Cryogenic absorption spectra of hydroperoxo-ferric heme oxygenase, the active intermediate of enzymatic heme oxygenation.

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 Lett

journal_title

FEBS letters

authors

Denisov IG,Ikeda-Saito M,Yoshida T,Sligar SG

doi

10.1016/s0014-5793(02)03674-8

keywords:

subject

Has Abstract

pub_date

2002-12-04 00:00:00

pages

203-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014579302036748

journal_volume

532

pub_type

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