Ensley B D, Gibson D T, Laborde A L
J Bacteriol. 1982 Mar;149(3):948-54. doi: 10.1128/jb.149.3.948-954.1982.
The initial reactions in the oxidation of naphthalene by Pseudomonas sp. strain NCIB 9816 involves the enzymatic incorporation of one molecule of oxygen into the aromatic nucleus to form (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The enzyme catalyzing this reaction, naphthalene dioxygenase, was resolved into three protein components, designated A, B, and C, by DEAE-cellulose chromatography. Incubation of naphthalene with components A, B, and C in the presence of NADH resulted in the formation of (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The ratio of oxygen and NADH utilization to product formation was 1:1:1. NADPH also served as an electron donor for naphthalene oxygenation. However, its activity was less than 50% of that observed with NADH. Component A showed NAD(P)H-cytochrome c reductase activity which was stimulated by the addition of flavin adenine dinucleotide and flavin mononucleotide. A similar stimulation was observed when these flavin nucleotides were added to the naphthalene dioxygenase assay system. These preliminary observations indicate that naphthalene dioxygenase has properties in common with both monooxygenase and dioxygenase multicomponent enzyme systems.
假单胞菌属菌株NCIB 9816氧化萘的初始反应涉及将一分子氧酶促掺入芳环中，形成(+)-顺式-(1R,2S)-二羟基-1,2-二氢萘。催化该反应的酶，即萘双加氧酶，通过DEAE-纤维素色谱法被分离为三个蛋白质组分，分别命名为A、B和C。在NADH存在下，将萘与组分A、B和C一起温育，导致形成(+)-顺式-(1R,2S)-二羟基-1,2-二氢萘。氧、NADH利用与产物形成的比例为1:1:1。NADPH也可作为萘氧化的电子供体。然而，其活性不到用NADH时观察到的活性的50%。组分A显示出NAD(P)H-细胞色素c还原酶活性，该活性可通过添加黄素腺嘌呤二核苷酸和黄素单核苷酸来刺激。当将这些黄素核苷酸添加到萘双加氧酶测定系统中时，也观察到类似的刺激作用。这些初步观察结果表明，萘双加氧酶具有与单加氧酶和双加氧酶多组分酶系统共有的特性。
