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Design Parameters for Tuning the Type 1 Cu Multicopper Oxidase Redox Potential: Insight from a Combination of First Principles and Empirical Molecular Dynamics Simulations
70/70 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 70 checked references that resolve
resolves10.1073/pnas.73.5.1389
Spectroscopic studies and a structural model for blue copper centers in proteins.
resolves10.1007/s00775-009-0590-9
Multicopper oxidases: a workshop on copper coordination chemistry, electron transfer, and metallophysiology
resolves10.1134/S1063774508010124
Three-dimensional organization of three-domain copper oxidases: A review
resolves10.1007/s00775-005-0035-z
Reduction thermodynamics of the T1 Cu site in plant and fungal laccases
resolves10.1039/b716002j
An assessment of the relative contributions of redox and steric issues to laccase specificity towards putative substrates
resolves10.1007/s00253-009-1869-z
Fungal laccases as tools for the synthesis of new hybrid molecules and biomaterials
resolves10.1016/j.copbio.2009.05.002
Enzymatic delignification of plant cell wall: from nature to mill
resolves10.1074/jbc.M204571200
Crystal Structure of a Laccase from the FungusTrametes versicolor at 1.90-Å Resolution Containing a Full Complement of Coppers
resolves10.1073/pnas.052710499
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in
<i>Escherichia coli</i>
resolves10.1016/j.jmb.2008.11.024
The Structure of the Small Laccase from Streptomyces coelicolor Reveals a Link between Laccases and Nitrite Reductases
resolves10.1002/tcr.20125
Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
resolves10.1073/pnas.0902127106
Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase
resolves10.1016/j.jinorgbio.2006.05.007
Kinetic studies on the reaction between Trametes villosa laccase and dioxygen
resolves10.1021/ja0475510
A Four-Electron O<sub>2</sub>-Electroreduction Biocatalyst Superior to Platinum and a Biofuel Cell Operating at 0.88 V
resolves10.1021/cr0680639
Enzymes as Working or Inspirational Electrocatalysts for Fuel Cells and Electrolysis
resolves10.1021/ic9022486
Electroreduction of Dioxygen for Fuel-Cell Applications: Materials and Challenges
resolves10.1039/b703114a
A stable electrode for high-potential, electrocatalytic O2 reduction based on rational attachment of a blue copper oxidase to a graphite surface
resolves10.1039/B808939F
Efficient electrocatalytic oxygen reduction by the ‘blue’ copper oxidase, laccase, directly attached to chemically modified carbons
resolves10.1246/cl.2007.132
Bioelectrocatalytic Reduction of O2 Catalyzed by CueO from <i>Escherichia coli</i> Adsorbed on a Highly Oriented Pyrolytic Graphite Electrode
resolves10.1002/fuce.200800027
Direct Electrochemistry of CueO and Its Mutants at Residues to and Near Type I Cu for Oxygen‐Reducing Biocathode
resolves10.1016/j.bioelechem.2008.05.003
Surface characterization and direct electrochemistry of redox copper centers of bilirubin oxidase from fungi Myrothecium verrucaria
resolves10.1021/jp054783s
Interpreting the Catalytic Voltammetry of an Adsorbed Enzyme by Considering Substrate Mass Transfer, Enzyme Turnover, and Interfacial Electron Transport
resolves10.1016/j.jelechem.2006.10.035
Effects of axial ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type bioelectrocatalytic reduction of dioxygen
resolves10.1002/1097-461X(2001)81:5<335::AID-QUA1003>3.0.CO;2-Q
Structure, strain, and reorganization energy of blue copper models in the protein
resolves10.1016/0005-2728(72)90045-X
Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin
resolves10.1007/s00775-006-0102-0
Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies
resolves10.1016/j.bios.2007.11.004
Oxygen-reducing enzyme cathodes produced from SLAC, a small laccase from Streptomyces coelicolor
resolves10.1016/0022-2836(76)90311-9
Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
resolves10.1021/ar950140r
Hybrid Quantum and Molecular Mechanical Simulations: An Alternative Avenue to Solvent Effects in Organic Chemistry
resolves10.1021/ar970218z
Combined Quantum Mechanical/Molecular Mechanical Methodologies Applied to Biomolecular Systems
resolves10.1063/1.480503
Free energy calculation on enzyme reactions with an efficient iterative procedure to determine minimum energy paths on a combined <i>ab initio</i> QM/MM potential energy surface
resolves10.1002/jcc.540140205
Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the POLARIS and ENZYMIX programs
resolves10.1016/0009-2614(85)87168-2
Polarization constraints in molecular dynamics simulation of aqueous solutions: The surface constraint all atom solvent (SCAAS) model
resolves10.1021/j100209a016
Dynamics of reactions in polar solvents. Semiclassical trajectory studies of electron-transfer and proton-transfer reactions
resolves10.1063/1.2162881
Diabatic free energy curves and coordination fluctuations for the aqueous Ag+∕Ag2+ redox couple: A biased Born-Oppenheimer molecular dynamics investigation
resolves10.1021/ja049345y
Determinants of the Relative Reduction Potentials of Type-1 Copper Sites in Proteins
resolves10.1021/ja029699u
Probing the Role of Axial Methionine in the Blue Copper Center of Azurin with Unnatural Amino Acids
resolves10.1038/nature08551
Rationally tuning the reduction potential of a single cupredoxin beyond the natural range
resolves10.1038/nsb1096-842
Experimentally determined hydrophobicity scale for proteins at membrane interfaces
resolves10.1021/ja0212157
Frozen Density Functional Free Energy Simulations of Redox Proteins: Computational Studies of the Reduction Potential of Plastocyanin and Rusticyanin
resolves10.1073/pnas.0607890103
Role of protein frame and solvent for the redox properties of azurin from
<i>Pseudomonas aeruginosa</i>
resolves10.1021/ja971518e
Reorganization Energy of Blue Copper: Effects of Temperature and Driving Force on the Rates of Electron Transfer in Ruthenium- and Osmium-Modified Azurins
resolves10.1093/protein/gzj004
Shifting the optimal pH of activity for a laccase from the fungus Trametes versicolor by structure-based mutagenesis
resolves10.1039/b922734b
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
resolves10.1016/j.ica.2007.05.029
Pre-steady state kinetic studies on the microsecond time scale of the laccase from Trametes versicolor
resolves10.1021/ja900751c
Identification of a Radical Intermediate in the Enzymatic Reduction of Oxygen by a Small Laccase
resolves10.1021/ja908793d
Site−Site Interactions Enhances Intramolecular Electron Transfer in <i>Streptomyces coelicolor</i> laccase
The 3 references without a DOI — listed, not checked
no DOI — not checkedFrisch, M. J.Gaussian, Inc.,Wallingford CT, 2009.
no DOI — not checkedChu, Z. T.; Villa, J.; Strajbl, M.; Schutz, C. N.; Shurki, A.; Warshel, A.; MOLARIS 9.05 ed.University of the Southern California:Los-Angeles, 2004.
no DOI — not checkedAdvanced Inorganic Chemistry
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