NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450. [electronic resource]
Producer: 20180208Description: 126-133 p. digitalISSN:- 1570-9639
- Acetophenones -- chemistry
- Amino Acid Motifs
- Bacterial Proteins -- chemistry
- Binding Sites
- Biocatalysis
- Camphor -- chemistry
- Camphor 5-Monooxygenase -- chemistry
- Cloning, Molecular
- Electron Spin Resonance Spectroscopy
- Escherichia coli -- genetics
- Ferric Compounds -- chemistry
- Gene Expression
- Heme -- chemistry
- Kinetics
- Models, Molecular
- NAD -- chemistry
- Oxidation-Reduction
- Protein Binding
- Protein Conformation, alpha-Helical
- Protein Conformation, beta-Strand
- Protein Interaction Domains and Motifs
- Recombinant Proteins -- chemistry
- Substrate Specificity
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Publication Type: Journal Article; Research Support, N.I.H., Extramural
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