对嗜热栖热袍菌中一种极其活跃的NADH氧化酶的特性研究
Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima.
作者信息
Yang Xianqin, Ma Kesen
机构信息
Department of Biology, University of Waterloo, 200 University Avenue West, Waterloo, Ontario N2L 3G1, Canada.
出版信息
J Bacteriol. 2007 Apr;189(8):3312-7. doi: 10.1128/JB.01525-06. Epub 2007 Feb 9.
Abstract
An NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima was purified. The enzyme was very active in catalyzing the reduction of oxygen to hydrogen peroxide with an optimal pH value of 7 at 80 degrees C. The V(max) was 230 +/- 14 mumol/min/mg (k(cat)/K(m) = 548,000 min(-1) mM(-1)), and the K(m) values for NADH and oxygen were 42 +/- 3 and 43 +/- 4 muM, respectively. The NADH oxidase was a heterodimeric flavoprotein with two subunits with molecular masses of 54 kDa and 46 kDa. Its gene sequences were identified, and the enzyme might represent a new type of NADH oxidase in anaerobes. An NADH-dependent peroxidase with a specific activity of 0.1 U/mg was also present in the cell extract of T. maritima.
摘要
从嗜热厌氧菌海栖热袍菌中纯化出一种NADH氧化酶。该酶在催化氧气还原为过氧化氢方面具有很高的活性，在80℃时最适pH值为7。V(max)为230±14 μmol/分钟/毫克（k(cat)/K(m)=548,000分钟(-1)毫摩尔(-1)），NADH和氧气的K(m)值分别为42±3和43±4 μM。该NADH氧化酶是一种异二聚体黄素蛋白，由两个亚基组成，分子量分别为54 kDa和46 kDa。其基因序列已被鉴定，该酶可能代表厌氧菌中的一种新型NADH氧化酶。海栖热袍菌的细胞提取物中还存在一种比活性为0.1 U/毫克的NADH依赖性过氧化物酶。
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