Potassium-induced partial inhibition of lactoperoxidase: structure of the complex of lactoperoxidase with potassium ion at 2.20 Å resolution.
Binding properties
Crystal structure
Distal heme cavity
Lactoperoxidase
Potassium ion
Journal
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
ISSN: 1432-1327
Titre abrégé: J Biol Inorg Chem
Pays: Germany
ID NLM: 9616326
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
received:
25
09
2020
accepted:
07
12
2020
pubmed:
12
1
2021
medline:
17
8
2021
entrez:
11
1
2021
Statut:
ppublish
Résumé
Lactoperoxidase, a heme-containing glycoprotein, catalyzes the oxidation of thiocyanate by hydrogen peroxide into hypothiocyanite which acts as an antibacterial agent. The prosthetic heme moiety is attached to the protein through two ester linkages via Glu258 and Asp108. In lactoperoxidase, the substrate-binding site is formed on the distal heme side. To study the effect of physiologically important potassium ion on the structure and function of lactoperoxidase, the fresh protein samples were isolated from yak (Bos grunniens) colostrum and purified to homogeneity. The biochemical studies with potassium fluoride showed a significant reduction in the catalytic activity. Lactoperoxidase was crystallized using 200 mM ammonium nitrate and 20% PEG-3350 at pH 6.0. The crystals of LPO were soaked in the solution of potassium fluoride and used for the X-ray intensity data collection. Structure determination at 2.20 Å resolution revealed the presence of a potassium ion in the distal heme cavity. Structure determination further revealed that the propionic chain attached to pyrrole ring C of the heme moiety, was disordered into two components each having an occupancy of 0.5. One component occupied a position similar to the normally observed position of propionic chain while the second component was found in the distal heme cavity. The potassium ion in the distal heme cavity formed five coordinate bonds with two oxygen atoms of propionic moiety, N
Identifiants
pubmed: 33427997
doi: 10.1007/s00775-020-01844-6
pii: 10.1007/s00775-020-01844-6
doi:
Substances chimiques
Heme
42VZT0U6YR
Hydrogen Peroxide
BBX060AN9V
Lactoperoxidase
EC 1.11.1.-
Potassium
RWP5GA015D
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
149-159Références
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