Abstract
Porphyrin-sensitized photo-oxidation of bovine serum albumin results in oxidation at specific sites to produce protein radical species: at the Cys-34 residue (to give a thiyl radical) and at one or both tryptophan residues (Trp-134 and Trp-214) to give tertiary carbon-centered radicals and cause disruption of the indole ring system. This study shows that these photo-oxidation processes also consume oxygen and give rise to hydrogen peroxide, protein hydroperoxides, and carbonyl functions. The yield of hydrogen peroxide, protein hydroperoxides, and carbonyl functions is shown to be dependent on illumination time, the nature of the sensitizer, and the concentration of oxygen; the yield of hydroperoxides can also be markedly diminished by the presence of a spin trap which reacts with the initial protein radicals. The mechanism of formation of the protein hydroperoxides is suggested to be primarily through type I processes (i.e., independent of singlet oxygen), while type II (singlet oxygen) mechanisms may play a significant role in protein carbonyl formation. Reaction of the protein hydroperoxide species with metal ion complexes is shown to produce further protein-derived radicals which are predominantly present on amino acid side chains.
| Original language | English |
|---|---|
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 350 |
| Issue number | 2 |
| Pages (from-to) | 249-58 |
| Number of pages | 10 |
| ISSN | 0003-9861 |
| DOIs | |
| Publication status | Published - 15 Feb 1998 |
Keywords
- Animals
- Cysteine
- Electron Spin Resonance Spectroscopy
- Free Radicals
- Hydrogen Peroxide
- Light
- Oxidation-Reduction
- Oxygen
- Peroxides
- Photolysis
- Porphyrins
- Serum Albumin, Bovine
- Spin Trapping
- Tryptophan