Copper Bioinorganic Chemistry: From Health to Bioinspired Catalysis

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Copper Bioinorganic Chemistry: From Health to Bioinspired Catalysis
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Preface
	References
Contents
1. Ligands as a Tool to Tune the Toxicity of Cu on Bacteria: from Boosting to Silencing
	I. Introduction
	II. Copper, a Biocidal Compound
	III. Copper Homeostasis Systems in Bacteria
	IV. Copper Toxicity: A Phenomenon Dependent on the Bioavailability of Copper and on Bacteria
	V. Specificity of Copper Chemistry
		A. Cu Coordination Chemistry
		B. Cu Reactivity: The Case of ROS Production
		C. In Vivo Complexation of Cu
	VI. Mechanisms of Cu Toxicity: Macromolecules Targeted by Copper
		A. Membranes
		B. DNA
		C. Proteins
	VII. Chemistry of Copper Complexes
		A. Reactivity of Cu Complexes
		B. Stability of the Cu-L Complex
		C. Kinetics of the Cu-L Complex
		D. Redox Potential
	VIII. Impact of Ligands on the Biological Activity of Copper
		A. Localization
		B. Presence in Biology of Potentially Competing Ligands for Cu(II)
		C. Presence in Biology of Potentially Competing Ligands for Cu(I)
		D. Reactivity of Cu-L in Bacteria
		E. Reactivity of the Free Ligand in Bacteria
	IX. Copper Complexes as Antimicrobial Agents, a Non-Exhaustive List
		A. Dithiocarbamates Compounds
		B. 8-Hydroxychinoline (8-HQ) Compounds
		C. Phenanthrolines
		D. Pyrithione
		E. Bis-Thiosemicarbazones (atsm, gtsm)
	X. Peptides-Based Cu-Chelators
	XI. Recent Advances Toward the Future Use of Copper in Medicine
	XII. References
2. Transition State Analogue Molecules as Mechanistic Tools and Inhibitors for Tyrosinase
	I. Introduction
	II. Biological Functions of Melanins
		A. Melanin as Color Pigment
		B. Melanin as a Defensive Barrier
	III. Tyrosinase
		A. Structures of the Tyrosinase Active Sites
		B. Catalytic Mechanism of Tyrosinase
		C. Tyrosinase-Related Proteins TRP1 and TRP2
	IV. Dysfunction in Tyrosinase Activity
		A. Pathologies Linked to TYR Dysfunction
		B. Skin Whitening
	V. Tyrosinase Inhibition
		A. Variation in TYR Sources
		B. Transition-State Analogue (TSA) Inhibitors
			1. L-Mimosine
			2. Kojic acid and derivatives
			3. Tropolone and derivatives
			4. HOPNO inhibitor
			5. HOPNO derivatives
	VI. Conclusions
	Acknowledgment
	VII. References
3. Modeling Tyrosinase Activity Using m-Xylyl-Based Ligands: Ring Hydroxylation, Reactivity, and Theoretical Investigation
	I. Introduction
		A. General Considerations
		B. Scope of the Review
	II. Dicopper Proteins — Brief Overview
		A. Hemocyanins
		B. Tyrosinases
		C. Catechol Oxidase
	III. Three Cu2O2 Core Structures
	IV. Biomimetic Studies on Tyrosinase
		A. Intramolecular m-Xylyl and Aromatic Ring Hydroxylation
		B. Intramolecular m-Xylyl and Aromatic Ring Hydroxylation
		C. Ring Hydroxylation Reactions with Non-m-Xylyl-Based Ligands
		D. Oxidation of External Substrates by Dicopper Systems
	V. Theoretical Studies on Tyrosinase Models
		A. Frontier Molecular Orbitals of the Cu2O2 Cores
			1. μ-η2:η2-Peroxo-dicopper(II): {CuII2(μ-η2:η2 O2)}2+{Cu2PS}
			2. Trans-μ-1,2-peroxo-dicopper(II): {CuII2(μ-η1:η1-O2)}2+ {Cu2PE}
			3. Bis(μ-oxido)dicopper(III): {CuIII2(μ-O)2}2+ {Cu2O2}
		B. Interconversion Between {Cu2PS} and {Cu2O2} Cores: A Torture Track for Computations
