TRANSITION METALS IN BIOCHEMISTRY
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 LIST OF ABBREVIATIONS 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 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 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 ?-?2:?2-PEROXO-DICOPPER(II); {CUII 2(?-?2:?2 O2)}2+ {CU2PS} 2 TRANS-?-1,2-PEROXO-DICOPPER(II): {CUII 2(?-?1:?1-O2)}2+ {CU2PE} 3 BIS(?-OXIDO)DICOPPER(III): {CUIII 2(?-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} 4 MONOOXYGENATION OF PHENOLS BY SMALL-MOLECULE MODELS OF TYROSINASE: CORRELATIONS BETWEEN STRUCTURE AND CATALYTIC ACTIVITY 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 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 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 7 STRUCTURE AND FUNCTION OF CU–PEPTOID COMPLEXES 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