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Evidence for enormous iodide anion migration in lanthanum oxyiodide–based solid

ABSTRACT: Description Iodide ion conduction was demonstrated and quantified. The I− ion conduction was demonstrated and quantified in the La0.70Sr0.25Zn0.05OI0.70 solid. The I− ion is considered to be an inferior conductor because of its large ionic size compared to the previously reported conducting ion species. Using modified Tubandt electrolysis, a weight increase at the anodic pellet and a corresponding weight decrease at the cathodic pellet were observed. The weight changes were in good agreement with the theoretical values estimated by considering pure I− ion migration. Furthermore, the iodine element appeared at the anode, and the iodine concentration at the cathode decreased after electrolysis, indicating that the migrating species was only I−. This is the first study to elucidate the conduction of iodide ions in solids.

SUBMITTER: Imanaka N

PROVIDER: S-EPMC8535799 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:The sodium iodide symporter (NIS) transports iodide, which is necessary for thyroid hormone production. NIS also transports other monovalent anions such as tetrafluoroborate (BF4-), pertechnetate (TcO4-), and thiocyanate (SCN-), and is competitively inhibited by perchlorate (ClO4-). However, the mechanisms of substrate selectivity and inhibitor sensitivity are poorly understood. Here, a comparative approach was taken to determine whether naturally evolved NIS proteins exhibit variability in their substrate transport properties. The NIS proteins of thirteen animal species were initially assessed, and three species from environments with differing iodide availability, freshwater species Danio rerio (zebrafish), saltwater species Balaenoptera acutorostrata scammoni (minke whale), and non-aquatic mammalian species Homo sapiens (human) were studied in detail. NIS genes from each of these species were lentivirally transduced into HeLa cells, which were then characterized using radioisotope uptake assays, 125I- competitive substrate uptake assays, and kinetic assays. Homology models of human, minke whale and zebrafish NIS were used to evaluate sequence-dependent impact on the organization of Na+ and I- binding pockets. Whereas each of the three proteins that were analyzed in detail concentrated iodide to a similar degree, their sensitivity to perchlorate inhibition varied significantly: minke whale NIS was the least impacted by perchlorate inhibition (IC50 = 4.599 ?M), zebrafish NIS was highly sensitive (IC50 = 0.081 ?M), and human NIS showed intermediate sensitivity (IC50 = 1.566 ?M). Further studies with fifteen additional substrates and inhibitors revealed similar patterns of iodide uptake inhibition, though the degree of 125I- uptake inhibition varied with each compound. Kinetic analysis revealed whale NIS had the lowest Km-I and the highest Vmax-I. Conversely, zebrafish NIS had the highest Km and lowest Vmax. Again, human NIS was intermediate. Molecular modeling revealed a high degree of conservation in the putative ion binding pockets of NIS proteins from different species, which suggests the residues responsible for the observed differences in substrate selectivity lie elsewhere in the protein. Ongoing studies are focusing on residues in the extracellular loops of NIS as determinants of anion specificity. These data demonstrate significant transport differences between the NIS proteins of different species, which may be influenced by the unique physiological needs of each organism. Our results also identify naturally-existing NIS proteins with significant variability in substrate transport kinetics and inhibitor sensitivity, which suggest that the affinity and selectivity of NIS for certain substrates can be altered for biotechnological and clinical applications. Further examination of interspecies differences may improve understanding of the substrate transport mechanism.

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Evidence for enormous iodide anion migration in lanthanum oxyiodide–based solid

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