulfur cluster biosynthesis
From Wikipedia, the free encyclopedia
In biochemistry, the iron–sulfur cluster biosynthesis describes the components and processes involved in the biosynthesis of iron–sulfur proteins. The topic is of interest because these proteins are pervasive. The iron sulfur proteins contain iron–sulfur clusters, some with elaborate structures, that feature iron and sulfide centers. One broad biosynthetic task is producing sulfide (S2-), which requires various families of enzymes. Another broad task is affixing the sulfide to iron, which is achieved on scaffolds, which are nonfunctional. Finally these Fe-S cluster is transferred to a target protein, which then become functional.[1]
Fe-S_biosyn | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Fe-S_biosyn | ||||||||
Pfam | PF01521 | ||||||||
InterPro | IPR000361 | ||||||||
PROSITE | PDOC00887 | ||||||||
SCOP2 | 1nwb / SCOPe / SUPFAM | ||||||||
|
The formation of iron–sulfur clusters are produced by one of four pathways:[2]
- Nitrogen fixation (NIF) system, which is also found in bacteria that are not nitrogen-fixing.[3]
- Iron–sulfur cluster (ISC) system, in bacterial and mitochondria
- Sulfur assimilation (SUF) system, in plastids and some bacteria
In addition to those three systems, the so-called Cystosolic Iron–sulfur Assembly (CIA) is invoked for cytosolic and nuclear Fe–S proteins.