Structural Investigations of Biomimetic Complexes of Cytochrome P-450 by Difference EXAFS Spectroscopy View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

J. Goulon , M. Loos , I. Ascone , C. Goulon-Ginet , P. Battioni , J. P. Battioni , J. P. Mahy , D. Mansuy , B. Meunier

ABSTRACT

Over the past decade, intensive efforts have been made in the synthesis and structural study of high valent (porphyrinato):metal-oxo complexes which could mimic the heme mediated activation of oxygen as performed by monooxygenase hemoproteins like cytochromes P-450 or by hemoperoxidases like the horseradish peroxidase (HRP). Various oxidants: NaOCl, PhIO, alkylhydroperoxides or even molecular oxygen have been used in the frame of competing strategies [l]. In all cases, the central question is to know whether or not these compounds are featuring a real and short Metal…Oxygen double bond because it is currently postulated that formal FeV=0 species or a π-cation porphyrin FeIV=0 complex might be the active centers in the catalytic cycle of alkane hydroxylation by cytochromes P-450 and because such a short Fe… O bond was also detected recently by PENNER-HAHN et al. for HRP-I [2]. More... »

PAGES

191-200

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-642-71490-0_24

DOI

http://dx.doi.org/10.1007/978-3-642-71490-0_24

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1053401155


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