Structural organization and energy transduction mechanism of Na+, K+-ATPase studied with transition metal-catalyzed oxidative cleavage

Keyphrases

• Fe2+ 100%
• Cu2+ 100%
• Structural Organization 100%
• Oxidative Cleavage 100%
• Energy Transduction 100%
• Transduction Mechanism 100%
• Structural Energy 100%
• Na+/K+ ATPase 100%
• Transition-metal-catalyzed 100%
• Mg2+ 60%
• Diphenyl 40%
• P-type Pump 40%
• Cytoplasmic Domain 20%
• Hydrogen Peroxide 20%
• Phenanthroline 20%
• Ligation 20%
• Membrane Protein 20%
• Spatial Organization 20%
• Peptide Bond 20%
• Phenanthroline Complex 20%
• Transmembrane Segment 20%
• Native Structure 20%
• Structure Function 20%
• Domain-domain Interaction 20%
• β Subunit 20%
• Subunit Interaction 20%
• ATP Binding Proteins 20%
• Metal Can 20%
• Conformation-dependent 20%
• Membrane-water Interface 20%

Biochemistry, Genetics and Molecular Biology

• ATPase 100%
• Adenosine Triphosphate 100%
• Energy Transfer 100%
• Conformation 50%
• Binding Protein 25%
• Hydrogen Peroxide 25%
• Membrane Protein 25%
• Ascorbic Acid 25%
• Enzymatic Hydrolysis 25%
• Peptide Bond 25%
• Structure Activity Relation 25%
• Beta Chain 25%
• Vitamin C 25%