In:
Angewandte Chemie, Wiley, Vol. 133, No. 36 ( 2021-09), p. 19989-19995
Abstract:
Coupled dinuclear copper oxygen cores (Cu 2 O 2 ) featured in type III copper proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for O 2 transport and substrate oxidation in many organisms. μ ‐1,2‐ cis peroxido dicopper cores ( C P ) have been proposed as key structures in the early stages of O 2 binding in these proteins; their reversible isomerization to other Cu 2 O 2 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 C P cores in biological and synthetic systems, the properties and reactivity of C P Cu 2 O 2 species remain largely unexplored. Herein, we report the reversible interconversion of μ ‐1,2‐ trans peroxido ( T P ) and C P dicopper cores. Ca II mediates this process by reversible binding at the Cu 2 O 2 core, highlighting the unique capability for metal‐ion binding events to stabilize novel reactive fragments and control O 2 activation in biomimetic systems.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v133.36
DOI:
10.1002/ange.202105421
Language:
English
Publisher:
Wiley
Publication Date:
2021
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