Myoglobin peroxidase activity

Roncone R, Monzani E, Nicolis S, Casella L (2004) Engineering and prosthetic-group modification of myoglobin peroxidase activity, chemical stability and unfolding properties. Eur J Inorg Chem 2203-2213... 

For practical purposes in immunohistochemistry, endogenous peroxidase activity can be defined as any activity that results in the decomposition of H202. Such activity is a common property of all hemoproteins such as hemoglobin (red cells), myoglobin (muscle cells), cytochrome (granulocytes, monocytes) and catalases (liver and kidney). Peroxidase activity may also be encountered in tissue areas adjacent to vascularized areas due to the diffusion of blood prior to fixation. 

Redaelli C, Monzani E, Santagostini L et al (2002) Characterization and peroxidase activity of a myoglobin mutant containing a distal arginine. ChemBioChem 3 226-233... 

Roncone R, Monzani E, Murtas M et al (2004) Engineering peroxidase activity in myoglobin the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine. Biochem J 377 717-724... 

Wan L, Twitchett MB, Eltis LD, Mauk AG, Smith M (1998) In vitro evolution of horse heart myoglobin to increase peroxidase activity. Proc Natl Acad Sci USA 95 12825-12831... 

Hayashi T, Murata D, Makino M (2006) Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene. Inorg Chem 45 10530-10536... 

Hayashi T, Hitomi Y, Ando T et al (1999) Peroxidase activity of myoglobin is enhanced by chemical mutation of heme-propionates. J Am Chem Soc 121 7747-7750... 

Matsuo T, Hayashi A, Abe M et al (2009) Meso-unsubstituted iron corrole in hemoproteins remarkable differences in effects on peroxidase activities between myoglobin and horseradish peroxidase. J Am Chem Soc 131 15124-15125... 

One set of site-directed mutagenesis studies improved the peroxygenase activity of Mb [128] in a different random mutagenesis study the peroxidase activity was improved. Clearly these reactions are very different from one another, and neither is myoglobin s natural function. Here is another example where an alternative scaffold supports functions that are characteristic of other conserved structures. Heme enzyme function is flexible and highly evolvable. 

Nevertheless, protein designers have recognized the importance of precisely defined OSC. Watanabe and coworkers have exploited the importance of the distal heme in 02-binding heme proteins to repurpose myoglobin for peroxidase activity... 

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