초록
<P>Herein, we report the site-specific incorporation of <SMALL>L</SMALL>-3,4-dihydroxyphenylalanine as a promising method to engineer an oxygen-tolerant alcohol dehydrogenase II. The engineered mutant alcohol dehydrogenase II binds Zn<SUP>2+</SUP> with high binding affinity and is functional under aerobic and oxidative conditions for a longer time than the wild-type, Fe<SUP>2+</SUP>-binding alcohol dehydrogenase II. Overall, the mutant enzyme demonstrated electrochemical activity toward both acetaldehyde reduction and ethanol oxidation reactions. This enzyme could have a potential use in efficient biofuel production under aerobic conditions in photosynthetic organisms despite the inherent oxygen evolution reaction by photosystem II.</P><BR>[FIG OMISSION]</BR>