Journal
TOPICS IN CATALYSIS
Volume 65, Issue 1-4, Pages 187-195Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s11244-021-01444-x
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Funding
- NSFC [21933009, 22073077]
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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.
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.
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