These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Electron pathways involved in H(2)-metabolism in the green alga Scenedesmus obliquus.
    Author: Wünschiers R, Senger H, Schulz R.
    Journal: Biochim Biophys Acta; 2001 Jan 19; 1503(3):271-8. PubMed ID: 11115639.
    Abstract:
    The green alga Scenedesmus obliquus is capable of both uptake and production of H(2) after anaerobic adaptation (photoreduction of CO(2) or photohydrogen production). The essential enzyme for H(2)-metabolism is a NiFe-hydrogenase with a [2Fe-2S]-ferredoxin as its natural redox partner. Western blot analysis showed that the hydrogenase is constitutively expressed. The K(m) values were 79.5 microM and 12.5 microM, determined with ferredoxin and H(2), respectively, as electron donor for the hydrogenase. In vitro, NADP(+) was reduced by H(2) in the presence of the hydrogenase, the ferredoxin and a ferredoxin-NADP reductase. From these results and considerations on the stoichiometry we propose that this light-independent electron transfer is part of the photoreduction of CO(2) in vivo. For ATP synthesis, necessary for the photoreduction of CO(2), light-dependent cyclic electron transfer around Photosystem (PS) I accompanies this 'dark reaction'. PS II fluorescence data suggest that (a) in S. obliquus H(2)-reduction might function as the anaerobic counterpart of the O(2)-dependent Mehler reaction, and (b) the presence of either a ferredoxin quinone-reductase or NAD(P)-dehydrogenase (complex I) in S. obliquus chloroplasts.
    [Abstract] [Full Text] [Related] [New Search]