Hydride transfer catalysed by Escherichia coli and Bacillus subtilis dihydrofolate reductase: Coupled motions and distal mutations

Keyphrases

• Escherichia Coli 100%
• Bacillus Subtilis (B. subtilis) 100%
• Coupled Motion 100%
• Methylenetetrahydrofolate Reductase (MTHFR) 100%
• Hydride Transfer 100%
• Distal mutation 100%
• Conformational Change 42%
• Donor-acceptor Distance 28%
• Free Energy Barrier 28%
• Hydride Transfer Reactions 28%
• Transition State 14%
• Reaction Coordinate 14%
• Across Species 14%
• Tertiary Structure 14%
• Classical Molecular Dynamics Simulations 14%
• Transfer Rate 14%
• Nuclear Quantum Effects 14%
• Sequence Identity 14%
• Single-molecule Experiments 14%
• Local Structural Changes 14%
• Hydrogen Tunneling 14%
• Millisecond Interval 14%
• Sample Configuration 14%
• Motion Change 14%
• B.subtilis 14%
• Structure Transfer 14%
• Hybrid Quantum-classical 14%
• Zero-point Energy 14%
• Reductase Enzymes 14%
• Energy Tunnel 14%

Chemistry

• Dihydrofolates 100%
• Donor 66%
• Gibbs Free Energy 66%
• Energy Barrier 66%
• Transfer Reaction 66%
• Structure 33%
• Hydrogen 33%
• Transition State 33%
• Molecular Dynamics 33%
• Primary Structure 33%
• Zero Point Energy 33%
• Tertiary Structure 33%