Non-Coordinative Binding of O2 at the Active Center of a Copper-Dependent Enzyme

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Non-Coordinative Binding of O2 at the Active Center of a Copper-Dependent Enzyme

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	4639984
Author(s)	Leisinger, Florian; Miarzlou , Dzmitry A.; Seebeck, Florian P.
Author(s) at UniBasel	Seebeck, Florian Peter
Year	2021
Title	Non-Coordinative Binding of O2 at the Active Center of a Copper-Dependent Enzyme
Journal	Angewandte Chemie International Edition
Volume	60
Number	11
Pages / Article-Number	6154-6159
Keywords	C−H activation; copper enzyme; low dose crystallography; oxygen activation
Abstract	Molecular oxygen (O 2 ) is a sustainable oxidation reagent. O 2 is strongly oxidizing but kinetically stable and its final reaction product is water. For these reasons learning how to activate O 2 and how to steer its reactivity along desired reaction pathways is a longstanding challenge in chemical research. [1] Activation of ground-state diradical O 2 can occur either via conversion to singlet oxygen or by one-electron reduction to superoxide. Many enzymes facilitate activation of O 2 by direct fomation of a metal-oxygen coordination complex concomitant with inner sphere electron transfer. The formylglycine generating enzyme (FGE) is an unusual mononuclear copper enzyme that appears to follow a different strategy. Atomic-resolution crystal structures of the precatalytic complex of FGE demonstrate that this enzyme binds O 2 juxtaposed, but not coordinated to the catalytic Cu I . Isostructural complexes that contain Ag I instead of Cu I or nitric oxide instead of O 2 confirm that formation of the initial oxygenated complex of FGE does not depend on redox activity. A stepwise mechanism that decouples binding and activation of O 2 is unprecedented for metal-dependent oxidases, but is reminiscent of flavin-dependent enzymes.
Publisher	Wiley
ISSN/ISBN	1433-7851 ; 1521-3773
edoc-URL	https://edoc.unibas.ch/87391/
Full Text on edoc	Available
Digital Object Identifier DOI	10.1002/anie.202014981
PubMed ID	http://www.ncbi.nlm.nih.gov/pubmed/33245183
ISI-Number	000614352900001
Document type (ISI)	Journal Article

12/05/2024

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