Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy

Keyphrases

• Cysteine 100%
• Magnetic Circular Dichroism Spectroscopy 100%
• Hydrogen Bond Network 100%
• P450cam 100%
• Electronic Transitions 60%
• Charge Transfer Transition 60%
• Low Temperature 40%
• Variable Temperature 40%
• Amino Acids 20%
• Fe-S 20%
• Circular Dichroism Spectra 20%
• Sulfur 20%
• Hydrogen Bonds (H-bonds) 20%
• Q-band 20%
• Magnetic Circular Dichroism 20%
• Variable Electric Field 20%
• Heme 20%
• Higher Spin 20%
• Cytochrome P450 (CYP450) 20%
• Charge Transfer 20%
• Oscillator Strength 20%
• Thiolate 20%
• Low Spin 20%
• Porphyrin 20%
• Small Shift 20%
• Charge-transfer Excited State 20%
• Soret 20%
• Donor Strength 20%

Chemistry

• Cysteine 100%
• Magnetic Circular Dichroism Spectroscopy 100%
• Hydrogen Bonding 100%
• Cytochrome 100%
• Charge Transfer Transition 60%
• Electronic Transition 60%
• Heme 40%
• Purity 40%
• Circular Dichroism 20%
• Magnetic Circular Dichroism 20%
• Density Functional Theory 20%
• Amino Acid 20%
• Excited State 20%
• Oscillator Strength 20%
• Time-Dependent Density Functional Theory 20%
• Porphyrin 20%
• Coordination Sphere 20%
• Sulfur Donor 20%