H2 metabolism in photosynthetic bacteria and relationship to N2 fixation.
The photosynthetic bacteria can evolve H2 in the light through a nitrogenase-mediated reaction. The nitrogenase enzyme in the photosynthetic bacteria is similar to other nitrogenases. It is made of two soluble components: a) the Fe protein (dinitrogenase reductase or Component II) which receives electrons from ferredoxin, and b) the Mo-Fe protein (dinitrogenase or Component I) on which the substrates (including protons) are reduced. In photosynthetic bacteria, the physiological regulation of nitrogenase activity involves inactivation by covalent modification of the nitrogenase Fe protein. This inactivation can be reversed by an activating factor (or activating enzyme) which is an extrinsic membrane protein. After an ammonia shock, both the Fe protein of nitrogenase, and the glutamine synthetase, become adenylylated in vivo. In the adenylylation state, glutamine synthetase has AMP moieties bound to the protein by phosphate linkage. In toluene-treated cells of Rhodopseudomas capsulata preincubated with radioactive ATP, labelled either by 14C on the adenine or by 32P on the P alpha of ATP and then submitted to an ammonia shock, the Fe protein becomes covalently labelled only with [14C]ATP ad not with [32P]alpha ATP, while glutamine synthetase becomes labelled with both radioactive ATP molecules. This indicates that a different type of linkage is involved in the binding of the modifying group to Fe protein and to glutamine synthetase. Like other N2 fixers, the photosynthetic bacteria also contain a hydrogenase. In R. capsulata, the hydrogenase is an intrinsic membrane protein which protrudes in the cytoplasmic space and is not accessible to anti-hydrogenase antibodies from the periplasmic side. The hydrogenase can transfer electrons from H2 to the electron transport chain. It functions physiologically as an uptake-hydrogenase and may contribute to the recycling of electrons to nitrogenase. In the presence of excess carbon compounds, its main role may be to maintain an anaerobic microenvironment for the nitrogenase. Ferredoxin has been isolated from photosynthetic bacteria. Rhodospirillum rubrum and Rhodopseudomonas capsulata each contain two different soluble ferredoxin molecules. Reduced Fd I from R. capsulata has been shown to donate its electrons to nitrogenase.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000641:Ammonia / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology / Q000378:metabolism*; D004579:Electron Transport; D005288:Ferredoxins / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D006859:Hydrogen / Q000378:metabolism*; D006864:Hydrogenase; D008027:Light; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism; D010100:Oxygen / Q000494:pharmacology; D010788:Photosynthesis; D012241:Rhodopseudomonas / Q000201:enzymology / Q000378:metabolism*; D012247:Rhodospirillum rubrum / Q000378:metabolism
D005288:Ferredoxins; D000641:Ammonia; D006859:Hydrogen; D000255:Adenosine Triphosphate; D010088:Oxidoreductases; D006864:Hydrogenase; D009591:Nitrogenase; D005974:Glutamate-Ammonia Ligase; D010100:Oxygen