Structural characterization of lactoperoxidase in the heme environment by proton NMR spectroscopy.

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

Biochemistry

journal_title

Biochemistry

authors

Shiro Y,Morishima I

doi

10.1021/bi00368a002

subject

Has Abstract

pub_date

1986-10-07 00:00:00

pages

5844-9

issue

20

eissn

0006-2960

issn

1520-4995

journal_volume

25

pub_type

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