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First Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity

https://doi.org/10.1016/j.jmb.2010.10.048
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Discriminating between homodimeric and monomeric proteins in the crystalline state
inferredcites →https://doi.org/10.1002/1097-0134(20001001)41:1<47::aid-prot80>3.3.co;2-#openalex-snapshot
Discriminating between homodimeric and monomeric proteins in the crystalline state
inferredcites →https://doi.org/10.1002/anie.200601255openalex-snapshot
The First Crystal Structure of Tyrosinase: All Questions Answered?
inferredcites →https://doi.org/10.1002/chin.200741276openalex-snapshot
Monooxygenase Activity of Type 3 Copper Proteins
inferredcites →https://doi.org/10.1002/pro.5560020411openalex-snapshot
Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation
inferredcites →https://doi.org/10.1006/jmbi.1998.1647openalex-snapshot
Crystal structure of a functional unit from Octopus hemocyanin
inferredcites →https://doi.org/10.1007/s00018-005-5054-yopenalex-snapshot
Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future
inferredcites →https://doi.org/10.1007/s007750050370openalex-snapshot
Inhibition of the catecholase activity of biomimetic dinuclear copper complexes by kojic acid
inferredcites →https://doi.org/10.1016/0022-2836(87)90658-9openalex-snapshot
Rat submaxillary gland serine protease, tonin
inferredcites →https://doi.org/10.1016/j.bbapap.2007.04.011openalex-snapshot
The inhibition kinetics and thermodynamic changes of tyrosinase via the zinc ion
inferredcites →https://doi.org/10.1016/j.enzmictec.2010.08.008openalex-snapshot
Directed evolution of tyrosinase for enhanced monophenolase/diphenolase activity ratio
inferredcites →https://doi.org/10.1016/j.gene.2007.02.051openalex-snapshot
Similar enzyme activation and catalysis in hemocyanins and tyrosinases
inferredcites →https://doi.org/10.1016/j.jbiotec.2007.05.018openalex-snapshot
Comparison of the characteristics of fungal and plant tyrosinases
inferredcites →https://doi.org/10.1016/j.str.2009.03.005openalex-snapshot
Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy
inferredcites →https://doi.org/10.1016/j.syapm.2005.07.012openalex-snapshot
Bacterial tyrosinases
inferredcites →https://doi.org/10.1016/j.tibtech.2003.10.006openalex-snapshot
Oxidizing enzymes as biocatalysts
inferredcites →https://doi.org/10.1016/s0014-5793(00)01609-4openalex-snapshot
EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus
inferredcites →https://doi.org/10.1016/s0924-2244(00)89054-8openalex-snapshot
The biochemistry and control of enzymatic browning
inferredcites →https://doi.org/10.1016/s0959-440x(99)00029-9openalex-snapshot
Catechol oxidase — structure and activity
inferredcites →https://doi.org/10.1016/s0968-0004(00)01602-9openalex-snapshot
Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
inferredcites →https://doi.org/10.1016/s1357-2725(03)00234-6openalex-snapshot
Tyrosinase kinetics: discrimination between two models to explain the oxidation mechanism of monophenol and diphenol substrates
inferredcites →https://doi.org/10.1021/ar6000395openalex-snapshot
Monooxygenase Activity of Type 3 Copper Proteins
inferredcites →https://doi.org/10.1021/ar990019aopenalex-snapshot
The Crystal Structure of Catechol Oxidase: New Insight into the Function of Type-3 Copper Proteins
inferredcites →https://doi.org/10.1021/bi00716a007openalex-snapshot
Monomer-dimer equilibriums of yeast hexokinase during reacting enzyme sedimentation
inferredcites →https://doi.org/10.1021/bi011535nopenalex-snapshot
Identification of Active Site Residues Involved in Metal Cofactor Binding and Stereospecific Substrate Recognition in Mammalian Tyrosinase. Implications to the Catalytic Cycle
inferredcites →https://doi.org/10.1021/cr00027a009openalex-snapshot
Recent Structural Work on the Oxygen Transport Protein Hemocyanin
inferredcites →https://doi.org/10.1021/jf902939qopenalex-snapshot
Cloning, Sequencing, Purification, and Crystal Structure of Grenache (Vitis vinifera) Polyphenol Oxidase
inferredcites →https://doi.org/10.1038/309023a0openalex-snapshot
3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin
inferredcites →https://doi.org/10.1038/4193openalex-snapshot
Crystal structure of a plant catechol oxidase containing a dicopper center
inferredcites →https://doi.org/10.1073/pnas.0906095106openalex-snapshot
Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes
inferredcites →https://doi.org/10.1074/jbc.273.40.25889openalex-snapshot
Tarantula Hemocyanin Shows Phenoloxidase Activity
inferredcites →https://doi.org/10.1074/jbc.m509785200openalex-snapshot
Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis
inferredcites →https://doi.org/10.1074/jbc.m805540200openalex-snapshot
NS3 Helicase from the Hepatitis C Virus Can Function as a Monomer or Oligomer Depending on Enzyme and Substrate Concentrations
inferredcites →https://doi.org/10.1074/jbc.r100010200openalex-snapshot
Hemocyanins and Invertebrate Evolution
inferredcites →https://doi.org/10.1107/97809553602060000865openalex-snapshot
PHENIX: a comprehensive Python-based system for macromolecular structure solution
inferredcites →https://doi.org/10.1107/s0108767304097648openalex-snapshot
Direct incorporation of experimental phase information in model refinement
inferredcites →https://doi.org/10.1107/s0907444904019079openalex-snapshot
Direct incorporation of experimental phase information in model refinement
inferredcites →https://doi.org/10.1107/s0907444904019158openalex-snapshot
Coot : model-building tools for molecular graphics
inferredcites →https://doi.org/10.1107/s0907444906045975openalex-snapshot
Solving structures of protein complexes by molecular replacement with Phaser
inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot
PHENIX : a comprehensive Python-based system for macromolecular structure solution
inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
inferredcites →https://doi.org/10.1107/s0907444998003254openalex-snapshot
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
inferredcites →https://doi.org/10.1107/s1744309110031520openalex-snapshot
Crystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase fromBacillus megaterium
inferredcites →https://doi.org/10.1111/j.1755-148x.2009.00636.xopenalex-snapshot
New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins
inferredcites →https://doi.org/10.1159/000233506openalex-snapshot
Isolation, Cloning and Characterization of a Tyrosinase with Improved Activity in Organic Solvents from Bacillus megaterium
inferredcites →https://doi.org/10.3390/ijms10062440openalex-snapshot
An Updated Review of Tyrosinase Inhibitors
inferredcites →https://doi.org/10.3390/molecules14010257openalex-snapshot
Molecular Docking Studies and Anti-Tyrosinase Activity of Thai Mango Seed Kernel Extract

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1002/ange.201704616openalex-snapshot
Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis
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Copper–Oxygen Dynamics in the Tyrosinase Mechanism
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inferred← citeshttps://doi.org/10.1002/anie.201506994openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/anie.201704616openalex-snapshot
Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis
inferred← citeshttps://doi.org/10.1002/anie.202004733openalex-snapshot
Copper–Oxygen Dynamics in the Tyrosinase Mechanism
inferred← citeshttps://doi.org/10.1002/anie.202416967openalex-snapshot
Imidazolate‐Stabilized Cu(III): Dioxygen to Oxides at Type 3 Copper Sites
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Identification of an Activity Selector for the Nitroso‐Forming Activity in Bacterial Type‐III Copper Enzymes
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Circular permutation of a bacterial tyrosinase enables efficient polyphenol‐specific oxidation and quantitative preparation of orobol
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Interactions of Phenylalanine Derivatives with Human Tyrosinase: Lessons from Experimental and Theoretical Studies
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Radical Control in Binuclear Copper Enzymes: Structure, Dioxygen Activation, and Mechanisms
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The Versatile Binding Mode of Transition‐State Analogue Inhibitors of Tyrosinase towards Dicopper(II) Model Complexes: Experimental and Theoretical Investigations
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Ditopic Chelators of Dicopper Centers for Enhanced Tyrosinases Inhibition
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Catalytic Models of Tyrosinase: Reactivity Differences between Systems Based on Mono‐ and Binucleating Ligands
