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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.
Iron sulfide or Iron sulphide can refer to range of chemical compounds composed of iron and sulfur. Minerals
Iron sulfides occur widely in nature in the form of iron–sulfur proteins. As organic matter decays under low-oxygen (or hypoxic ) conditions such as in swamps or dead zones of lakes and oceans, sulfate-reducing bacteria reduce various sulfates present in the water, producing hydrogen sulfide .
For the ores Cu 2 S and ZnS , balanced equations for the roasting are: 2 Cu 2 S + 3 O 2 → 2 Cu 2 O + 2 SO 2 2 ZnS + 3 O 2 → 2 ZnO + 2 SO 2. The gaseous product of sulfide roasting, sulfur dioxide (SO 2) is often used to produce sulfuric acid. Many sulfide minerals contain other components such as arsenic that are released into the environment.
Iron(II,III) sulfide is a blue-black (sometimes pinkish [citation needed]) chemical compound of iron and sulfur with formula Fe 3 S 4 or FeS·Fe 2 S 3, which is much similar to iron(II,III) oxide. It occurs naturally as the sulfide mineral greigite and is magnetic. It is a bio-mineral produced by and found in magnetotactic bacteria.
The resulting solid decays at a temperature over 20 °C into iron(II) sulfide (FeS) and elemental sulfur: [3] Fe 2 S 3 → 2 FeS + S. With hydrochloric acid it decays according to the following reaction equation: [4] Fe 2 S 3 + 4 HCl → 2 FeCl 2 + 2 H 2 S + S
The specific regulator protein, the IRE-BP, binds to IREs in both 5' and 3' regions, but only to RNA in the apo form, without the Fe-S cluster. Expression of IRE-BP in cultured cells has revealed that the protein functions either as an active aconitase, when cells are iron-replete, or as an active RNA-binding protein, when cells are iron-depleted.
Mössbauer spectroscopy has been widely applied to bioinorganic chemistry, especially for the study of iron-containing proteins and enzymes. Often the technique is used to determine the oxidation state of iron. Examples of prominent iron-containing biomolecules are iron-sulfur proteins, ferritin, and hemes including the cytochromes. These ...