IRON-CONTAINING SUPEROXIDE-DISMUTASE FROM STRICT ANAEROBE DESULFOVIBRIO-DESULFURICANS (NORWAY 4)
IRON-CONTAINING SUPEROXIDE-DISMUTASE FROM STRICT ANAEROBE DESULFOVIBRIO-DESULFURICANS (NORWAY 4)
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DOI：
10.1016/s0300-9084(77)80286-1
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发表时间：
1977-01-01
期刊：
影响因子：
3.9
通讯作者：
HENRY, YA
中科院分区：
文献类型：
--
作者：
HATCHIKIAN, EC;HENRY, YA
超氧化物歧化酶，催化超氧化物自由基的歧化酶。+ 2 H+。O2 + H2O2从严格厌氧硫酸盐还原菌D.脱硫中纯化至均匀（挪威4）。其分子量为43,000，由2个大小相等的非共价键亚基组成。该酶通过原子吸收含有铁，而不含酸不稳定的S表明它不是铁-S蛋白。EPR谱显示铁以高自旋铁态存在。给出了酶的紫外和可见吸收光谱，以及氨基酸分析结果。与好氧微生物中发现的含铁歧化酶相比，从严格的厌氧菌中分离出的这种超氧化物歧化酶显然具有相似的物理化学性质。讨论了超氧化物歧化酶在这种严格厌氧硫酸盐还原剂中存在的意义。
Superoxide dismutase, the enzyme which catalyzes the dismutation of superoxide free radicals .**GRAPHIC**. + 2 H+ .fwdarw. O2 + H2O2) was purified to homogeneity from the strictly anaerobic sulfate-reducing bacterium D. desulfuricans (Norway 4). Its MW is 43,000, and it is composed of 2 subunits of equal size which are not covalently bound. The enzyme contained Fe by atomic absorption, and the absence of acid-labile S indicates that it is not an Fe-S protein. EPR spectrum revealed that Fe occurs in a high spin ferric form. The UV and visible absorption spectra of the enzyme are presented, as are results of amino-acid analysis. This superoxide dismutase isolated from a strict anaerobe apparently exhibits similar physicochemical properties as compared to the Fe-containing dismutases found in aerobic microorganisms. The significance of the presence of a superoxide dismutase in this strictly anaerobic sulfate reducer is discussed.