He, Kan published the artcileIdentification of the Heme-Modified Peptides from Cumene Hydroperoxide-Inactivated Cytochrome P450 3A4, Related Products of amides-buliding-blocks, the main research area is cytochrome P450 3A4 heme peptide cumene hydroperoxide inactivation.
Cumene hydroperoxide-mediated (CuOOH-mediated) inactivation of cytochromes P 450 (CYPs) results in destruction of their prosthetic heme to reactive fragments that irreversibly bind to the protein. We have attempted to characterize this process structurally, using purified, 14C-heme labeled, recombinant human liver P 450 3A4 as the target of CuOOH-mediated inactivation, and a battery of protein characterization approaches [chem. (CNBr) and proteolytic (lysylendopeptidase-C) digestion, HPLC-peptide mapping, microEdman sequencing, and mass spectrometric analyses]. The heme-peptide adducts isolated after CNBr/lysylendopeptidase-C digestion of the CuOOH-inactivated P 450 3A4 pertain to two distinct P 450 3A4 active site domains. One of the peptides isolated corresponds to the proximal helix L/Cys-region peptide 429-450 domain and the others to the K-region (peptide 359-386 domain). Although the precise residue(s) targeted remain to be identified, we have narrowed down the region of attack to within a 17 amino acid peptide (429-445) stretch of the 55-amino acid proximal helix L/Cys domain. Furthermore, although the exact structures of the heme-modifying fragments and the nature of the adduction remain to be established conclusively, the incremental masses of ≈ 302 and 314 Da detected by electrospray mass spectrometric analyses of the heme-modified peptides are consistent with a dipyrrolic heme fragment comprised of either pyrrole ring A-D or B-C, a known soluble product of peroxidative heme degradation, as a modifying species.
Biochemistry published new progress about Enzyme functional sites, active. 359-38-6 belongs to class amides-buliding-blocks, name is 2,2-Difluoroacetamide, and the molecular formula is C2H3F2NO, Related Products of amides-buliding-blocks.
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