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Generation and Quantification of Formate Ion Produced from Aqueous Sodium Bicarbonate in the Presence of Homogeneous Ruthenium Catalyst.

ABSTRACT: Formic acid and its salts are an alternative source for hydrogen generation. In this study, we store hydrogen using the formate-bicarbonate cycle. Aqueous sodium bicarbonate is hydrogenated to form sodium formate, which can then be decomposed to release hydrogen and sodium bicarbonate. The hydrogenation step is carried out under mild conditions in the presence of a homogeneous ruthenium catalyst. Hydrogen charge is realized at 70 °C under a hydrogen pressure of 20 bar, achieving yields > 80% and turnover number > 610. The catalyst is stable and robust through numerous cycles of the hydrogenation reaction. The formate ion formed during the bicarbonate hydrogenation is assayed and quantified by ion chromatography.

SUBMITTER: Treigerman Z

PROVIDER: S-EPMC6644996 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:RationaleSalt sensitivity of blood pressure affects >30% of the hypertensive and >15% of the normotensive population. Variants of the electrogenic sodium bicarbonate cotransporter NBCe2 gene, SLC4A5, are associated with increased blood pressure in several ethnic groups. SLC4A5 variants are also highly associated with salt sensitivity, independent of hypertension. However, little is known about how NBCe2 contributes to salt sensitivity, although NBCe2 regulates renal tubular sodium bicarbonate transport. We hypothesized that SLC4A5 rs10177833 and rs7571842 increase NBCe2 expression and human renal proximal tubule cell (hRPTC) sodium transport and may be a cause of salt sensitivity of blood pressure.ObjectiveTo characterize the hRPTC ion transport of wild-type (WT) and homozygous variants (HV) of SLC4A5.Methods and resultsThe expressions of NBCe2 mRNA and protein were not different between hRPTCs carrying WT or HV SLC4A5 before or after dopaminergic or angiotensin (II and III) stimulation. However, luminal to basolateral sodium transport, NHE3 protein, and Cl-/HCO3- exchanger activity in hRPTCs were higher in HV than WT SLC4A5. Increasing intracellular sodium enhanced the apical location of NBCe2 in HV hRPTCs (4.24±0.35% to 11.06±1.72% (P<0.05, N = 3, 2-way ANOVA, Holm-Sidak test)) as determined by Total Internal Reflection Fluorescence Microscopy (TIRFM). In hRPTCs isolated from kidney tissue, increasing intracellular sodium enhanced bicarbonate-dependent pH recovery rate and increased NBCe2 mRNA and protein expressions to a greater extent in HV than WT SLC4A5 (+38.00±6.23% vs HV normal salt (P<0.01, N = 4, 2-way ANOVA, Holm-Sidak test)). In hRPTCs isolated from freshly voided urine, bicarbonate-dependent pH recovery was also faster in those from salt-sensitive and carriers of HV SLC4A5 than from salt-resistant and carriers of WT SLC4A5. The faster NBCe2-specific bicarbonate-dependent pH recovery rate in HV SCL4A5 was normalized by SLC4A5- but not SLC4A4-shRNA. The binding of purified hepatocyte nuclear factor type 4A (HNF4A) to DNA was increased in hRPTCs carrying HV SLC4A5 rs7571842 but not rs10177833. The faster NBCe2-specific bicarbonate-dependent pH recovery rate in HV SCL4A5 was abolished by HNF4A antagonists.ConclusionNBCe2 activity is stimulated by an increase in intracellular sodium and is hyper-responsive in hRPTCs carrying HV SLC4A5 rs7571842 through an aberrant HNF4A-mediated mechanism.

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Generation and Quantification of Formate Ion Produced from Aqueous Sodium Bicarbonate in the Presence of Homogeneous Ruthenium Catalyst.

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