Sulfur organic, metabolism

A substantial fraction of the named enzymes are oxido-reductases, responsible for shuttling electrons along metabolic pathways that reduce carbon dioxide to sugar (in the case of plants), or reduce oxygen to water (in the case of mammals). The oxido-reductases that drive these processes involve a small set of redox active cofactors , that is, small chemical groups that gain or lose electrons. These cofactors include iron porjDhyrins, iron-sulfur clusters and copper complexes as well as organic species that are ET active. 

In summary, the capacity to synthesize both hemoproteins and iron sulfur proteins appears to be a ubiquitous attribute in organisms attacking reduced inorganic substrates. If the reactions by which these cells obtain energy represent relics of ancient forms of metabolism, it can only be concluded that heme formation and iron-sulfur coordination must have been invented at a very early stage in evolution. 

Kilbane, J. J., Sulfur-specific microbial metabolism of organic compounds. Reseources, Conservation and Recycling, 1990. 3 pp. 69-79. 

Two strains were isolated and purified, Pseudomonas sp. CDT-4, and Nocardia aster-oides, CDT-4b (ATCC 202160 and 202161, respectively). The microbes were passed through a multiple screen, first to allow growth on dibenzothiophene (DBT) as a sole source of sulfur, and then on fossil fuels, to identify organisms capable of desulfurization without metabolizing the DBT phenyl ring structures. N. asteroides sp. CDT-4b was found to metabolize DBT. The Pseudomonas species was found to utilize trace levels of sulfate from media and was found to be incapable of growth on DBT as a sole source of sulfur. However, the co-culture could remove more than 20% sulfur, with supplementation of a second sulfur-free carbon source. 

Microsomes are capable of oxidizing not only organic substrates but also inorganic ones. An interesting example is the metabolism of bisulfite (aqueous sulfur dioxide) in microsomes. Although mitochondrial sulfite oxidase is responsible for the in vivo oxidation of bisulfite by a two-electron mechanism, cytochrome P-450 is also able to reduce bisulfite to the sulfur dioxide radical anion [56] ... 

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