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Formation of Iron(II)-Nitrosoalkane Complexes: A New Activity of Microperoxidase 8

R R Ricoux, J L JL Boucher, D D Mansuy, and J P JP Mahy

Biochem Biophys Res Commun 278(1):7 (2000) PMID 11071875

Microperoxidase 8 (MP8) is a heme octapeptide, obtained by enzymatic hydrolysis of heart cytochrome c, in which a histidine is axially coordinated to the heme iron, and acts as its fifth ligand. It exhibits two kinds of activities: a peroxidase-like activity and a cytochrome P450-like activity. We here show that MP8 is not only able to oxidize various aliphatic and aromatic hydroxylamines with the formation of MP8-Fe(II)-nitrosoalkane or -arene complexes absorbing around 414 nm, but also that these complexes can be obtained by reduction of nitroalkanes. This is the first example of fully characterized iron(II)-metabolite complexes of MP8. Such complexes constitute good models for those obtained upon oxidation of amphetamine or macrolids by cytochromes P450. In addition, this is a new catalytic activity of MP8, which validates the use of this mini-enzyme as a convenient model for hemoproteins of interest in toxicology and pharmacology such as cytochromes P450 and peroxidases.

Copyright © 2000 Elsevier Ltd. All rights reserved.

DOI: 10.1006/bbrc.2000.3785
Version: za2963e q8za7 q8zbf q8zc3 q8zd1 q8ze9 q8zf6 q8zgb

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