| Literature DB >> 35237779 |
Ioannis Kipouros1, Agnieszka Stańczak2,3, Martin Culka2, Erik Andris2, Timothy R Machonkin4, Lubomír Rulíšek2, Edward I Solomon1,5.
Abstract
The factors that control the diverse reactivity of the μ-η2:η2-peroxo dicopper(II) oxy-intermediates in the coupled binuclear copper proteins remain elusive. Here, spectroscopic and computational methods reveal H-bonding interactions between active-site waters and the μ-η2:η2-peroxide of oxy-tyrosinase, and define their effects on the Cu(II)2O2 electronic structure and O2 activation.Entities:
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Year: 2022 PMID: 35237779 PMCID: PMC8966618 DOI: 10.1039/d2cc00750a
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222