来自恶臭假单胞菌F1的甲苯双加氧酶的α亚基可以从还原型铁氧还蛋白TOL接受电子，但在没有β亚基的情况下催化无活性。
The alpha subunit of toluene dioxygenase from Pseudomonas putida F1 can accept electrons from reduced FerredoxinTOL but is catalytically inactive in the absence of the beta subunit.
作者信息
Jiang H, Parales R E, Gibson D T
机构信息
Department of Microbiology and Center for Biocatalysis and Bioprocessing, The University of Iowa, Iowa City, Iowa 52242, USA.
出版信息
Appl Environ Microbiol. 1999 Jan;65(1):315-8. doi: 10.1128/AEM.65.1.315-318.1999.
Abstract
The oxygenase component of toluene dioxygenase from Pseudomonas putida F1 is an iron-sulfur protein (ISPTOL) consisting of alpha (TodC1) and beta (TodC2) subunits. Purified TodC1 gave absorbance and electron paramagnetic resonance spectra identical to those given by purified ISPTOL. TodC1 was reduced by NADH and catalytic amounts of ReductaseTOL and FerredoxinTOL. Reduced TodC1 did not oxidize toluene, and catalysis was strictly dependent on the presence of purified TodC2.
摘要
恶臭假单胞菌F1甲苯双加氧酶的加氧酶组分是一种铁硫蛋白（ISPTOL），由α（TodC1）和β（TodC2）亚基组成。纯化后的TodC1的吸光度和电子顺磁共振光谱与纯化后的ISPTOL相同。TodC1可被NADH以及催化量的还原酶TOL和铁氧还蛋白TOL还原。还原后的TodC1不能氧化甲苯，催化作用严格依赖于纯化后的TodC2的存在。
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