Purification and characterization of Fe-containing superoxide dismutase from Methanobrevibacter arboriphilus strain AZ
نویسندگان
چکیده
منابع مشابه
Characterization of a heme-dependent catalase from Methanobrevibacter arboriphilus.
Recently it was reported that methanogens of the genus Methanobrevibacter exhibit catalase activity. This was surprising, since Methanobrevibacter species belong to the order Methanobacteriales, which are known not to contain cytochromes and to lack the ability to synthesize heme. We report here that Methanobrevibacter arboriphilus strains AZ and DH1 contained catalase activity only when the gr...
متن کاملMolecular Cloning and Characterization of Fe-Superoxide Dismutase (Fe-SOD) from the Fern Ceratopteris thalictroides
Ferns are, evolutionarily, in a pivotal position between bryophytes and seed plants (Pryer et al., 2001). Fern gametophytes, like bryophytes, have no vascular system and live on substrate surfaces as small individual plants. However, fern sporophytes do have a vascular system enabling more vertical growth than the gametophytes, and resulting in a larger herbaceous plant form. The origins of pla...
متن کاملPurification and characterization of extracellular superoxide dismutase in mouse lung.
Extracellular superoxide dismutase (EC-SOD) is the major isozyme of SOD in arteries, but is also abundant in lungs. In particular, mouse lungs contain large amounts of EC-SOD compared to lungs in other mammals. This suggests that EC-SOD may have an amplified function in the mouse lung. This study describes the purification and characterization of mouse EC-SOD as well as its localization in mous...
متن کاملSpectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase.
We have compared the active sites of Escherichia coli Fe-substituted (Mn)superoxide dismutase [Fe-sub-(Mn)SOD] and Fe-SOD to elucidate the basis for the inactivity of Fe-sub-(Mn)SOD, despite its apparent similarity to Fe-SOD. The active site of (reduced) Fe2+-sub-(Mn)SOD is qualitatively similar to that of native Fe2+-SOD, indicating similar active site structures and coordination environments ...
متن کاملPurification and properties of superoxide dismutase from Drosophila melanogaster.
The major superoxide dismutase ("slow" electromorph) of the fruit fly, Drosophila melanogaster, has been purified to homogeneity. This enzyme contains 2 Cu2+ and 2 Zn2+/molecule. The ultraviolet absorption spectrum indicates a lack of tryptophan. This enzyme has a molecular weight of 32,000 and is composed of two subunits of equal size, which are joined by noncovalent interactions. Cyanide at 1...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemistry (Moscow)
سال: 2006
ISSN: 0006-2979,1608-3040
DOI: 10.1134/s0006297906040134