Geary P J, Saboowalla F, Patil D, Cammack R
Biochem J. 1984 Feb 1;217(3):667-73. doi: 10.1042/bj2170667.
Benzene dioxygenase from Pseudomonas putida comprises three components, namely a flavoprotein (NADH:ferredoxin oxidoreductase; Mr 81000), an intermediate electron-transfer protein, or ferredoxin (Mr 12000) with a [2Fe-2S] cluster, and a terminal dioxygenase containing two [2Fe-2S] iron-sulphur clusters (Mr 215000), which requires two additional Fe2+ atoms/molecule for oxygenase activity. The ferredoxin and the dioxygenase give e.s.r. signals in the reduced state with rhombic symmetry and average g values of 1.92 and 1.896 respectively. The mid-point redox potentials were determined by e.s.r. titration at pH 7.0 to be -155 mV and -112 mV respectively. The signal from the dioxygenase shows pronounced g anisotropy and most closely resembles those of 4-methoxybenzoate mono-oxygenase from Pseudomonas putida and the [2Fe-2S] 'Rieske' proteins of the quinone-cytochrome c region of electron-transport chains of respiration and photosynthesis.
恶臭假单胞菌的苯双加氧酶由三个组分组成，即一种黄素蛋白（NADH：铁氧化还原蛋白氧化还原酶；分子量81000）、一种中间电子传递蛋白或铁氧化还原蛋白（分子量12000），其含有一个[2Fe-2S]簇，以及一种末端双加氧酶，该双加氧酶含有两个[2Fe-2S]铁硫簇（分子量215000），其加氧酶活性需要另外两个Fe2+原子/分子。铁氧化还原蛋白和双加氧酶在还原状态下给出具有菱形对称性的电子顺磁共振信号，平均g值分别为1.92和1.896。通过在pH 7.0下进行电子顺磁共振滴定测定中点氧化还原电位分别为-155 mV和-112 mV。双加氧酶的信号显示出明显的g各向异性，并且与恶臭假单胞菌的4-甲氧基苯甲酸单加氧酶以及呼吸和光合作用电子传递链的醌-细胞色素c区域的[2Fe-2S]“ Rieske”蛋白的信号最为相似。
