We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Cryogenic absorption spectra of hydroperoxo-ferric heme oxygenase, the active intermediate of enzymatic heme oxygenation
- Authors
Denisov, Ilia G.; Ikeda-Saito, Masao; Yoshida, Tadashi; Sligar, Stephen G.
- Abstract
Using radiolysis with 32P enriched phosphate as an internal source of ionizing radiation, the formation of hydroperoxo-ferric complex from oxy-ferrous precursor with a high yield was monitored at 77 K in heme oxygenase (HO) by means of optical absorption spectroscopy. Well-resolved absorption spectra (maxima at 421 nm, 530 nm, 557 nm) of hydroperoxo-ferric intermediate of this heme enzyme were measured in 70% glycerol/buffer frozen glasses. After annealing at 210–215 K this complex converts to the product complex, α-meso hydroxyheme-HO. No heme degradation products were formed in control experiments with ferric HO or other heme proteins.
- Subjects
HEME oxygenase; ABSORPTION spectra
- Publication
FEBS Letters, 2002, Vol 532, Issue 1/2, p203
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03674-8