Jump to main content
Jump to site search
SCHEDULED MAINTENANCE Close the message box

Maintenance work is planned for Monday 16 August 2021 from 07:00 to 23:59 (BST).

Website performance may be temporarily affected and you may not be able to access some PDFs or images. If this does happen, refreshing your web browser should resolve the issue. We apologise for any inconvenience this might cause and thank you for your patience.


All chapters

Chapter 8

Mechanistic Aspects of Catalase-peroxidase

Catalase-peroxidases (KatGs) belong to the peroxidase-catalase superfamily and are found in bacteria, archaea, and lower eukaryotes including fungi. Despite having sequence and structural homology with monofunctional peroxidases, KatGs are the only bifunctional peroxidases with a dominating hydrogen peroxide dismutating activity which rivals that of typical catalases. Albeit both heme-containing catalases and KatGs catalyse the same reaction (2H2O2→2H2O+O2), the mechanism is clearly different. In KatG the activity is based on two redox cofactors, the iron-containing heme b and in close proximity the unique posttranslationally and endogenously generated Trp-Tyr-Met adduct. This strictly conserved adduct is essential for the pseudocatalytic activity of KatGs without influencing the peroxidase activity. The key element in the proposed reaction mechanism is the formation of an adduct radical during turnover. This review accounts for the available literature for this mechanism and additionally discusses the role of the peroxidase activity with a focus on the activation of the antitubercular pro-drug isoniazid by KatG.

Publication details


Print publication date
27 Oct 2015
Copyright year
2016
Print ISBN
978-1-84973-911-5
PDF eISBN
978-1-78262-262-8
ePub eISBN
978-1-78262-742-5
From the book series:
Metallobiology