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Frankia KB5 possesses a hydrogenase immunologically related to membrane-bound [NiFe]-hydrogenases
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0002-0536-903X
2001 (English)In: Current Microbiology, ISSN 0343-8651, E-ISSN 1432-0991, Vol. 42, no 6, 438-441 p.Article in journal (Refereed) Published
Abstract [en]

The immunological relationship of the hydrogenase in Frankia KB5 to hydrogenases in other microorganisms was investigated using antisera raised against holo-[NiFe]-hydrogenases isolated from Alcaligenes latus, Azotobacter vinelandii, Ralstonia eutropha, and the small and large hydrogenase subunits from Bradyrhizobium japonicum. The antisera raised against the A. latus, R. eutropha, and B. japonicum (large subunit) polypeptides were found to recognize two polypeptides, corresponding to the unprocessed and processed forms of the hydrogenase subunit in Frankia KB5. None of the antisera, including the antibodies produced against the small hydrogenase subunit isolated from B. japonicum, recognized any polypeptide related to the small hydrogenase subunit in Frankia KB5. An immunogold localization study of the intracellular distribution of hydrogenase in Frankia KB5, with the cryo-section technique, showed that labeling in the membrane of both hyphae and vesicles was positively correlated with hydrogenase activity.

Place, publisher, year, edition, pages
2001. Vol. 42, no 6, 438-441 p.
URN: urn:nbn:se:umu:diva-44759ISI: 000168466100013OAI: diva2:424366
Available from: 2011-06-17 Created: 2011-06-09 Last updated: 2015-04-29

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Sellstedt, Anita
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