Evidence for H-bonding interactions to the μ-η<sup>2</sup>:η<sup>2</sup>-peroxide of oxy-tyrosinase that activate its coupled binuclear copper site-Reference-Cited by-同舟云学术

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

Published:2022 Issue:24 Volume:58 Page:3913-3916
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Kipouros Ioannis¹^ORCID,Stańczak Agnieszka²³^ORCID,Culka Martin²,Andris Erik²^ORCID,Machonkin Timothy R.⁴,Rulíšek Lubomír²^ORCID,Solomon Edward I.¹⁵^ORCID

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305, USA

2. Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo náměstí 2, 166 10, Praha 6, Czech Republic

3. Faculty of Science, Charles University, Albertov 2038/6, 128 00 Praha 2, Czech Republic

4. Department of Chemistry, Whitman College, Walla Walla, WA 99362, USA

5. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025, USA

Abstract

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.

Funder

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CC/D2CC00750A

Reference32 articles.

1. Copper Active Sites in Biology

2. Oxygen Binding to Tyrosinase from Streptomyces antibioticus Studied by Laser Flash Photolysis

3. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences

4. Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis

5. Structural studies of the hemocyanin active site. 1. Extended x-ray absorption fine structure (EXAFS) analysis

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