Significant improvement of oxidase activity through the genetic incorporation of a redox-active unnatural amino acid.

ABSTRACT: While nature employs various covalent and non-covalent strategies to modulate tyrosine (Y) redox potential and pK _a in order to optimize enzyme activities, such approaches have not been systematically applied for the design of functional metalloproteins. Through the genetic incorporation of 3-methoxytyrosine (OMeY) into myoglobin, we replicated important features of cytochrome c oxidase (CcO) in this small soluble protein, which exhibits selective O₂ reduction activity while generating a small amount of reactive oxygen species (ROS). These results demonstrate that the electron donating ability of a tyrosine residue in the active site is important for CcO function. Moreover, we elucidated the structural basis for the genetic incorporation of OMeY into proteins b

SUBMITTER: Yu Y 

PROVIDER: S-EPMC4583198 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature