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Does P450-type catalysis proceed through a peroxo-iron intermediate? A review of studies with microperoxidase.

Abstract：

:Recent stopped-flow kinetics demonstrated the existence of an intermediate before the occurrence of the final product of the reaction of both iron-containing microperoxidase-8 (Fe(III)MP-8) and manganese-containing microperoxidase-8 (Mn(III)MP-8) with H(2)O(2). The intermediate was assigned to be (hydro)peroxo-iron. With both mini-catalysts the final state obtained after 30-40 ms showed a resemblance to PorM(IV)MP-8[double bond]O(R(+)*); (R(+)*) is a radical located at the peptide. Quantum mechanical calculations indicate that hydroperoxo-iron is inactive as a catalytic intermediate in cytochrome P450 (P450)-type catalysis. Instead, the calculations suggest that peroxo-iron acts as the catalytic intermediate in P450-type catalysis. In addition, the calculations demonstrate that, although less likely, the possibility that oxenoid-iron acts as a catalytic intermediate in P450 catalysis cannot be fully excluded. An interesting aspect of the reactions catalysed by MP-8 is the possibility that, in view of the reversibility of the reactions between (hydro)peroxo-iron and oxenoid-iron, H(2)O plays a decisive role, at least in some cytochromes P450, in the removal of halogens, avoiding the production of compounds hazardous to the organism.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Veeger C

doi

10.1016/s0162-0134(02)00393-8

subject

Has Abstract

pub_date

2002-07-25 00:00:00

pages

35-45

issue

1

eissn

0162-0134

issn

1873-3344

pii

S0162013402003938

journal_volume

91

pub_type

杂志文章,评审

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