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Calcium‐Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores
dc.contributor.authorVargo, Natasha P.
dc.contributor.authorHarland, Jill B.
dc.contributor.authorMusselman, Bradley W.
dc.contributor.authorLehnert, Nicolai
dc.contributor.authorErtem, Mehmed Z.
dc.contributor.authorRobinson, Jerome R.
dc.date.accessioned2021-09-08T14:35:12Z
dc.date.available2022-10-08 10:35:10en
dc.date.available2021-09-08T14:35:12Z
dc.date.issued2021-09-01
dc.identifier.citationVargo, Natasha P.; Harland, Jill B.; Musselman, Bradley W.; Lehnert, Nicolai; Ertem, Mehmed Z.; Robinson, Jerome R. (2021). "Calcium‐Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores." Angewandte Chemie International Edition 60(36): 19836-19842.
dc.identifier.issn1433-7851
dc.identifier.issn1521-3773
dc.identifier.urihttps://hdl.handle.net/2027.42/169279
dc.description.abstractCoupled dinuclear copper oxygen cores (Cu2O2) featured in type III copper proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for O2 transport and substrate oxidation in many organisms. μ‐1,2‐cis peroxido dicopper cores (CP) have been proposed as key structures in the early stages of O2 binding in these proteins; their reversible isomerization to other Cu2O2 cores are directly relevant to enzyme function. Despite the relevance of such species to type III copper proteins and the broader interest in the properties and reactivity of bimetallic CP cores in biological and synthetic systems, the properties and reactivity of CP Cu2O2 species remain largely unexplored. Herein, we report the reversible interconversion of μ‐1,2‐trans peroxido (TP) and CP dicopper cores. CaII mediates this process by reversible binding at the Cu2O2 core, highlighting the unique capability for metal‐ion binding events to stabilize novel reactive fragments and control O2 activation in biomimetic systems.Calcium‐ion binding mediates the reversible interconversion of the prototypical trans‐peroxido Cu2O2 core (TP) to the rare and biologically relevant cis‐peroxido Cu2O2 core (CP). This provides new opportunities to stabilize novel reactive fragments and control O2 activation in biomimetic systems.
dc.publisherElsevier
dc.publisherWiley Periodicals, Inc.
dc.subject.othercalcium
dc.subject.othercopper
dc.subject.otherheterometallic complexes
dc.subject.otherperoxides
dc.subject.otherbioinorganic chemistry
dc.titleCalcium‐Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores
dc.typeArticle
dc.rights.robotsIndexNoFollow
dc.subject.hlbsecondlevelChemistry
dc.subject.hlbtoplevelScience
dc.description.peerreviewedPeer Reviewed
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/169279/1/anie202105421-sup-0001-misc_information.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/169279/2/anie202105421_am.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/169279/3/anie202105421.pdf
dc.identifier.doi10.1002/anie.202105421
dc.identifier.sourceAngewandte Chemie International Edition
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