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Structure of [Fe 4 S 4 (SMe) 4] 2−, a synthetic analogue of 4Fe–4S cofactors. [1]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]
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 ...
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 (S 2-), which requires various families of enzymes. Another broad task is affixing the sulfide to iron, which is achieved on scaffolds, which are nonfunctional.
They participate in electron-transfer sequences. The core structure for the [Fe 4 S 4] cluster is a cube with alternating Fe and S vertices. These clusters exist in two oxidation states with a small structural change. Two families of [Fe 4 S 4] clusters are known: the ferredoxin (Fd) family and the high-potential iron–suflur protein (HiPIP ...
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.
Ferredoxins are small proteins containing iron and sulfur atoms organized as iron–sulfur clusters. These biological "capacitors" can accept or discharge electrons, with the effect of a change in the oxidation state of the iron atoms between +2 and +3. In this way, ferredoxin acts as an electron transfer agent in biological redox reactions.
An Iron–sulfur cluster. Structure of Heme b; in the protein additional ligand(s) would be attached to Fe. Examples of iron-containing proteins in higher organisms include hemoglobin, cytochrome (see high-valent iron), and catalase.
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.