Heme-(hydro)peroxide mediated O- and N-dealkylation - A study with microperoxidase

被引:27
作者
Boersma, MG
Primus, JL
Koerts, J
Veeger, C
Rietjens, IMCM
机构
[1] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[2] Wageningen Univ, Div Toxicol, NL-6703 HA Wageningen, Netherlands
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 2000年 / 267卷 / 22期
关键词
cytochrome P450; peroxidase; N-dealkylation; O-dealkylation;
D O I
10.1046/j.1432-1327.2000.01764.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The mechanism of microperoxidase-8 (MP-8) mediated O- and N-dealkylation was investigated. In the absence of ascorbate (peroxidase mode), many unidentified polymeric products are formed and the extent of substrate degradation correlates (r = 0.94) with the calculated substrate ionization potential, reflecting the formation of radical intermediates. In the presence of ascorbate (P450 mode) formation of polymeric products is largely prevented but, surprisingly, dealkylation is not affected. In addition, aromatic hydroxylation and oxidative dehalogenation is observed. The results exclude a radical mechanism and indicate the involvement of a (hydro)peroxo-iron heme intermediate in P450-type of heteroatom dealkylation.
引用
收藏
页码:6673 / 6678
页数:6
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