Mechanism of O2activation and substrate hydroxylation in noncoupled binuclear copper monooxygenases

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Abstract
Significance: Nature has evolved several strategies for using dioxygen (O2) for chemical oxidations. These enzymatic processes typically use metal cofactors to impart selectivity and minimize production of deleterious reactive oxygen species. In particular, hormone biosynthesis and neurotransmitter regulation are accomplished by copper- and O2-dependent enzymes possessing a unique copper active site; however, the mechanism has been debated and the role of the unique active site structure in enabling the chemistry is unclear. To understand this, structural and spectroscopic data are used to computationally model the full reaction mechanism to define the molecular basis for O2reactivity and define the role of the active site structure in controlling proper enzymatic function.
Funding Information
  • HHS | National Institutes of Health (R01-DK31450)
  • HHS | National Institutes of Health (F32-GM105288)

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