S-adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance

Keyphrases

• S-adenosylmethionine 100%
• Electron Paramagnetic Resonance 100%
• Iron-sulfur Center 100%
• Lysine 2,3-aminomutase 100%
• Lysine 44%
• Iron-sulfur Cluster 33%
• Reduced Form 33%
• S-adenosylhomocysteine 33%
• Rearrangement Mechanism 33%
• Pyridoxal 5′-phosphate 33%
• Active Sites 22%
• Tracer Experiment 22%
• Tritium 22%
• Reducing Agent 22%
• 5′-Deoxyadenosyl Radical 22%
• Low Temperature 11%
• EPR Spectra 11%
• Interconversion 11%
• Hydrogen Atom 11%
• Active Form 11%
• Hydrogen Abstraction 11%
• Dithionite 11%
• Clostridial 11%
• Radical Intermediates 11%
• Unusual Properties 11%

Chemistry

• EPR Spectroscopy 100%
• Lysine 100%
• Iron-Sulfur Cluster 50%
• Pyridoxal 50%
• S-Adenosyl-L-Homocysteine 50%
• L-Lysine 33%
• Tritium 33%
• Reducing Agent 33%
• Hydrogen 33%
• Hydrogen Atom 16%
• Catalysis 16%
• Aldimine 16%