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Absorption spectra of cytochrome P450 CAM in the reaction with peroxy acids
Author(s) -
Wagner Gerald C.,
Palcic Monica M.,
Dunford H.Brian
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80505-5
Subject(s) - chemistry , heme , substrate (aquarium) , hemeprotein , spectral line , cytochrome , absorption spectroscopy , cytochrome p450 , reaction intermediate , enzyme , cytochrome c , stereochemistry , spectroscopy , photochemistry , crystallography , analytical chemistry (journal) , computational chemistry , organic chemistry , catalysis , biochemistry , oceanography , physics , quantum mechanics , astronomy , mitochondrion , geology
The reaction of Fe(III) cytochrome P450 CAM with m ‐chloroperbenzoic acid was studied by rapid scanning absorption spectroscopy. Native low‐spin enzyme produced spectra characteristic of two reaction phases that were marked by time intervals with isosbestic positions. The high‐spin enzyme substrate complex yielded a series of Soret‐region spectra whose properties were dependent on peracid concentration. The simplest model describing the results was a sequence of at least two spectral intermediates, that were not entirely homologous with data measured in reactions with microsomal P450 LM2 . Comparisons with related heme protein states indicate higher Fe(IV) oxidation levels provide a plausible interpretation of the P450 CAM spectra.