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  2. Sulfur metabolism - Wikipedia

    en.wikipedia.org/wiki/Sulfur_metabolism

    From the sulfide they form the amino acids cysteine and methionine, sulfolipids, and other sulfur compounds. Animals obtain sulfur from cysteine and methionine in the protein that they consume. Sulfur is the third most abundant mineral element in the body. [21] The amino acids cysteine and methionine are used by the body to make glutathione.

  3. Methionine sulfoxide - Wikipedia

    en.wikipedia.org/wiki/Methionine_sulfoxide

    The sulfur-containing amino acids methionine and cysteine are more easily oxidized than the other amino acids. [ 1 ] [ 2 ] Unlike oxidation of other amino acids, the oxidation of methionine can be reversed by enzymatic action, specifically by enzymes in the methionine sulfoxide reductase family of enzymes.

  4. Sulfur-reducing bacteria - Wikipedia

    en.wikipedia.org/wiki/Sulfur-reducing_bacteria

    Desulfuromusa genus includes bacteria obligately anaerobic that use sulfur as an electron acceptor and short-chain fatty acids, dicarboxylic acids, and amino acids, as electron donors that are oxidized completely to CO 2. They are gram negative and complete oxidizer bacteria; their cells are motile and slightly curved or rod shaped.

  5. Organosulfur chemistry - Wikipedia

    en.wikipedia.org/wiki/Organosulfur_chemistry

    Nature is abound with organosulfur compounds—sulfur is vital for life. Of the 20 common amino acids, two (cysteine and methionine) are organosulfur compounds, and the antibiotics penicillin and sulfa drugs both contain sulfur. While sulfur-containing antibiotics save many lives, sulfur mustard is a deadly chemical warfare agent.

  6. Sulfur assimilation - Wikipedia

    en.wikipedia.org/wiki/Sulfur_assimilation

    Furthermore, the reduced sulfur is incorporated into cysteine, [2] an amino acid that is a precursor to many other sulfur-containing compounds. In animals, sulfur assimilation occurs primarily through the diet, as animals cannot produce sulfur-containing compounds directly.

  7. Adenylyl-sulfate reductase (thioredoxin) - Wikipedia

    en.wikipedia.org/wiki/Adenylyl-sulfate_reductase...

    The thioredoxin dependent adenylyl-sulfate reductase's cleaved disulfuric ions are incorporated into the molecular structure of the proto-proteins in the formation of the aforementioned amino acids. In studies such as one published in the Journal of Biological Chemistry experimentally observed the use of this enzyme type and thioredoxin in the ...

  8. Category:Sulfur amino acids - Wikipedia

    en.wikipedia.org/wiki/Category:Sulfur_amino_acids

    Pages in category "Sulfur amino acids" The following 24 pages are in this category, out of 24 total. This list may not reflect recent changes. A. Alliin; S-Allylcysteine;

  9. Microbial metabolism - Wikipedia

    en.wikipedia.org/wiki/Microbial_metabolism

    Sulfur oxidation involves the oxidation of reduced sulfur compounds (such as sulfide H 2 S), inorganic sulfur (S), and thiosulfate (S 2 O 2− 3) to form sulfuric acid (H 2 SO 4). A classic example of a sulfur-oxidizing bacterium is Beggiatoa, a microbe originally described by Sergei Winogradsky, one of the founders of environmental microbiology.

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