Dioxygen Binding to Diferrous Centers. Models for Diiron-Oxo Proteins

Keyphrases

• Dioxygen 100%
• Dioxygen Binding 100%
• Diiron-oxo Proteins 100%
• Carboxylate 66%
• Methane Monooxygenase 66%
• Tetrakis 66%
• Dichloromethane 66%
• Absorption Maxima 66%
• Fe(II) 66%
• Ribonucleotide Reductase 66%
• Dinucleating Ligand 66%
• Pyridine Analogs 66%
• Polar Aprotic Solvents 66%
• Low Temperature 33%
• Diiron 33%
• NMR Studies 33%
• Ethyl 33%
• Anions 33%
• Ambient Temperature 33%
• Resonance Raman 33%
• Radical Formation 33%
• Antiferromagnetic Coupling 33%
• Peroxo 33%
• Alkoxide 33%
• Benzoate 33%
• Carboxylato 33%
• Triclinic 33%
• Oxygenated Species 33%
• Ph3P 33%
• One-electron Oxidation 33%
• Trigonal 33%
• NMR Properties 33%
• Cell Constant 33%
• Coupling Interaction 33%
• Alkane Hydroxylation 33%
• Coordination Sites 33%
• 1,3-diaminopropane 33%
• Tyrosyl Radical 33%
• Visible Light Absorption 33%
• Biphenol 33%
• Peroxo Species 33%
• Geometrical Study 33%
• 2,4-di-tert-butylphenol 33%
• 2-hydroxy-1 33%
• Antiferromagnetically Coupled 33%

Chemistry

• Dioxygen 100%
• NMR Spectroscopy 50%
• Methane 50%
• Monooxygenase 50%
• Absorption Maxima 50%
• Polar Aprotic Solvent 50%
• Carboxylic Acid 50%
• Ribonucleotide 50%
• Antiferromagnetic 25%
• Ethyl 25%
• Benzoate 25%
• Triclinic Space Group 25%
• 2,4-di-tert-butylphenol 25%
• stability 25%
• formation 25%
• Phenol 25%
• Alkane 25%
• hydroxylation 25%