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Deuterium isotope effect on the suicide inactivation of tyrosinase in its action on o‐diphenols
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Heterologous expression of tyrosinase (MelC2) from Streptomyces avermitilis MA4680 in E. coli and its application for ortho-hydroxylation of resveratrol to produce piceatannol
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Computational studies of tyrosinase inhibitors
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Mechanistic studies of the tyrosinase-catalyzed oxidative cyclocondensation of 2-aminophenol to 2-aminophenoxazin-3-one
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The high-resolution crystal structure of lobster hemocyanin shows its enzymatic capability as a phenoloxidase
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Effects of dietary copper on elemental balance, plasma minerals and serum biochemical parameters of growing-furring male mink ( Mustela vison )
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Molecular optimization of autotransporter-based tyrosinase surface display
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Catalytic oxidation of o-aminophenols and aromatic amines by mushroom tyrosinase
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Extracellular tyrosinase from the fungus Trichoderma reesei shows product inhibition and different inhibition mechanism from the intracellular tyrosinase from Agaricus bisporus
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Kinetic characterisation of o-aminophenols and aromatic o-diamines as suicide substrates of tyrosinase
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Isobenzofuran-1(3H)-ones as new tyrosinase inhibitors: Biological activity and interaction studies by molecular docking and NMR
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Hydroxylation of p-substituted phenols by tyrosinase: Further insight into the mechanism of tyrosinase activity
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Kinetic studies, molecular docking, and antioxidant activity of novel 1,3-diphenyl pyrazole-thiosemicarbazone with anti-tyrosinase and anti-melanogenesis properties
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Tyrosinase: The four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation
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Structure–activity relationships of the thujaplicins for inhibition of human tyrosinase
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Rational design, synthesis and structure–activity relationships of 4-alkoxy- and 4-acyloxy-phenylethylenethiosemicarbazone analogues as novel tyrosinase inhibitors
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Structural requirement of phenylthiourea analogs for their inhibitory activity of melanogenesis and tyrosinase
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Design, synthesis and molecular simulation studies of dihydrostilbene derivatives as potent tyrosinase inhibitors
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Design, synthesis, molecular docking and ADME of novel phenylalanine derivatives as mushroom tyrosinase inhibitors
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Effects of known phenoloxidase inhibitors on hemocyanin-derived phenoloxidase from Limulus polyphemus
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Small-molecule models of tyrosinase: From ligand hydroxylation to catalytic monooxygenation of external substrates
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Coordination-site engineering in mononuclear non-heme metalloenzymes: From evolutionary motifs to programmable metal centers
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Formation of disulfide bonds in insect prophenoloxidase enhances immunity through improving enzyme activity and stability
inferred← citeshttps://doi.org/10.1016/j.dci.2014.01.021openalex-snapshot
Diverse immune functions of hemocyanins
inferred← citeshttps://doi.org/10.1016/j.drudis.2023.103843openalex-snapshot
Valorization of biomass polyphenols as potential tyrosinase inhibitors
inferred← citeshttps://doi.org/10.1016/j.dyepig.2025.112923openalex-snapshot
Design and application of HBT based probes: achieving color changing function and drug release through cascade reaction and photoactivation
inferred← citeshttps://doi.org/10.1016/j.ejmech.2015.02.013openalex-snapshot
Structure-based modification of 3-/4-aminoacetophenones giving a profound change of activity on tyrosinase: From potent activators to highly efficient inhibitors
inferred← citeshttps://doi.org/10.1016/j.ejmech.2017.08.033openalex-snapshot
Study on the design, synthesis and structure-activity relationships of new thiosemicarbazone compounds as tyrosinase inhibitors
inferred← citeshttps://doi.org/10.1016/j.ejmech.2019.111892openalex-snapshot
Tyrosinase inhibitors as potential antibacterial agents
inferred← citeshttps://doi.org/10.1016/j.ejmech.2022.114525openalex-snapshot
Azole inhibitors of mushroom and human tyrosinases: Current advances and prospects of drug development for melanogenic dermatological disorders
inferred← citeshttps://doi.org/10.1016/j.ejmech.2023.115090openalex-snapshot
Exploiting HOPNO-dicopper center interaction to development of inhibitors for human tyrosinase
inferred← citeshttps://doi.org/10.1016/j.ejmech.2023.115771openalex-snapshot
Computational methods to analyze and predict the binding mode of inhibitors targeting both human and mushroom tyrosinase
inferred← citeshttps://doi.org/10.1016/j.foodchem.2013.02.072openalex-snapshot
Hemocyanin-derived phenoloxidase activity: A contributing factor to hyperpigmentation in Nephrops norvegicus
inferred← citeshttps://doi.org/10.1016/j.foodchem.2016.08.027openalex-snapshot
Application of mesoporous silica materials for the immobilization of polyphenol oxidase
inferred← citeshttps://doi.org/10.1016/j.foodchem.2019.125310openalex-snapshot
Hydroxyphenyl thiosemicarbazones as inhibitors of mushroom tyrosinase and antibrowning agents
inferred← citeshttps://doi.org/10.1016/j.foodchem.2021.131848openalex-snapshot
Improved yield of theaflavin-3,3ʹ-digallate from Bacillus megaterium tyrosinase via directed evolution
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.132730openalex-snapshot
Design and synthesis of novel stilbene-hydroxypyridinone hybrids as tyrosinase inhibitors and their application in the anti-browning of freshly-cut apples
inferred← citeshttps://doi.org/10.1016/j.foodres.2016.06.018openalex-snapshot
Modulating the gel properties of soy glycinin by crosslinking with tyrosinase
inferred← citeshttps://doi.org/10.1016/j.foodres.2017.07.034openalex-snapshot
Oil-in-water emulsions stabilized by tyrosinase-crosslinked potato protein
inferred← citeshttps://doi.org/10.1016/j.foodres.2018.08.050openalex-snapshot
Tyrosinase-crosslinked pea protein emulsions: Impact of zein incorporation
inferred← citeshttps://doi.org/10.1016/j.ica.2017.04.041openalex-snapshot
What causes the different functionality in type-III-copper enzymes? A state of the art perspective
inferred← citeshttps://doi.org/10.1016/j.ica.2017.11.031openalex-snapshot
Are glutamate and asparagine necessary for tyrosinase activity of type-3 copper proteins?
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2011.11.010openalex-snapshot
Homology models of four Agaricus bisporus tyrosinases
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2011.12.035openalex-snapshot
Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.02.042openalex-snapshot
Biochemical characterization of a tyrosinase from Bacillus aryabhattai and its application
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.128313openalex-snapshot
Highly efficient site-specific protein modification using tyrosinase from Streptomyces avermitilis: Structural insight
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.141557openalex-snapshot
Unveiling an indole derivative YM818 as a novel tyrosinase inhibitor with anti-melanogenic and anti-melanin transfer effects
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.150551openalex-snapshot
Distal design improves thermostability and enzyme activity of type III tyrosinase from Nitrosospira
inferred← citeshttps://doi.org/10.1016/j.isci.2025.111771openalex-snapshot
Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2017.11.004openalex-snapshot
Isolation and characterization of a novel tyrosinase produced by Sahara soil actinobacteria and immobilization on nylon nanofiber membranes
inferred← citeshttps://doi.org/10.1016/j.jid.2018.01.019openalex-snapshot
Inhibition of Human Tyrosinase Requires Molecular Motifs Distinctively Different from Mushroom Tyrosinase
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.12.006openalex-snapshot
