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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
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 ...
However a few bacterial ferredoxins (of the 2[4Fe4S] type) have two iron sulfur clusters and can carry out two electron transfer reactions. Depending on the sequence of the protein, the two transfers can have nearly identical reduction potentials or they may be significantly different. [4] [5] Fd 0 ox + e − Fd −
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.
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 ...
Rubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea.Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide.
The FeMo cofactor is a cluster with composition Fe 7 MoS 9 C. This cluster can be viewed as two subunits composed of one Fe 4 S 3 (iron(III) sulfide) cluster and one MoFe 3 S 3 cluster. The two clusters are linked by three sulfide ligands and a bridging carbon atom. The unique iron (Fe) is anchored to the protein by a cysteine.
The most well-studied anaerobic FGE is the bacterial AtsB, an iron-sulfur cluster containing enzyme present in Klebsiella pneumoniae, that is able to convert either cysteine or serine to fGly with a distinctly different mechanism than the aerobic form.