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Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins , such as the ferredoxins , as well as NADH dehydrogenase , hydrogenases , coenzyme Q – cytochrome ...
Iron–sulfur clusters are molecular ensembles of iron and sulfide. They are most often discussed in the context of the biological role for iron–sulfur proteins , which are pervasive. [ 2 ] Many Fe–S clusters are known in the area of organometallic chemistry and as precursors to synthetic analogues of the biological clusters.
Finally these Fe-S cluster is transferred to a target protein, which then become functional. [1] 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
It is an iron-sulfur transferase that contains binding sites for and clusters. ISCU contains a transit peptide, 4 beta strands, 4 alpha helixes, and 4 turns. [8] [9] Alternative splicing results in transcript variants encoding different protein isoforms that localize either to the cytosol or to the mitochondrion.
The protein encoded by this gene is a bifunctional, cytosolic protein that functions as an essential enzyme in the TCA cycle and interacts with mRNA to control the levels of iron inside cells. When cellular iron levels are high, this protein binds to a 4Fe-4S cluster and functions as an aconitase. Aconitases are iron-sulfur proteins that ...
In 1979, Trumpower's team isolated the "oxidation factor" from bovine mitochondria and showed it was a reconstitutively-active form of the Rieske iron-sulfur protein. [2] It is a unique [2Fe-2S] cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues.