Pshenichnikova A B, Nevo A N, Volkova E V, Skladnev D A, Shvets V I
Lomonosov Moscow State Academy of Fine Chemical Technology, Moscow, 117571 Russia.
Prikl Biokhim Mikrobiol. 2004 Jan-Feb;40(1):24-7.
We studied the effect of deuterium oxide present in the medium on the activity of methanol dehydrogenase (EC 1.1.99.8) from methylotrophic bacteria Methylophilus sp. B-7741. Methanol dehydrogenase activity in extracts of the biomass obtained in a highly deuterated medium (2H-enzyme) was 34-47% of enzyme activity in the control biomass, which depended on reaction conditions. The isotopic effects of substrate deuterium (methanol) for 1H-enzyme and 2H-enzyme were 1.37 +/- 0.05 and 1.38 +/- 0.01, respectively. We revealed for the first time the reverse isotopic effect of solvent deuterium in the reaction catalyzed by methanol dehydrogenase (0.80 +/- 0.02 and 0.60 +/- 0.01 for 1H-enzyme and 2H-enzyme, respectively).
我们研究了培养基中重水对甲基营养菌嗜甲基菌属B-7741甲醇脱氢酶（EC 1.1.99.8）活性的影响。在高度氘化培养基中获得的生物质提取物中的甲醇脱氢酶活性（2H-酶）为对照生物质中酶活性的34-47%，这取决于反应条件。1H-酶和2H-酶的底物氘（甲醇）的同位素效应分别为1.37±0.05和1.38±0.01。我们首次揭示了甲醇脱氢酶催化反应中溶剂氘的反向同位素效应（1H-酶和2H-酶分别为0.80±0.02和0.60±0.01）。
