AI Article Synopsis
- Tridentate chelate ligands from the 2,6-bis[hydroxy(methyl)amino]-1,3,5-triazine family effectively release iron from human recombinant ferritin when oxygen is present.
- The release process is hindered by enzymes and compounds like superoxide dismutase, catalase, mannitol, and urea.
- The proposed mechanism includes the reduction of iron within ferritin by superoxide anions, the movement of iron(II) outside the ferritin, and the regeneration of superoxide ions due to the oxidation of iron(II) chelate complexes with oxygen.
Article Abstract
Tridentate chelate ligands of 2,6-bis[hydroxy(methyl)amino]-1,3,5-triazine family rapidly release iron from human recombinant ferritin in the presence of oxygen. The reaction is inhibited by superoxide dismutase, catalase, mannitol and urea. Suggested reaction mechanism involves reduction of the ferritin iron core by superoxide anion, diffusion of iron(II) cations outside the ferritin shell, and regeneration of superoxide anions through oxidation of iron(II) chelate complexes with molecular oxygen.
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| http://dx.doi.org/10.1039/c0cc03454a | DOI Listing |
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