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Evidence for H-bonding interactions to the μ-η2:η2-peroxide of oxy-tyrosinase that activate its coupled binuclear copper site
- 1.0556188 - ÚOCHB 2023 RIV GB eng J - Journal Article
Kipouros, I. - Stanczak, Agnieszka - Culka, Martin - Andris, Erik - Machonkin, T. R. - Rulíšek, Lubomír - Solomon, E. I.
Evidence for H-bonding interactions to the μ-η2:η2-peroxide of oxy-tyrosinase that activate its coupled binuclear copper site.
Chemical Communications. Roč. 58, č. 24 (2022), s. 3913-3916. ISSN 1359-7345. E-ISSN 1364-548X
R&D Projects: GA MŠMT(CZ) LTAUSA19148
Research Infrastructure: IT4Innovations - 90070
Institutional support: RVO:61388963
Keywords : absorption fine structure * hemocyanins * spectroscopy * binding
OECD category: Physical chemistry
Impact factor: 4.9, year: 2022
Method of publishing: Limited access
https://doi.org/10.1039/D2CC00750A
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.
Permanent Link: http://hdl.handle.net/11104/0331028
Number of the records: 1