Editing Iron–sulfur cluster

{{Short description|Synthetic analogue of active redox-center in enzymes and Fe–S proteins}}
{{For|biological Fe–S clusters|iron–sulfur protein}}
{{Use American English|date=August 2020}}
[[Image:OBINIX2.png|thumb|right|Structure of [Fe<sub>4</sub>S<sub>4</sub>(SMe)<sub>4</sub>]<sup>2−</sup>, a synthetic analogue of 4Fe–4S [[Cofactor (biochemistry)|cofactors]].<ref>{{cite journal|title=Application of a Universal Force Field to Mixed Fe/Mo−S/Se Cubane and Heterocubane Clusters. 1. Substitution of Sulfur by Selenium in the Series [Fe<sub>4</sub>X<sub>4</sub>(YCH<sub>3</sub>)<sub>4</sub>]<sup>2–</sup>; X = S/Se and Y = S/Se|author=Axel Kern |author2=Christian Näther |author3=Felix Studt |author4=Felix Tuczek|journal=Inorg. Chem.|year=2004|volume=43|issue=16|pages=5003–5010|doi=10.1021/ic030347d|pmid=15285677}}</ref>]]
'''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 protein]]s, which are pervasive.<ref>Lippard, S. J. and Berg, J. M. (1994). "Principles of Bioinorganic Chemistry". University Science Books: Mill Valley, CA.  {{ISBN|0-935702-73-3}}.</ref>  Many Fe–S clusters are known in the area of [[organometallic chemistry]] and as precursors to synthetic analogues of the biological clusters. It is supposed that the [[last universal common ancestor]] had many iron-sulfur clusters.<ref>Weiss, Madeline C., et al. (2016). "The physiology and habitat of the last universal common ancestor." ''Nature Microbiology'' '''1''' (9): 1–8.</ref>

==Organometallic clusters==
Organometallic Fe–S clusters include the sulfido carbonyls with the formula Fe<sub>2</sub>S<sub>2</sub>(CO)<sub>6</sub>, H<sub>2</sub>Fe<sub>3</sub>S(CO)<sub>9</sub>, and Fe<sub>3</sub>S<sub>2</sub>(CO)<sub>9</sub>.  Compounds are also known that incorporate [[cyclopentadienyl]] [[Ligand (biochemistry)|ligands]], such as (C<sub>5</sub>H<sub>5</sub>)<sub>4</sub>Fe<sub>4</sub>S<sub>4</sub>.<ref>{{cite journal|author=Ogino, H. |author2=Inomata, S. |author3=Tobita, H. |title=Abiological Iron-Sulfur Clusters|journal=Chem. Rev.|year=1998|volume=98|issue=6|pages=2093–2122|doi=10.1021/cr940081f|pmid=11848961}}</ref>

[[Image:FeS.png|thumb|center|600px|'''Figure.'''  Illustrative synthetic Fe–S clusters.  From left to right: Fe<sub>3</sub>S<sub>2</sub>(CO)<sub>9</sub>, [Fe<sub>3</sub>S(CO)<sub>9</sub>]<sup>2−</sup>, (C<sub>5</sub>H<sub>5</sub>)<sub>4</sub>Fe<sub>4</sub>S<sub>4</sub>, and [Fe<sub>4</sub>S<sub>4</sub>Cl<sub>4</sub>]<sup>2−</sup>.]]

==Inorganic materials==
{{Expand section|date=November 2022}}[[image:KFeS2.svg|thumb|center|Structure of [[potassium dithioferrate]], which features infinite chains of Fe(III) centers.]]

==Biological Fe–S clusters==
{{main|iron–sulfur protein}}
Iron–sulfur clusters occur in many biological systems, often as components of [[electron transfer]] proteins.  The [[ferredoxin]] proteins are the most common Fe–S clusters in nature.  They feature either 2Fe–2S or 4Fe–4S centers. They occur in all branches of life.<ref name=":0">{{cite journal|author=Johnson, D. C. |author2=Dean, D. R. |author3=Smith, A. D. |author4=Johnson, M. K. |year=2005|title=Structure, function, and formation of biological iron-sulfur clusters|journal=Annual Review of Biochemistry|volume=74|issue=1 |pages=247–281|doi=10.1146/annurev.biochem.74.082803.133518|pmid=15952888}}</ref>

Fe–S clusters can be classified according to their Fe:S stoichiometry [2Fe–2S], [4Fe–3S], [3Fe–4S], and [4Fe–4S].<ref>{{cite journal |last1=Lill |first1=Roland |title=Issue of iron-sulfur protein |journal=Biochimica et Biophysica Acta (BBA) - Molecular Cell Research |volume=1853 |issue=6 |pages=1251–1252 |pmc=5501863 |year=2015 |pmid=25746719 |doi=10.1016/j.bbamcr.2015.03.001 }}</ref> The [4Fe–4S] clusters occur in two forms: normal ferredoxins and [[High potential iron–sulfur protein|high potential iron proteins]] (HiPIP). Both adopt [[Cube|cuboidal]] structures, but they utilize different [[oxidation state]]s.  They are found in all forms of life.<ref name="ReferenceA">{{cite journal |last1=Fisher |first1=N |title=Intramolecular electron transfer in [4Fe–4S)] |journal=The EMBO Journal |date=1998 |pages=849–858}}</ref>

The relevant [[Redox|redox couple]] in all [[Iron–sulfur protein|Fe–S proteins]] is Fe(II)/Fe(III).<ref name="ReferenceA"/>

Many clusters have been synthesized in the laboratory with the formula [Fe<sub>4</sub>S<sub>4</sub>(SR)<sub>4</sub>]<sup>2−</sup>, which are known for many R substituents, and with many cations.  Variations have been prepared including the incomplete [[Cubane-type cluster|cubanes]] [Fe<sub>3</sub>S<sub>4</sub>(SR)<sub>3</sub>]<sup>3−</sup>.<ref>{{cite journal|author1=Rao, P. V. |author2=Holm, R. H. |title=Synthetic Analogues of the Active Sites of Iron-Sulfur Proteins|journal=Chem. Rev.|year=2004|volume=104|issue=2|pages=527─559|doi=10.1021/Cr020615+|pmid=14871134}}</ref>

==See also==
* [[Bioinorganic chemistry]]

==References==
{{reflist|2}}

==External links==
{{iron compounds}}
{{sulfur compounds}}

{{DEFAULTSORT:Iron-sulfur cluster}}
[[Category:Cluster chemistry]]
[[Category:Iron compounds]]
[[Category:Sulfur compounds]]