Classical catalase: ancient and modern.
This review describes the historical difficulties in devising a kinetically satisfactory mechanism for the classical catalase after its identification as a unique catalytic entity in 1902 and prior to the breakthrough 1947 analysis by Chance and co-workers which led to the identification of peroxide compounds I and II. The role of protons in the formation of these two ferryl complexes is discussed and current problems of inhibitory ligand and hydrogen donor binding at the active site are outlined, especially the multiple roles involving formate or formic acid. A previous mechanism of NADPH-dependent catalase protection against substrate inhibition is defended. A revised model linking the catalytic ('catalatic') action and the one-electron side reactions involving compound II is suggested. And it is concluded that, contrary to an idea proposed in 1963 that eukaryotic catalase might be a 'fossil enzyme', current thinking gives it a central role in the redox protective processes of long term importance for human and other eukaryotic and prokaryotic life.
Department of Biological Sciences, University of Essex, Colchester Essex CO4 3SQ, UK. pnicholl@essex.ac.uk
Peter
P
Nicholls
D001671:Biochemistry / Q000266:history*; D002374:Catalase / Q000378:metabolism / Q000502:physiology*; D004583:Electrons; D015971:Gene Expression Regulation, Enzymologic; D006418:Heme / Q000737:chemistry; D049673:History, 20th Century; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D008968:Molecular Conformation; D009249:NADP / Q000737:chemistry; D011522:Protons
D008024:Ligands; D011522:Protons; D006418:Heme; D009249:NADP; D002374:Catalase