Characterization of the predominant Azotobacter vinelandii envelope protein
نویسندگان
چکیده
منابع مشابه
Plasmids 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 کاملCrystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.
The nitrogenase enzyme system catalyzes the ATP (adenosine triphosphate)-dependent reduction of dinitrogen to ammonia during the process of nitrogen fixation. Nitrogenase consists of two proteins: the iron (Fe)-protein, which couples hydrolysis of ATP to electron transfer, and the molybdenum-iron (MoFe)-protein, which contains the dinitrogen binding site. In order to address the role of ATP in ...
متن کاملUnique features of the nitrogenase VFe protein from Azotobacter vinelandii.
Nitrogenase is an essential metalloenzyme that catalyzes the biological conversion of dinitrogen (N(2)) to ammonia (NH(3)). The vanadium (V)-nitrogenase is very similar to the "conventional" molybdenum (Mo)-nitrogenase, yet it holds unique properties of its own that may provide useful insights into the general mechanism of nitrogenase catalysis. So far, characterization of the vanadium iron (VF...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1981
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.146.1.398-403.1981