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

Kipouros, Ioannis; Stańczak, Agnieszka; Culka, Martin; Andris, Erik; Machonkin, Timothy R.; Rulíšek, Lubomír; Solomon, Edward I.

doi:10.1039/d2cc00750a

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

Journal Article · 22 February 2022 · ChemComm

DOI: https://doi.org/10.1039/d2cc00750a · OSTI ID:1870808

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^[2]; Culka, Martin ^[3];

^[3]; Machonkin, Timothy R. ^[4];

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^[5]

Stanford Univ., CA (United States)
Czech Academy of Sciences (CAS), Prague (Czech Republic); Charles Univ., Prague (Czech Republic)
Czech Academy of Sciences (CAS), Prague (Czech Republic)
Whitman College, Walla Walla, WA (United States)
Stanford Univ., CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States)

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. In this study, 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.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1870808

Journal Information:: ChemComm, Journal Name: ChemComm Journal Issue: 24 Vol. 58; ISSN 1359-7345

Publisher:: Royal Society of ChemistryCopyright Statement

Country of Publication:: United States

Language:: English

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