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Horseradish peroxidase formation, modeling

I. M.C.M., Reversible formation of high-valent-iron-oxo prophyrin intermediates in heme-based catalysis revisiting the kinetic model for horseradish peroxidase, Inorg. Chim. Acta, 275/276, 98-105, 1998. [Pg.686]

Iron (IV, V) porphyrins were studied by resonance Raman spectroscopy. These compounds have biological significance, because oxoferryl posphyrins 0=Fe (TV)(por) are involved in enzymatic reactions of cytochrome P450, horseradish peroxidase (HRP). and related heme proteins. The mechanism of formation of the oxoferryl porphyrin Ti-cation radical was determined from resonance Raman measurements. The former radical is considered to be a model compound of HRP-I. [Pg.1561]

See other pages where Horseradish peroxidase formation, modeling is mentioned: [Pg.185]    [Pg.162]    [Pg.92]    [Pg.481]    [Pg.156]    [Pg.2189]    [Pg.138]    [Pg.191]    [Pg.383]    [Pg.45]    [Pg.2188]    [Pg.25]    [Pg.148]    [Pg.491]    [Pg.201]    [Pg.143]   
See also in sourсe #XX -- [ Pg.72 , Pg.73 , Pg.74 , Pg.75 , Pg.76 , Pg.77 , Pg.78 , Pg.79 ]



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