Regulation of the Properties of the Heme-NO Complexes in Nitric-oxide Synthase by Hydrogen Bonding to the Proximal Cysteine

Medicine & Life Sciences

• Hydrogen Bonding 100%
• Heme 92%
• Nitric Oxide Synthase 80%
• Cysteine 78%
• Protein Isoforms 33%
• Enzymes 30%
• Oxygenases 19%
• Raman Spectrum Analysis 18%
• Citrulline 17%
• Catalysis 16%
• Sulfur 16%
• Tryptophan 14%
• Arginine 12%
• Iron 11%
• Oxygen 9%
• Population 5%

Chemical Compounds

• Heme 76%
• Cysteine 71%
• Hydrogen 41%
• Cysteine Residue 34%
• Citrulline 23%
• L-Arginine 21%
• Resonance Raman Spectroscopy 20%
• Hydrogen Bond 20%
• Resonance Raman Spectrum 19%
• Environment 18%
• Tryptophan Residue 18%
• Sulfur Atom 16%
• Enzyme Activity 13%
• Electronic Property 13%
• Dissociation 11%
• Catalysis 10%
• Probe 10%
• Dioxygen 8%