Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10768218 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
O2-dependent reactions of the ferric and ferrous forms of α-hydroxyheme complexed with water-soluble rat heme oxygenase-1 were examined by rapid-scan stopped-flow measurements. Ferric α-hydroxyheme reacted with O2 to form ferric verdoheme with an O2-dependent rate constant of 4 Ã 105 Mâ1 sâ1 at pH 7.4 and 9.0. A decrease of the rate constant to 2.8 Ã 105 Mâ1 sâ1 at pH 6.5 indicates that the reaction proceeds by direct attack of O2 on the Ï-neutral radical form of α-hydroxyheme, which is generated by deprotonation of the α-hydroxy group. The reaction of ferrous α-hydroxyheme with O2 yielded ferrous verdoheme in a biphasic fashion involving a new intermediate having absorption maxima at 415 and 815 nm. The rate constants for this two-step reaction were 68 and 145 sâ1. These results show that conversion of α-hydroxyheme to verdoheme is much faster than the reduction of coordinated iron (<1 sâ1) under physiological conditions [Y. Liu, P.R. Ortiz de Montellano, Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1, J. Biol. Chem. 275 (2000) 5297-5307], suggesting that, in vivo, the conversion of ferric α-hydroxyheme to ferric verdoheme precedes the reduction of ferric α-hydroxyheme.
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Authors
Hiroshi Sakamoto, Kenichi Takahashi, Yuichiro Higashimoto, Saori Harada, Graham Palmer, Masato Noguchi,