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Grayson DA, Tewari YB, Mayhew MP, Vilker VL, Goldberg RN: Tetralin as a substrate for camphor (cytochrome P450) 5-monooxygenase. Arch Biochem Biophys. 1996 Aug 15;332(2):239-47.
Camphor (cytochrome P450) 5-monooxygenase, originally isolated from the bacterium Pseudomonas putida PgG 786, catalyzes the essentially stereospecific conversion of tetralin (1,2,3,4-tetrahydronaphthalene) to (R)-1-tetralol ((R).(-)-1,2,3,4-tetrahydro-1-naphthol): tetralin (aq) + NADH (aq) + O2 (aq) = (R)-1-tetralol (aq) + NAD (aq) + H2O (l). The ratio of the amount of (S)-1-tetralol to the amount of (R)-1-tetralol is small (approximately 0.04) and the reaction is essentially stereospecific. The reaction time-course plot indicates the formation of additional product (s) from the (R)-1-tetralol. It is found that the above reaction obeys Michaelis-Menten kinetics and that dimethyl sulfoxide, methanol, and p-dioxane serve as accelerators. Approximate values of a Michaelis constant Km, limiting rate Vmax, and catalytic constant kcat are obtained for this reaction under a specified set of conditions. It is shown by means of a thermochemical cycle calculation that the apparent equilibrium constant for this reaction is approximately 4 x 10 (65) at T = 298.15 K and pH 7.3. Thus, this reaction is "irreversible" and, unless the enzyme system is inactivated, it will proceed in the direction of complete formation of 1-tetralol from tetralin. A detailed description of the preparation of the camphor (cytochrome P450) 5-monooxygenase enzyme system from recombinant microorganisms is given. |
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