Insertion of a single oxygen atom into an unactivated substrate is an intriguing phenomenon in a variety of metalloenzymes, such as cytochrome P450. The mechanistic aspects of formation of reactive oxygen species (ROS) in oxygenation and peroxygenation (with hydrogen peroxide) reactions are not yet clearly understood, however the involvement of common ROS (Compound 0 and Compound I) have been proposed. Therefore, to understand proton transfer in monooxygenation, a holo-monooxygenase mimic have been generated using genetically incorporated redox-active 3-amino-L-tyrosine and dihydroxy-L-phenyl alanine into myoglobin (Mb) active site. This mutant showed high turnover rates for thioanisole and benzaldehyde oxidation (reported for the first time with Mb) compared to wild-type. In the presence of hydrogen peroxide significant increase (9-fold to 81-fold) in activity have been observed. This study offers insight into the role of the active site protein environment in oxygen activation in heme proteins.

Bioengineering of myoglobin: Implications for substrate oxidation

243rd National Meeting (2012)

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