Abstract:
:Using radiolysis with (32)P 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, alpha-meso hydroxyheme-HO. No heme degradation products were formed in control experiments with ferric HO or other heme proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Denisov IG,Ikeda-Saito M,Yoshida T,Sligar SGdoi
10.1016/s0014-5793(02)03674-8keywords:
subject
Has Abstractpub_date
2002-12-04 00:00:00pages
203-6issue
1-2eissn
0014-5793issn
1873-3468pii
S0014579302036748journal_volume
532pub_type
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