		C. {Cu2PS}, {Cu2PE}, and {Cu2O2} Motifs in C−H Oxidation: DFT Studies
			1. Aromatic C−H hydroxylation via {Cu2PS} motifs
			2. Aromatic C−H hydroxylation via {Cu2O2}
			3. Aromatic C−H hydroxylation via {Cu2PE}
	VI. Conclusions
	VII. References
4. Monooxygenation of Phenols by Small-molecule Models of Tyrosinase: Correlations Between Structure and Catalytic Activity
	I. Introduction
	II. Model Systems of Tyrosinase
		A. Model Systems Performing Ligand Hydroxylation
		B. Model Systems Exhibiting Reactivity Toward External Substrates
	III. Catalytic Tyrosinase Models with Bidentate Ligands
		A. Mechanistic Cycle of the Tyrosinase-like Monooxygenation of External Substrates
		B. Substitution of Pyridine in the Lpy1 Ligand by N-Heterocycles
		C. Substitution of Imine in the Lpy1 Ligand by N-heterocycles: Symmetric Bidentate Ligands
		D. Hybrid Ligands Composed of Different N-Heterocycles
		E. Steric Influence of Substituents on the Supporting Ligands
		F. Variation of Substrates: Electronic and Steric Factors
	IV. Summary
	V. Acknowledgment
	VI. References
5. Electrochemistry and Spectroelectrochemistry of Copper-Oxygen-Relevant Species
	I. Introduction
	II. Electrochemistry of Peroxide and Superoxide Copper–Oxygen Species
	III. Electrochemistry of Copper(II) Hydroxo, Alkoxo, Carboxylato, and Oxo Precusors
	IV. Electrochemistry of Copper Hydroperoxide and Alkoxoperoxide Species
	V. Electrochemistry of Copper(II)-Phenoxide Species
	VI. Electrochemistry of Nitroso and Sulfide Analogues of Copper–Oxygen Complexes
	VII. Summary
	VIII. References
6. Inorganic Models of Lytic Polysaccharide Monooxygenases
	I. Introduction
	II. Lytic Polysaccharide Monooxygenases
	III. Copper Complexes as Hydrolase Mimics
		A. Polysaccharide Hydrolysis
		B. Copper Complexes
	IV. Copper Complexes as LPMO Mimics
		A. Copper(II)/Bis(Benzimidazolyl)Amine System
		B. Copper(III)/Bis(Carboxamido)Pyridine System
		C. Copper(II)/Copper(I)/(Pyridyl,Imidazolyl)Amine System
		D. Copper(II)/(Pyridyl)Diazepane Complexes
		E. Copper(II)/Bis(Imidazolyl)Amine System
		F. Copper(II)/Bis(Picolyl)Amine System
	V. Concluding Remarks
	VI. References
7. Structure and Function of Cu–Peptoid Complexes
	I. Introduction
		A. Peptoid Synthesis
		B. Secondary Structure of Peptoid Oligomers
	II. Structural Aspects of Cu(II)–Peptoid Complexes
		A. Structural Design of Cu(II)–Peptoid Complexes
		B. Choice of the Metal-Binding Ligands
		C. Characterization of Cu(II)–Peptoid Complexes
			1. Evaluation of Cu(II) binding and synthesis of Cu(II)–peptoid complexes
			2. Determining the association constants and evaluating the selectivity of the peptoid chelators to Cu(II)
			3. Structure and coordination sphere of Cu centers within Cu(II)–peptoid complexes
	III. Effect of Cu(II) Binding on the Structure of Peptoid
		A. Cu(II) Binding as a New Approach for Peptoid Folding
		B. Cu(II)-Mediated Peptoids Self-Assembly
	IV. From Structure to Function: Cu-Binding Peptoids and Cu–Peptoids as Functional Materials
		A. Selective Recognition of Small Molecules by Self-Assembled Cu(II)–Peptoids
		B. Selective Recognition of Cu(II) by Peptoids Toward Drug Design
		C. Positive Allosteric Cooperativity in Metal Binding to Cu(II)–Peptoid
		D. Cu(II)–Peptoid Complexes as Versatile, Efficient, and Selective Bio-Inspired Catalysts
	V. Summary
	VI. References
Index