Phosphorylating respiratory membranes from Azotobacter vinelandii
نویسندگان
چکیده
منابع مشابه
Genes 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 کاملIron Core from Azotobacter vinelandii Bacterial Ferritin
Bacterial ferritin from Azotobacter vinelandii (AvBFJ has a function in H2 uptake. The Fe3+ reduction on the surface of the iron core from AvBF0 is accompanied simultaneously by H2 uptake, with a maximum activity of H2 uptake of 450 H2/AvBF0. A reduction potential of -402 mV for iron reduction on the surface of the core is found. A shift to the red the protein absorbance peaks ranging from 280 ...
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 کاملucture 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...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1970
ISSN: 0306-3283
DOI: 10.1042/bj1160021pa