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A Road Less Traveled: Trafficking Hydrogen Sulfide and B 12
Author(s) -
Banerjee Ruma
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.340.1
Subject(s) - intracellular , enzyme , cofactor , biochemistry , metabolism , chemistry , hydrogen sulfide , biology , microbiology and biotechnology , sulfur , organic chemistry
Similar in their very low intracellular abundance, the metabolism of hydrogen sulfide (H 2 S) and vitamin B 12 intersect at the sulfur mobility in PPD network where B 12 serves as a cofactor, and H 2 S spews from enzymes with relaxed specificity. While only two mammalian enzymes require B 12 for activity, cells maintain a regiment of chaperones to tailor and escort B 12 from its point of entry into the cell to its targets. During this inter‐compartmental voyage, B 12 is translocated between active sites in transient protein‐protein complexes, which exhibit the artful use of coordination chemistry. Structural enzymology studies on trafficking proteins are providing molecular insights into the cellular strategies for moving this portly organometallic cofactor. While the metabolic activity of gut microbiota represents a limited source of B 12 , it is a substantial source of H 2 S and necessitates adaptations by host cells to routine exposure to this respiratory toxin. Our studies are revealing the metabolic reprogramming that is part of the stress response to H 2 S in colon epithelial cells. Thus, although low in abundance, B 12 and H 2 S have profound impacts on cellular biochemistry. Support or Funding Information National Institutes of Health (DK45776, HL58984, GM112455) This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .