Model studies of the Cu _B site of cytochrome c oxidase utilizing a Zn(ii) complex containing an imidazole-phenol cross-linked ligand

Keyphrases

• Cytochrome c Oxidase 100%
• B-site 100%
• Cross-linked 100%
• Zn(II) 100%
• Cu-B 100%
• Imidazole 100%
• PK a 40%
• Amines 20%
• Active Sites 20%
• Spectroscopic Data 20%
• Dication 20%
• Bonding Interactions 20%
• Histidine 20%
• Bromide 20%
• Bimetallic 20%
• Hydrogen Peroxide 20%
• Protonation 20%
• Heme 20%
• Axial Ligand 20%
• Pyridine 20%
• Redox State 20%
• Deprotonation 20%
• Tertiary Amine 20%
• Electron Reduction 20%
• Electron Density 20%
• Tyrosine 20%
• 1H NMR Spectroscopy 20%
• Chelating Ligands 20%
• Axial Position 20%
• Ortho 20%
• Phenolate 20%
• Cationic Complexes 20%
• Enzyme Complex 20%
• Coordination Environment 20%
• Nitrogen Ligands 20%
• Oxidation Potential 20%
• Tetrahedral Geometry 20%
• Equatorial Plane 20%
• Tripod 20%
• Trigonal Bipyramidal Geometry 20%
• Gain Stabilization 20%
• Imidazole Ligands 20%
• Complex Gain 20%
• Tripodal 20%
• Coordination Properties 20%
• Electron Donating Capacity 20%
• Phenoxyl Radical 20%
• Strong Donor 20%

Chemistry

• Cytochrome 100%
• Phenol 100%
• Imidazole 100%
• Density Functional Theory 33%
• Dissociation Exponent 33%
• 1H NMR Spectroscopy 16%
• Histidine 16%
• Heme 16%
• Redox State 16%
• Substance Spectroscopy 16%
• Deprotonation 16%
• Donor 16%
• Electron Density 16%
• Phenolate 16%
• Tertiary Amine 16%
• Oxidation Potential 16%

Material Science

• Protein 100%
• Theoretical Calculation 100%
• Oxidation Reaction 50%
• Carrier Concentration 50%
• Nuclear Magnetic Resonance Spectroscopy 50%