Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation

Keyphrases

• Oxygen Activation 100%
• Tyrosine 100%
• Homoprotocatechuate 2,3-dioxygenase 100%
• Substrate Activation 100%
• 4-nitrocatechol 100%
• Local Distortion 60%
• Active Sites 40%
• Reaction Cycle 40%
• Fe(II) 40%
• O2 Activation 20%
• Aromatic Ring 20%
• Non-planar 20%
• Chelates 20%
• Binding Residues 20%
• X-ray Crystal Structure 20%
• Hydroxyl 20%
• Planarity 20%
• Van Der Waals 20%
• Enzyme Complex 20%
• Alternative Substrates 20%
• Strong Hydrogen Bond 20%
• Semiquinone Radicals 20%
• Aromatic Ring Cleavage 20%
• Global Deviation 20%
• Strained Structures 20%
• Substrate Structure 20%

Biochemistry, Genetics and Molecular Biology

• Active Site 100%
• Tyrosine 100%
• Dioxygenase 100%
• X Ray 33%
• Conformation 33%
• Wild Type 33%
• Crystal Structure 33%
• Hydrogen Bond 33%
• Semiquinone 33%
• Enzyme 33%