the enzyme also catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant
electron-transfer reaction between the electrode and heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide film on a plastic formed carbon electrode is demonstrated. A quasi-reversible redox response is observed at temperatures of up to 80°C
the enzyme also catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant
electron-transfer reaction between the electrode and heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide film on a plastic formed carbon electrode is demonstrated. A quasi-reversible redox response is observed at temperatures of up to 80°C
cytochrome P450 from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 (P450st) is a thermophilic cytochrome P450 that shows high tolerance of harsh conditions and is capable of catalyzing some peroxygenase reactions. Both hydrogen peroxide-driven ethylbenzene hydroxylation and styrene epoxidation by wild-type P450st are found to be activated in weak acidic and weak basic solutions
cytochrome P450 from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 (P450st) is a thermophilic cytochrome P450 that shows high tolerance of harsh conditions and is capable of catalyzing some peroxygenase reactions. Both hydrogen peroxide-driven ethylbenzene hydroxylation and styrene epoxidation by wild-type P450st are found to be activated in weak acidic and weak basic solutions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method using a protein solution (15 mg/ml) and a reservoir solution (30% (w/v) polyethylene glycol 4000, 200 mM lithium sulfate monohydrate and 100 mM Tris-HCl, pH 8.5)
vapour diffusion method, X-ray crystallography at a resolution of 1.94 A reveals a sufficiently large heme pocket for NAD(P)H binding and a novel contiguous channel from the active site to bulk solvent in the distal heme pocket. The mutant shows a higher affinity for NADH compared with the wild-type because the mutant has a more widely open distal pocket for NAD(P)H binding
site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s
site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s
HOME
login
history
all enzymes
BRENDA home
History
1.14.13.B28 monooxygenase CYP119A2
more
top
Information
