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

Smalley, John W.; Birss, Andrew J.; Szmigielski, Borys and Potempa, Jan (2008) Mechanism of methaemoglobin breakdown by the Lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis. Biochemical Journal, 389 (9). pp. 1235-1238. ISSN 1437-4315 (Online); 1431-6730 (Print)

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Official URL: http://www.reference-global.com/toc/bchm/current

Cited 8 times in WoS

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 heam-free globin susceptible to proteolytic attack.

Item Type:Article
Additional Information:published online: 17/09/2008. Citation Information. Biological Chemistry. Volume 389, Issue 9, Pages 1235–1238, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2008.140, September 2008
Uncontrolled Keywords:haem; haemoglobin; gingipains; Porphyromonas; periodontal disease; protease
Subjects:R Medicine > RK Dentistry
Departments, Research Centres and Related Units:Academic Faculties, Institutes and Research Centres > Faculty of Medicine > School of Dental Sciences
DOI:10.1515/BC.2008.140
Publisher's Statement:The Version of Record (VoR) is available at www.biochemj.org
Refereed:Yes
Status:Published
ID Code:946
Deposited On:05 Dec 2008 10:17
Last Modified:27 Mar 2012 09:16

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