Intramolecular Phenolic H-Atom Abstraction by a N3ArOH Ligand-Supported (μ-η2:η2-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase-Reference-Cited by-同舟云学术

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Intramolecular Phenolic H-Atom Abstraction by a N₃ArOH Ligand-Supported (μ-η²:η²-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase

Published:2024-05-22 Issue:22 Volume:146 Page:14942-14947
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Panda Sanjib¹^ORCID,Phan Hai¹^ORCID,Dunietz Eleanor M.²^ORCID,Brueggemeyer Magdalene T.²^ORCID,Hota Pradip Kumar¹^ORCID,Siegler Maxime A.¹^ORCID,Jose Anex²^ORCID,Bhadra Mayukh¹^ORCID,Solomon Edward I.²³^ORCID,Karlin Kenneth D.¹^ORCID

Affiliation:

1. Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218, United States

2. Department of Chemistry, Stanford University, Stanford, California 94305, United States

3. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States

Funder

National Institutes of Health

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.4c04402

Reference50 articles.

1. Copper Active Sites in Biology

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

3. Recent Structural Work on the Oxygen Transport Protein Hemocyanin

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

5. The Crystal Structure of Catechol Oxidase: New Insight into the Function of Type-3 Copper Proteins

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