Search results
Results from the WOW.Com Content Network
The anoxygenic phototrophic iron oxidation was the first anaerobic metabolism to be described within the iron anaerobic oxidation metabolism. The photoferrotrophic bacteria use Fe 2+ as electron donor and the energy from light to assimilate CO 2 into biomass through the Calvin Benson-Bassam cycle (or rTCA cycle) in a neutrophilic environment (pH 5.5-7.2), producing Fe 3+ oxides as a waste ...
Although the biological oxidation of reduced sulfur compounds competes with abiotic chemical reactions (e.g. the iron-mediated oxidation of sulfide to iron sulfide (FeS) or pyrite (FeS 2)), [10] thermodynamic and kinetic considerations suggest that biological oxidation far exceeds the chemical oxidation of sulfide in most environments. [4]
Dibenzyl sulfide is a symmetrical thioether. It contains two C 6 H 5 CH 2 - (benzyl) groups linked by a sulfide bridge. It is a colorless or white solid that is soluble in nonpolar solvents.
The bacterial oxidation of iron sulfide minerals produces iron(III) sulfate and sulfuric acid, and in the case of arsenopyrite, arsenic acid is also produced. The arsenic is removed from the liquor by coprecipitation with the iron and sulfate in a two-stage neutralisation process.
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.
Three sulfide ions bridge two iron ions each, while the fourth sulfide bridges three iron ions. Their formal oxidation states may vary from [Fe 3 S 4] + (all-Fe 3+ form) to [Fe 3 S 4] 2− (all-Fe 2+ form). In a number of iron–sulfur proteins, the [Fe 4 S 4] cluster can be reversibly converted by oxidation and loss of one iron ion to a [Fe 3 ...
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.
Sulfur can be found under several oxidation states in nature, mainly −2, −1, 0, +2 (apparent), +2.5 (apparent), +4, and +6. When two sulfur atoms are present in the same polyatomic oxyanion in an asymmetrical situation, i.e, each bound to different groups as in thiosulfate, the oxidation state calculated from the known oxidation state of accompanying atoms (H = +1, and O = −2) can be an ...