5,10,15,20-Tetrakis(4-sulfonatophenyl)porphyrinato iron(III) chloride (FeTPPS), a peroxynitrite decomposition catalyst, catalyzes protein tyrosine nitration in the presence of hydrogen peroxide and nitrite
Zhang, P; Ma, L; Yang, Z; Li, H; Gao, Z
| HERO ID | 4328149 |
|---|---|
| In Press | No |
| Year | 2018 |
| Title | 5,10,15,20-Tetrakis(4-sulfonatophenyl)porphyrinato iron(III) chloride (FeTPPS), a peroxynitrite decomposition catalyst, catalyzes protein tyrosine nitration in the presence of hydrogen peroxide and nitrite |
| Authors | Zhang, P; Ma, L; Yang, Z; Li, H; Gao, Z |
| Journal | Journal of Inorganic Biochemistry |
| Volume | 183 |
| Page Numbers | 9-17 |
| Abstract | 5,10,15,20-Tetrakis(4-sulfonatophenyl)porphyrinato iron(III) chloride (FeTPPS) is a water-soluble heme analog, which has been used as a scavenger of peroxynitrite in many studies. Similar to heme, it may also possess pseudo-peroxidase activity that could cause protein tyrosine nitration through the peroxidase-H2O2-NO2- pathway. In this paper, we used western blotting and spectrophotometry analysis to study the capability of FeTPPS in catalyzing protein tyrosine nitration. Furthermore, the capability of FeTPPS in catalyzing protein nitration in tissue homogenate and cultured cells was also investigated. Our results showed that FeTPPS induced bovine serum albumin (BSA) nitration in the presence of H2O2 and NaNO2, and the reaction was dose-, time- and pH-dependent. In acidic condition, more protein was nitrated by FeTPPS than heme, which corresponded to their peroxidase activities. Meanwhile, our results also confirmed the catalytic effect of FeTPPS on protein tyrosine nitration in rat brain homogenate and human hepatocellular carcinoma (HepG2) cells. At the end of this study, we used liquid chromatography (LC)-tandem mass spectrometry (MS/MS) to investigate differences of site selectivity between heme and FeTPPS catalyzed protein tyrosine nitration. The result indicated that FeTPPS tended to catalyze tyrosine residues locating in more hydrophilic sites, whereas heme was more likely to induce nitration of tyrosine residues locating in relatively hydrophobic environment. Taken together, this is the first report that FeTPPS is an effective and convenient nitration catalyzer in vitro, and this study confirms that the hydrophilicity of the nitrating agents would play an important role in nitration site selection. |
| Doi | 10.1016/j.jinorgbio.2018.03.003 |
| Pmid | 29525695 |
| Wosid | WOS:000432233100002 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |