Abstract
Microperoxidase 8 (MP8) is obtained by controlled proteolytic digestion of horse heart cytochrome c (Aron et al 1986). It consists of an iron(III)-protoporphyrin IX covalently bound through thioether links to two cysteine side chains and a histidine is axially coordinated to the heme iron, and acts as its fifth ligand. MP8 has an open active site, which leads to broad substrate specificity in the two types of catalytic activities it shows: a peroxidase-like activity (Baldwin et al 1987) and a cytochrome P450-like activity (Osman et al 1996).
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References
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Ricoux, R., Boucher, JL., Mansuy, D., Mahy, JP. (2001). Microperoxidase 8 (MP8) as a Convenient Model for Hemoproteins: Formation and Characterisation of New Iron(II)-Nitrosoalkane Complexes of Biological Relevance. In: Dansette, P.M., et al. Biological Reactive Intermediates VI. Advances in Experimental Medicine and Biology, vol 500. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0667-6_19
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DOI: https://doi.org/10.1007/978-1-4615-0667-6_19
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