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Hot nitric acid diffusion in fluoroelastomer composite and its degradation.

ABSTRACT: Fluoroelastomers (FKM) are vital sealing materials in acidic environment and their failure can cause severe safety problems. Therefore, investigation of the degradation behavior and mechanism of FKM materials is of great significant. Herein, we investigate a diffusion model of an acidic solution into an FKM composite and its degradation behavior upon immersion in hot nitric acid solution. The results indicate that the diffusion process of the HNO₃ solution into the FKM composite conforms to the Fick diffusion model at a low concentration of nitric acid solution. Besides, the concentration of HNO₃ solution affects the diffusion process of solvent molecules and the dissolution process of the filler particles to some extent. SEM showed that the surface topography of the FKM was significantly altered after it was immersed in HNO₃ solution. The structural and chemical changes of the FKM were studied using ATR-FTIR, SEM-EDS and MAS NMR, which demonstrated the occurrence of decrosslinking via hydrolysis of the crosslinks and backbone cleavage by dehydrofluorination. This was also manifested by the decrease in crosslinking degree and mechanical properties. The present study is helpful for revealing the chemical changes in FKM in hot HNO₃ solution.

SUBMITTER: Kang H

PROVIDER: S-EPMC9075819 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Hot nitric acid diffusion in fluoroelastomer composite and its degradation.

Kang Hailan H Chen Long L Du Hongyang H Wang Haoyu H Li Donghan D Fang Qinghong Q

RSC advances 20191121 65

Fluoroelastomers (FKM) are vital sealing materials in acidic environment and their failure can cause severe safety problems. Therefore, investigation of the degradation behavior and mechanism of FKM materials is of great significant. Herein, we investigate a diffusion model of an acidic solution into an FKM composite and its degradation behavior upon immersion in hot nitric acid solution. The results indicate that the diffusion process of the HNO<sub>3</sub> solution into the FKM composite confo ...[more]

PMID: 35541790

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Project description:Human cytochrome P450 (P450) CYP2B6 undergoes nitric oxide (NO)-dependent proteasomal degradation in response to the NO donor dipropylenetriamine NONOate (DPTA) and biologic NO in HeLa and HuH7 cell lines. CYP2B6 is also downregulated by NO in primary human hepatocytes. We hypothesized that NO or derivative reactive nitrogen species may generate adducts of tyrosine and/or cysteine residues, causing CYP2B6 downregulation, and selected Tyr and Cys residues for mutation based on predicted solvent accessibility. CYP2B6V5-Y317A, -Y380A, and -Y190A mutant proteins expressed in HuH7 cells were less sensitive than wild-type (WT) enzyme to degradation evoked by DPTA, suggesting that these tyrosines are targets for NO-dependent downregulation. The Y317A or Y380A mutants did not show increases in high molecular mass (HMM) species after treatment with DPTA or bortezomib + DPTA, in contrast to the WT enzyme. Carbon monoxide-releasing molecule 2 treatment caused rapid suppression of 2B6 enzyme activity, significant HMM species generation, and ubiquitination of CYP2B6 protein but did not stimulate CYP2B6 degradation. The CYP2B6 inhibitor 4-(4-chlorophenyl)imidazole blocked NO-dependent CYP2B6 degradation, suggesting that NO access to the active site is important. Molecular dynamics simulations predicted that tyrosine nitrations of CYP2B6 would cause significant destabilizing perturbations of secondary structure and remove correlated motions likely required for enzyme function. We propose that cumulative nitrations of Y190, Y317, and Y380 by reactive nitrogen species cause destabilization of CYP2B6, which may act synergistically with heme nitrosylation to target the enzyme for degradation. SIGNIFICANCE STATEMENT: This work provides novel insight into the mechanisms by which nitric oxide, which is produced in hepatocytes in response to inflammation, triggers the ubiquitin-dependent proteasomal degradation of the cytochrome P450 (P450) enzyme CYP2B6. Our data demonstrate that both nitration of specific tyrosine residues and interaction of nitric oxide (NO) with the P450 heme are necessary for NO to trigger ubiquitination and protein degradation.

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Hot nitric acid diffusion in fluoroelastomer composite and its degradation.

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Hot nitric acid diffusion in fluoroelastomer composite and its degradation.

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