Comparative effects of substrates and pterin cofactor on the heme midpoint potential in inducible and neuronal nitric oxide synthases

Keyphrases

• Heme 100%
• Inducible Nitric Oxide Synthase 100%
• Midpoint Potential 100%
• Pterin 100%
• Neuronal Nitric Oxide Synthase (nNOS) 100%
• Substrate Effect 100%
• Heme Iron 69%
• Arginine 61%
• Tetrahydrobiopterin 61%
• Oxygenase 46%
• Iron Reduction 30%
• Heme Group 23%
• Thermodynamics 15%
• Reduction Potential 15%
• Nitric Oxide 7%
• Aminoguanidine 7%
• Electronic Properties 7%
• Regulatory Mechanism 7%
• Electron Transfer 7%
• Binding Site 7%
• Binding Affinity 7%
• Free Radicals 7%
• Nitric Oxide Synthase Inhibitors 7%
• Reductase 7%
• Substrate Binding 7%
• Consumption Rate 7%
• Nicotinamide Adenine Dinucleotide Phosphate (NADPH) 7%
• Cofactor Binding 7%
• Oxidative Attack 7%
• Electron Flux 7%
• L-NAME 7%
• Thermodynamic Data 7%
• Nitric Oxide Synthase Isoforms 7%
• Molecular Oxygen Activation 7%
• Heme Reduction 7%
• Heme-containing Enzymes 7%
• Iron Forms 7%
• Substrate-based Inhibitor 7%
• Consumption Capacity 7%
• Guanidino 7%
• Reduction Thermodynamics 7%

Biochemistry, Genetics and Molecular Biology

• Nitric Oxide Synthase 100%
• Arginine 45%
• Heme Iron 45%
• Sapropterin 40%
• Enzyme 30%
• Oxygenase 30%
• Isoform 15%
• Electron Transport 10%
• Reductase 5%
• Crystal Structure 5%
• Binding Site 5%
• Binding Affinity 5%
• Nitric Oxide 5%
• Oxidoreductase 5%