Reversible inactivation of the O2-labile hydrogenases from Azotobacter vinelandii and Rhizobium japonicum.
نویسندگان
چکیده
منابع مشابه
ucture of the bacterioferritin from Azotobacter vinelandii
The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a d...
متن کاملPlasmids of Azotobacter vinelandii.
Four laboratory strains and two isolates of Azotobacter vinelandii were found to contain plasmids. Twenty-five laboratory strains which could fix nitrogen did not have free, covalently closed circular plasmid DNA. The plasmids varied in size from 9 to 52 megadaltons, and each strain yielded only one plasmid. No discernible differences in ability to fix nitrogen were found between plasmid-bearin...
متن کاملUltrastructure of Azotobacter vinelandii.
Vegetative cells and cysts of Azotobacter vinelandii 12837 were prepared for electron microscopy by several methods assumed to preserve structural details destroyed by techniques previously reported in the literature. Examination of large numbers of cells and cysts by these methods revealed four structural details not reported previously: intine fibrils, intine vesicles, intine membrane, and mi...
متن کاملGenes in Azotobacter vinelandii
Azotobacter vinelandii contains a heterodimeric, membrane-bound [NiFelhydrogenase capable of catalyzing the reversible oxidation of H2. The 13 and at subunits of the enzyme are encoded by the structural genes hoxK and hoxG, respectively, which appear to form part of an operon that contains at least one further potential gene (open reading frame 3 1ORF3]). In this study, determination of the nuc...
متن کاملCytochrome c oxidase from Azotobacter vinelandii.
Although the terminal respiratory chain of Azotobacter has been the subject of several recent studies, the nature of the cytochrome oxidase portion is still somewhat obscure. Repaske (1) partially purified and characterized a soluble succinic dehydrogenase and succinoxidase system from Azotobacter z&elan&i. Wilson and Wilson (2) studied the soluble succinoxidase in Repaske’s preparation and dem...
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: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)67440-x