Experimental and bioinformatic investigation of the proteolytic degradation of the C-terminal domain of a fungal tyrosinase
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2015.07.001openalex-snapshot
Metal coordination and tyrosinase inhibition studies with Kojic-βAla-Kojic
inferred← citeshttps://doi.org/10.1016/j.jmb.2013.01.009openalex-snapshot
Catalytic Metal Ion Rearrangements Underline Promiscuity and Evolvability of a Metalloenzyme
inferred← citeshttps://doi.org/10.1016/j.jorganchem.2017.05.009openalex-snapshot
Aerobic oxidative coupling of alcohols and amines towards imine formation by a dicopper(I,I) catalyst
inferred← citeshttps://doi.org/10.1016/j.jscs.2022.101489openalex-snapshot
Rotenoids and coumaronochromonoids from Boerhavia erecta and their biological activities: In vitro and in silico studies
inferred← citeshttps://doi.org/10.1016/j.jsps.2023.04.028openalex-snapshot
A detailed biochemical characterization, toxicological assessment and molecular docking studies of Launaea fragilis: An important medicinal xero-halophyte
inferred← citeshttps://doi.org/10.1016/j.jsps.2024.102090openalex-snapshot
A novel source of biologically active compounds – The leaves of Serbian herbaceous peonies
inferred← citeshttps://doi.org/10.1016/j.molcatb.2011.11.001openalex-snapshot
Unravelling the suicide inactivation of tyrosinase: A discrimination between mechanisms
inferred← citeshttps://doi.org/10.1016/j.molcatb.2013.02.003openalex-snapshot
Catalysis and inactivation of tyrosinase in its action on o-diphenols, o-aminophenols and o-phenylendiamines: Potential use in industrial applications
inferred← citeshttps://doi.org/10.1016/j.molcatb.2015.12.008openalex-snapshot
Further insight into the pH effect on the catalysis of mushroom tyrosinase
inferred← citeshttps://doi.org/10.1016/j.molliq.2021.115651openalex-snapshot
Carbazole derivatives: Synthesis, spectroscopic characterization, antioxidant activity, molecular docking study, and the quantum chemical calculations
inferred← citeshttps://doi.org/10.1016/j.molstruc.2020.128295openalex-snapshot
Experimental and theoretical charge density analysis of skin whitening agent kojic acid
inferred← citeshttps://doi.org/10.1016/j.molstruc.2021.130940openalex-snapshot
DFT, Molecular Docking and Drug-likeness Analysis: Acrylate molecule bearing perfluorinated pendant unit
inferred← citeshttps://doi.org/10.1016/j.molstruc.2022.134018openalex-snapshot
Design, synthesis, in vitro, and in silico studies of novel benzylidene 6-methoxy-1-tetralone linked to benzyloxy and benzyl -1,2,3- triazole rings as potential tyrosinase inhibitors
inferred← citeshttps://doi.org/10.1016/j.molstruc.2025.142868openalex-snapshot
Design, synthesis, crystal structures, characterization and molecular docking analysis of six lithium(I)-based metal organic frameworks with antibacterial activities
inferred← citeshttps://doi.org/10.1016/j.molstruc.2025.144100openalex-snapshot
Bio-evaluation of the p-(arylsulfonyl)benzaldehydes against tyrosinase, lipoxygenase-15 (LOX-15) and inducible nitric oxide synthase (iNOS)
inferred← citeshttps://doi.org/10.1016/j.molstruc.2026.147800openalex-snapshot
Naphthyl-Based Thiosemicarbazide, 1,2,4-Triazole, and 1,3,4-Oxadiazole Derivatives: Synthesis, Tyrosinase and α-Glucosidase Inhibition, and Molecular Modeling Studies
inferred← citeshttps://doi.org/10.1016/j.nbt.2011.05.007openalex-snapshot
Bacterial tyrosinases: old enzymes with new relevance to biotechnology
inferred← citeshttps://doi.org/10.1016/j.nexres.2025.100182openalex-snapshot
In vitro, in silico anti-tyrosinase and anti-inflammatory activity elucidation of chrysophanol isolated from Platycladus orientalis (L.) Franco
inferred← citeshttps://doi.org/10.1016/j.nxnano.2026.100452openalex-snapshot
Tyrosinase inhibitors: Molecular mechanisms, therapeutic potentials, and translational applications in dermatology and beyond
inferred← citeshttps://doi.org/10.1016/j.phytochem.2012.05.022openalex-snapshot
Purification and spectroscopic studies on catechol oxidase from lemon balm (Melissa officinalis)
inferred← citeshttps://doi.org/10.1016/j.procbio.2012.08.018openalex-snapshot
Bacterial tyrosinases and their applications
inferred← citeshttps://doi.org/10.1016/j.procbio.2013.02.030openalex-snapshot
Computational prediction for the protein interactions of tyrosinase: Protein experimental interactome MAP
