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Significant Enhancement of Monooxygenase Activity of Oxygen Carrier Protein Hemocyanin by Urea

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journal contribution
posted on 2006-05-31, 00:00 authored by Chiyuki Morioka, Yoshimitsu Tachi, Shinnichiro Suzuki, Shinobu Itoh
Oxygenation of a series of p-substituted phenols to the corresponding catechols (phenolase activity) by the (μ-η22-peroxo)dicopper(II) species of Octopus hemocyanin has been directly examined for the first time by using a UV−vis spectroscopic method in a 0.5 M borate buffer solution containing 8 M urea under anaerobic conditions. Preliminary kinetic studies have indicated that the reaction involves an electrophilic aromatic substitution mechanism as in the case of phenolase reaction of tyrosinase. The oxygenation of phenols by hemocyanin also proceeded catalytically when the reaction was carried out under aerobic conditions.

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