Evidence for H-bonding interactions to the μ-η2:η2-peroxide of oxy-tyrosinase that activate its coupled binuclear copper site.

Autor: Kipouros, Ioannis, Stańczak, Agnieszka, Culka, Martin, Andris, Erik, Machonkin, Timothy R., Rulíšek, Lubomír, Solomon, Edward I.
Předmět:
Zdroj: Chemical Communications; 3/25/2022, Vol. 58 Issue 24, p3913-3916, 4p
Abstrakt: The factors that control the diverse reactivity of the μ-η22-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-η22-peroxide of oxy-tyrosinase, and define their effects on the Cu(II)2O2 electronic structure and O2 activation. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index