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A Structurally Characterized Mononuclear Copper(II)-Superoxo Complex

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This article is published in Journal of the American Chemical Society.The article was published on 1994-11-01. It has received 72 citations till now. The article focuses on the topics: Copper.

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Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes

TL;DR: A detailed molecular mechanism has been proposed for IPNS based on spectroscopic and crystallographic studies and the role of cosubstrate ascorbate is proposed to reduce the toxic peroxo byproduct to water.
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Copper–Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity

TL;DR: The scope of this review has been limited to well-characterized examples of copper-oxygen species but seeks to provide a thorough picture of the spectroscopic characteristics and reactivity trends of the copper- oxygengen cores discussed.
Journal ArticleDOI

New insights into copper monooxygenases and peptide amidation: structure, mechanism and function.

TL;DR: The structure of the catalytic core of rat PHM at atomic resolution provides a framework for understanding the broad substrate specificity of PHM, identifying residues critical for PHM activity, and proposing mechanisms for the chemical and electron-transfer steps in catalysis.
Journal ArticleDOI

Dioxygen Binds End-On to Mononuclear Copper in a Precatalytic Enzyme Complex

TL;DR: The x-ray crystal structure of the copper-dioxygen complex in the enzyme peptidylglycine-alphahydroxylating monooxygenase is trapped by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen.
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