Catalase (EC 126.96.36.199) is a heme-containing enzyme ubiquitously present in most aerobic organisms. Although the full range of biological functions of catalase still remains unclear, its main function is the decomposition of hydrogen peroxide into water and oxygen. Catalases have been studied for over 100 years, with examples of the enzyme isolated, purified, and characterized from many different organisms. The crystal structures of 16 heme-containing catalases have now been solved, revealing a common, highly conserved core in all enzymes. The active center consists of a heme with a tyrosine ligand on the proximal side and a conserved histidine and an aspartate on the distal side. Although catalases have been studied for many years, additional functions of catalases have recently been recognized. For example, Scytalidium thermophilum catalase (CATPO) has been shown to oxidize o-diphenolic and some p-diphenolic compounds in the absence of hydrogen peroxide. This and other studies have led to the proposal that this secondary oxidative activity may be a general characteristic of catalases. The present chapter will focus on the function and structure of monofunctional heme catalases, emphasizing the information obtained in the last few years mainly in relation to the secondary activity of these enzymes.
Part of the book: Glutathione System and Oxidative Stress in Health and Disease