Abstract
Lignin peroxidase, cytochrome c and haemoglobin were tested for oxidation of polycyclic aromatic hydrocarbon (PAH) in the presence of hydrogen peroxide. The reaction mixture Contained water-miscible organic solvents in order to reduce the mass transfer limitation of hydrophobic substrates. The reaction products from all three haemoproteins were mainly quinones, suggesting the same oxidation mechanism for the three biocatalysts. The haeme prosthetic group must have located in a protein environment for it to catalyze these reactions, and only certain types of protein environment are able to induce this type of haemebased catalytic activity. The solvent hydrophobicity is a factor affecting the biocatalysis in organic media. Substrate partitioning between the active site (haeme) and the bulk solvent is the main factor of the biocatalytic behaviour in organic solvent mixtures. Site-directed mutagenesis of yeast cytochrome c significantly altered the kinetic behaviour of the protein. The Gly82;Thr 102 variant was 10 times more active and showed a catalytic efficiency 10-fold greater than the wild-type iso-1-cytochrome c. These results suggest that it is possible to design a new biocatalyst for environmental purposes.
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