A Single Mutation in Cytochrome P450 BM3 Induces the Conformational Rearrangement Seen upon Substrate Binding in the Wild-type Enzyme

Keyphrases

• Conformational Rearrangement 100%
• In the Wild 100%
• Substrate Binding 100%
• Heme Iron 100%
• Cytochrome P450 BM3 100%
• Single-point mutation 100%
• Spin State 50%
• Palmitate 50%
• Heme 50%
• P450 BM3 50%
• P450 Enzymes 50%
• Structural Change 25%
• Bound Form 25%
• Active Sites 25%
• Reductase 25%
• Electron Transfer 25%
• Redox Couple 25%
• Iron Reduction 25%
• Glutamate 25%
• Reduction Potential 25%
• Multi-domain 25%
• Dioxygen 25%
• Conformational Change 25%
• Substrate-induced 25%
• Ligation 25%
• Flavocytochrome 25%
• P450 25%
• Diflavin Reductase 25%
• State Shift 25%
• Substrate-free 25%
• Low-spin State 25%
• Heme Ligand 25%
• Fatty Acid 2-hydroxylase 25%
• P450cam 25%
• Structural Rearrangement 25%
• High-resolution Crystal Structure 25%
• Microsomal P450 25%
• Paradigm Model 25%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Wild Type 100%
• Cytochrome P450 100%
• Heme Iron 80%
• Crystal Structure 60%
• Oxidoreductase 40%
• Reductase 40%
• Palmitoleic Acid 40%
• Oxygenase 20%
• Active Site 20%
• Conformation 20%
• Glutamic Acid 20%
• Conformational Change 20%
• Electron Transport 20%
• Unspecific Monooxygenase 20%
• Derived Protein 20%