Pub. Date : 2018 Sep 26
PMID : 30145880
16 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | LC-MS/MS profiling reveals that the proteoforms of cytochrome c peroxidase (Ccp1) isolated from respiring yeast mitochondria are oxidized at numerous Met, Trp, and Tyr residues. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | LC-MS/MS profiling reveals that the proteoforms of cytochrome c peroxidase (Ccp1) isolated from respiring yeast mitochondria are oxidized at numerous Met, Trp, and Tyr residues. | Tyrosine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | In vitro oxidation of recombinant Ccp1 by H2O2 in the absence of its reducing substrate, ferrocytochrome c, gives rise to similar proteoforms, indicating uncoupling of Ccp1 oxidation and reduction in mitochondria. | Hydrogen Peroxide | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | The oxidative modifications found in the Ccp1 proteoforms are consistent with radical transfer (hole hopping) from the heme along several chains of redox-active residues (Trp, Met, Tyr). | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | The oxidative modifications found in the Ccp1 proteoforms are consistent with radical transfer (hole hopping) from the heme along several chains of redox-active residues (Trp, Met, Tyr). | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 6 | The oxidative modifications found in the Ccp1 proteoforms are consistent with radical transfer (hole hopping) from the heme along several chains of redox-active residues (Trp, Met, Tyr). | Tyrosine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 7 | Moreover, a decrease in recombinant Ccp1 oxidation by H2O2 in vitro in the presence of glutathione supports a protective role for hole hopping to this antioxidant. | Hydrogen Peroxide | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 8 | Moreover, a decrease in recombinant Ccp1 oxidation by H2O2 in vitro in the presence of glutathione supports a protective role for hole hopping to this antioxidant. | Glutathione | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 9 | Isolation and characterization of extramitochondrial Ccp1 proteoforms reveals that hole hopping from the heme in these proteoforms results in selective oxidation of the proximal heme ligand (H175) and heme labilization. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 10 | Isolation and characterization of extramitochondrial Ccp1 proteoforms reveals that hole hopping from the heme in these proteoforms results in selective oxidation of the proximal heme ligand (H175) and heme labilization. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 11 | Isolation and characterization of extramitochondrial Ccp1 proteoforms reveals that hole hopping from the heme in these proteoforms results in selective oxidation of the proximal heme ligand (H175) and heme labilization. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 12 | The targeting of Ccp1 for selective H175 oxidation may be linked to the phosphorylation status of Y153 close to the heme since pY153 is abundant in certain proteoforms. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 13 | In sum, when insufficient electrons from ferrocytochrome c are available to Ccp1 in mitochondria, hole hopping from its heme expands its physiological functions. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 14 | Specifically, we observe an unprecedented hole-hopping sequence for heme labilization and identify hole-hopping pathways from the heme to novel substrates and to glutathione at Ccp1"s surface. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 15 | Specifically, we observe an unprecedented hole-hopping sequence for heme labilization and identify hole-hopping pathways from the heme to novel substrates and to glutathione at Ccp1"s surface. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 16 | Specifically, we observe an unprecedented hole-hopping sequence for heme labilization and identify hole-hopping pathways from the heme to novel substrates and to glutathione at Ccp1"s surface. | Glutathione | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |