In Biotech Business Week, September 3, 2007, BIOMEDICINE; Report summarizes biomedicine study findings from Osaka City University, Department of Chemistry was published. The experiment's goal is to determine the monoxygenase activity of three copper proteins and undergo ortho-hydroxylation of phenols and later electrophilic aromatic substitution to give the final product. During this experiment, the third copper protein tested undergoes electrophilic aromatic substitution. Lithium phenolates and peroxo dicopper(II) will react by electrophilic aromatic substitution to give an oxygenated product called catechols. The researchers determined that the monoxygenase activity is similar to that of tyrosinase because they both undergo a simple enzymatic reaction that is the same mechanism as electrophilic aromatic substition. In the conclusion, the author states, "In this case as well, the ortho-hydroxylation of phenols to catechols has been demonstrated to involve the same ionic mechanism." The ionic mechanism being electrophilic aromatic substitution.
Jesslyn
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After studying EAS for a few weeks now, it's kind of cool to actually understand what that last quote you used means. A month ago "ortho-hydroxylation of phenols" would have had no means to me at all but now I can picture that vividly in my mind. I think it might have been helpful in this post to say why their finding was important or relevant. But helpful find overall on research that involves what we have been directly studying about in class.
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