Abstract:
:The heme environmental structures of lactoperoxidase (LP) have been studied by the use of hyperfine-shifted proton NMR and optical absorption spectra. The NMR spectra of the enzyme in native and cyanide forms in H2O indicated that the fifth ligand of the heme iron is the histidyl imidazole with an anionic character and that the sixth coordination site is possibly vacant. These structural characteristics are quite similar to those of horseradish peroxidase (HRP), suggesting that these may be prerequisite to peroxidase activity. The pH dependences of the spectra of LP in cyanide and azide forms showed the presence of two ionizable groups with pK values of 6 and 7.4 in the heme vicinity, which is consistent with the kinetic results. The group with pK = 7.4 is associated with azide binding to LP in a slow NMR exchange limit, which is in contrast to the fast entry of azide to HRP.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Shiro Y,Morishima Idoi
10.1021/bi00368a002subject
Has Abstractpub_date
1986-10-07 00:00:00pages
5844-9issue
20eissn
0006-2960issn
1520-4995journal_volume
25pub_type
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