inferred← citeshttps://doi.org/10.1016/j.rechem.2026.103588openalex-snapshot
Synthesis, characterization, and computational investigation of a novel quercetin-derived chromene-4-thione
inferred← citeshttps://doi.org/10.1016/j.saa.2013.01.058openalex-snapshot
Molecular inhibitory mechanism of tricin on tyrosinase
inferred← citeshttps://doi.org/10.1016/j.saa.2021.119669openalex-snapshot
5-Substituted isatin thiosemicarbazones as inhibitors of tyrosinase: Insights of substituent effects
inferred← citeshttps://doi.org/10.1016/j.saa.2022.121590openalex-snapshot
Modulation of the lipophilicity and molecular size of thiosemicarbazone inhibitors to regulate tyrosinase activity
inferred← citeshttps://doi.org/10.1016/j.soilbio.2025.109903openalex-snapshot
Bacterial tyrosinases as extracellular sources of quinone-based electron shuttles in soil
inferred← citeshttps://doi.org/10.1016/j.tifs.2017.12.011openalex-snapshot
Crosslinking of food proteins mediated by oxidative enzymes – A review
inferred← citeshttps://doi.org/10.1016/j.tifs.2020.06.014openalex-snapshot
Applications of oxidases in modification of food molecules and colloidal systems: Laccase, peroxidase and tyrosinase
inferred← citeshttps://doi.org/10.1021/acs.accounts.3c00336openalex-snapshot
A Specific Guide for Metalloenzyme Designers: Introduction and Evolution of Metal-Coordination Spheres Embedded in Protein Environments
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00635openalex-snapshot
Activation Mechanism of the Streptomyces Tyrosinase Assisted by the Caddie Protein
inferred← citeshttps://doi.org/10.1021/acs.bioconjchem.5c00468openalex-snapshot
Enhancing Enzymatic Bioconjugation Efficiency via Computer-Based Installation of a Substrate Recruitment Domain
inferred← citeshttps://doi.org/10.1021/acs.chemrev.8b00201openalex-snapshot
Targeting Metalloenzymes for Therapeutic Intervention
inferred← citeshttps://doi.org/10.1021/acs.est.2c03770openalex-snapshot
The Novel Role of Tyrosinase Enzymes in the Storage of Globally Significant Amounts of Carbon in Wetland Ecosystems
inferred← citeshttps://doi.org/10.1021/acs.est.3c02910openalex-snapshot
Biochemical Investigations of Five Recombinantly Expressed Tyrosinases Reveal Two Novel Mechanisms Impacting Carbon Storage in Wetland Ecosystems
inferred← citeshttps://doi.org/10.1021/acs.inorgchem.2c01898openalex-snapshot
Symmetry-Adapted Synthesis of Dicopper Oxidases with Divergent Dioxygen Reactivity
inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00484openalex-snapshot
Ensemble-Based Virtual Screening Led to the Discovery of New Classes of Potent Tyrosinase Inhibitors
inferred← citeshttps://doi.org/10.1021/acs.jpca.0c00004openalex-snapshot
Electron Paramagnetic Resonance Characteristics and Crystal Structure of a Tutton Salt Analogue: Copper-Doped Cadmium Creatininium Sulfate
inferred← citeshttps://doi.org/10.1021/acs.jpca.4c06133openalex-snapshot
Cu(II) Stability and UV-Induced Electron Transfer in a Metal–Organic Hybrid: An EPR, DFT, and Crystallographic Characterization of Copper-Doped Zinc Creatininium Sulfate
inferred← citeshttps://doi.org/10.1021/acs.jpca.5b07864openalex-snapshot
Models for Copper Dynamic Behavior in Doped Cadmium dl -Histidine Crystals: Electron Paramagnetic Resonance and Crystallographic Analysis
inferred← citeshttps://doi.org/10.1021/acsmedchemlett.6b00369openalex-snapshot
2-Hydroxypyridine-N-oxide-Embedded Aurones as Potent Human Tyrosinase Inhibitors
inferred← citeshttps://doi.org/10.1021/acsomega.2c00256openalex-snapshot
Photodegradation and In Silico Molecular Docking Study of a Diuretic Drug: Clopamide
inferred← citeshttps://doi.org/10.1021/bi200395topenalex-snapshot
Crystal Structure of Agaricus bisporus Mushroom Tyrosinase: Identity of the Tetramer Subunits and Interaction with Tropolone
inferred← citeshttps://doi.org/10.1021/cr400327topenalex-snapshot
Copper Active Sites in Biology
inferred← citeshttps://doi.org/10.1021/ic501829sopenalex-snapshot
Exploring the Interaction of N/S Compounds with a Dicopper Center: Tyrosinase Inhibition and Model Studies
inferred← citeshttps://doi.org/10.1021/jacs.3c13183openalex-snapshot
Tyrosinase-Based Proximity Labeling in Living Cells and In Vivo
inferred← citeshttps://doi.org/10.1021/jf501145bopenalex-snapshot
Biological Activity and Molecular Docking Studies of Curcumin-Related α,β-Unsaturated Carbonyl-Based Synthetic Compounds as Anticancer Agents and Mushroom Tyrosinase Inhibitors
