NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450.
Pochapsky, Thomas C
NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450. [electronic resource] - Biochimica et biophysica acta. Proteins and proteomics Jan 2018 - 126-133 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1570-9639
10.1016/j.bbapap.2017.04.003 doi
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
NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450. [electronic resource] - Biochimica et biophysica acta. Proteins and proteomics Jan 2018 - 126-133 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1570-9639
10.1016/j.bbapap.2017.04.003 doi
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