How Do Metalloproteins Tame the Fenton Reaction and Utilize •oH Radicals in Constructive Manners?

Keyphrases

• Hydrogen Peroxide 100%
• Fenton Reaction 100%
• OH Radical 100%
• Metalloproteins 100%
• Fenton 42%
• Lytic Polysaccharide Monooxygenase 35%
• Protein Environment 21%
• H-bond Network 21%
• Co-substrate 21%
• Homolysis 21%
• Active Sites 14%
• Cu(II) 14%
• Tight 14%
• Metalloenzymes 14%
• Active Species 14%
• P450 14%
• Fe(III) 14%
• Heme Peroxidase 14%
• H-abstraction 14%
• Oxidative Transformation 14%
• P450 BM3 14%
• Hydrogen Bonds (H-bonds) 7%
• Activation Mechanism 7%
• Oxidative Damage 7%
• OH Groups 7%
• Fe(II) 7%
• Hydrogen Atom 7%
• Flexible Molecules 7%
• Highly Flexible 7%
• Resting State 7%
• Hydrophilic Drug 7%
• Cu-catalyzed 7%
• Heterotic 7%
• C-H Bond 7%
• Presence-absence 7%
• H-bonding Interaction 7%
• Non-heme 7%
• Non-enzymatic Reaction 7%
• Synthetic System 7%
• Radical Species 7%
• Coordination Environment 7%
• Radical Intermediates 7%
• Compound I 7%
• P450cam 7%
• Fe(IV) 7%
• Heme Enzyme 7%
• Non-heme Iron Enzyme 7%
• P450 Fatty Acid Decarboxylase 7%
• O-O Activation 7%
• Non-productive Binding 7%
• OleT 7%
• Reaction Environment 7%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Polysaccharide 100%
• Unspecific Monooxygenase 100%
• Fenton Reaction 100%
• Metalloprotein 100%
• Cytochrome P450 60%
• Active Site 40%
• Metalloenzyme 40%
• Carboxy-Lyases 20%
• Hydrogen Peroxide 20%
• Substrate Concentration 20%
• Lactoperoxidase 20%
• Heme Enzymes 20%

Chemistry

• Metalloprotein 100%
• Fenton Reaction 100%
• Fenton 100%
• Polysaccharide 71%
• Monooxygenase 71%
• Heme 42%
• Cytochrome P450 42%
• Metalloenzyme 28%
• Hydrogen Peroxide 14%
• Hydrogen Atom 14%
• formation 14%