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Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis

  • John W. Smalley , Andrew J. Birss , Borys Szmigielski and Jan Potempa
Published/Copyright: August 19, 2008
Biological Chemistry
From the journal Volume 389 Issue 9

Abstract

The R- and K-gingipain proteases of Porphyromonas gingivalis are involved in proteolysis of haemoglobin from which the defensive dimeric haem pigment is formed. Whilst oxyhaemoglobin is refractory towards K-gingipain, methaemoglobin is rapidly degraded. Ligation of methaemoglobin with N3-, which effectively blocks haem dissociation from the protein, prevented haemoglobin breakdown. Haem-free globin was rapidly degraded by K-gingipain. These data emphasise the need for haemoglobin oxidation which encourages haem dissociation and makes the haem-free globin susceptible to proteolytic attack.


Corresponding author

Received: 2008-4-1
Accepted: 2008-4-28
Published Online: 2008-08-19
Published in Print: 2008-09-01

©2008 by Walter de Gruyter Berlin New York

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