Recent Computational Insights into the Oxygen Activation by Copper-Dependent Metalloenzymes

Dioxygen-(O-2) is a key component of the earth's atmosphere and is essential for life activities on the planet. Upon-O-2 activation, metalloenzymes are able to mediate various oxidative transformations related to many biosynthesis and metabolism processes. In this mini-review, we focus on the recent computational insights into the oxygen activation by several copper-dependent enzymes, including mono-copper enzyme lytic polysaccharide monooxygenase (LPMO), particulate methane monooxygenase (pMMO), as well as the binuclear copper enzymes peptidylglycine alpha-hydroxylating monooxygenase (PHM) and dopamine beta-monooxygenase (D beta M). Understanding the structure-function relationships of these enzymes is of fundamental importance in chemistry and biology, and is also beneficial to engineering of these metalloenzymes for new functions.

Automated summary

Activation of dioxygen allows metalloenzymes to mediate various oxidative transformations crucial for biosynthesis and metabolism processes. Recent computational insights into oxygen activation by copper-dependent enzymes are essential for understanding their structure-function relationships and engineering these metalloenzymes for novel functions.