:Iron–sulfur cluster
{{Short description|Molecular structures and ubiquitous inorganic cofactors found in all domains of life}}
{{Use American English|date=August 2020}}
Image:OBINIX2.png.{{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 [Fe4X4(YCH3)4]2–; 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}}]]
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.Lippard, S. J. and Berg, J. M. (1994). "Principles of Bioinorganic Chemistry". University Science Books: Mill Valley, CA. {{ISBN|0-935702-73-3}}. 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.Weiss, Madeline C., et al. (2016). "The physiology and habitat of the last universal common ancestor." Nature Microbiology 1 (9): 1–8.
In biology
{{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 proteins in nature. They feature either 2Fe–2S or 4Fe–4S centers. They occur in all branches of life.{{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}}
Fe–S clusters can be classified according to their Fe:S stoichiometry [2Fe–2S], [4Fe–3S], [3Fe–4S], and [4Fe–4S].{{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 }} The [4Fe–4S] clusters occur in two forms: normal ferredoxins and high potential iron proteins (HiPIP). Both adopt cuboidal structures, but they utilize different oxidation states. They are found in all forms of life.{{cite journal |last1=Fisher |first1=N |title=Intramolecular electron transfer in [4Fe–4S)] |journal=The EMBO Journal |date=1998 |pages=849–858}}
The relevant redox couple in all Fe–S proteins is Fe(II)/Fe(III).
Many clusters have been synthesized in the laboratory with the formula [Fe4S4(SR)4]2−, which are known for many R substituents, and with many cations. Variations have been prepared including the incomplete cubanes [Fe3S4(SR)3]3−.{{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}}
Synthetic Fe–S clusters
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=Organometallic clusters=
Organometallic Fe–S clusters include the sulfido carbonyls with the formula Fe2S2(CO)6, H2Fe3S(CO)9, and Fe3S2(CO)9. Compounds are also known that incorporate cyclopentadienyl ligands, such as (C5H5)4Fe4S4.{{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}}
=Inorganic materials=
{{Expand section|date=November 2022}}image:KFeS2.svg, which features infinite chains of Fe(III) centers.]]
See also
References
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External links
{{iron compounds}}
{{sulfur compounds}}
{{DEFAULTSORT:Iron-sulfur cluster}}