inferred← citeshttps://doi.org/10.1021/jp401477mopenalex-snapshot
Electron Paramagnetic Resonance Spectroscopic Study of Copper Hopping in Doped Bis( l -histidinato)cadmium Dihydrate
inferred← citeshttps://doi.org/10.1021/jp500981copenalex-snapshot
Copper Dynamics in Doped Metal–Bis(histidine) Complexes
inferred← citeshttps://doi.org/10.1038/nbt.2671openalex-snapshot
Accelerating the design of biomimetic materials by integrating RNA-seq with proteomics and materials science
inferred← citeshttps://doi.org/10.1038/ncomms5505openalex-snapshot
Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins
inferred← citeshttps://doi.org/10.1038/s41467-018-04227-3openalex-snapshot
Bacterial encapsulins as orthogonal compartments for mammalian cell engineering
inferred← citeshttps://doi.org/10.1038/s41467-022-33122-1openalex-snapshot
Enzymatic synthesis of benzylisoquinoline alkaloids using a parallel cascade strategy and tyrosinase variants
inferred← citeshttps://doi.org/10.1038/s41467-025-57767-wopenalex-snapshot
Spatiotemporally resolved mapping of extracellular proteomes via in vivo-compatible TyroID
inferred← citeshttps://doi.org/10.1038/s42004-018-0045-8openalex-snapshot
Nanocarbon and nanodiamond for high performance phenolics sensing
inferred← citeshttps://doi.org/10.1038/srep34993openalex-snapshot
The unravelling of the complex pattern of tyrosinase inhibition
inferred← citeshttps://doi.org/10.1039/9781837677955-00026openalex-snapshot
Structure and Function of Dinuclear Copper Tyrosinase
inferred← citeshttps://doi.org/10.1039/c0cs00202jopenalex-snapshot
Copper–O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme
inferred← citeshttps://doi.org/10.1039/c3cc47469kopenalex-snapshot
Probing kojic acid binding to tyrosinase enzyme: insights from a model complex and QM/MM calculations
inferred← citeshttps://doi.org/10.1039/c3cc47888bopenalex-snapshot
New catalytic model systems of tyrosinase: fine tuning of the reactivity with pyrazole-based N-donor ligands
inferred← citeshttps://doi.org/10.1039/c4dt03010aopenalex-snapshot
Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism
inferred← citeshttps://doi.org/10.1039/c5cs00923eopenalex-snapshot
Design and engineering of artificial oxygen-activating metalloenzymes
inferred← citeshttps://doi.org/10.1039/c5nr03316kopenalex-snapshot
A practical and highly sensitive C 3 N 4 -TYR fluorescent probe for convenient detection of dopamine
inferred← citeshttps://doi.org/10.1039/c5ra02995copenalex-snapshot
Molecular docking studies and biological evaluation of chalcone based pyrazolines as tyrosinase inhibitors and potential anticancer agents
inferred← citeshttps://doi.org/10.1039/c6mt00062bopenalex-snapshot
pH-regulated metal–ligand switching in the HM loop of ATP7A: a new paradigm for metal transfer chemistry
inferred← citeshttps://doi.org/10.1039/c6ra09365eopenalex-snapshot
Computational approaches to predict binding interactions between mammalian tyrosinases and (S)-(+)-decursin and its analogues as potent inhibitors
inferred← citeshttps://doi.org/10.1039/c9md00005dopenalex-snapshot
Thiosemicarbazones with tyrosinase inhibitory activity
inferred← citeshttps://doi.org/10.1039/d2cc00750aopenalex-snapshot
Evidence for H-bonding interactions to the μ-η 2 :η 2 -peroxide of oxy-tyrosinase that activate its coupled binuclear copper site
inferred← citeshttps://doi.org/10.1071/ch16426openalex-snapshot
The Evolution of New Catalytic Mechanisms for Xenobiotic Hydrolysis in Bacterial Metalloenzymes*
inferred← citeshttps://doi.org/10.1073/pnas.1208718109openalex-snapshot
Structure/function correlations among coupled binuclear copper proteins through spectroscopic and reactivity studies of NspF
inferred← citeshttps://doi.org/10.1073/pnas.1523575113openalex-snapshot
Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases
inferred← citeshttps://doi.org/10.1074/jbc.m111.222745openalex-snapshot
Characterization of a Dipartite Iron Uptake System from Uropathogenic Escherichia coli Strain F11
inferred← citeshttps://doi.org/10.1074/jbc.m113.477612openalex-snapshot
Crystal Structures of Copper-depleted and Copper-bound Fungal Pro-tyrosinase
inferred← citeshttps://doi.org/10.1074/jbc.ra118.002560openalex-snapshot
Pseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases
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