A hydrogen-evolving enzyme is present in Frankia sp. R43
FEMS Microbiology Letters, ISSN: 0378-1097, Vol: 236, Issue: 2, Page: 235-240
2004
- 9Citations
- 15Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations9
- Citation Indexes9
- CrossRef4
- Captures15
- Readers15
- 14
Article Description
The ability to evolve hydrogen using methyl viologen as an electron donor was assayed in the nitrogen-fixing actinomycetes Frankia sp. R43 and Frankia sp. KB5. To further examine the nature of hydrogen-evolving enzymes that may be present in these organisms immunological studies were performed. Under anaerobic conditions (both nitrogen-limiting and nitrogen-containing) Frankia sp. R43 but not Frankia sp. KB5 evolved hydrogen,which was not linked to NAD-reducing activity. Immunological analysis of total protein from Frankia sp. R43 and Frankia sp. KB5 using an antiserum raised against Ralstonia eutropha HoxF, recognized an antigen in Frankia sp. R43 but not in Frankia sp. KB5. Immunogold labeling using antibodies raised against the R. eutropha HoxH recognized sites in both hyphae and vesicles of Frankia sp. R43, but not in Frankia sp. KB5. Based on these physiological and immunological findings, we conclude that Frankia sp. R43 has a hydrogen-evolving hydrogenase.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0378109704004021; http://dx.doi.org/10.1016/j.femsle.2004.05.049; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=3142566435&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15251202; https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.2004.tb09652.x; http://dx.doi.org/10.1111/j.1574-6968.2004.tb09652.x; http://doi.wiley.com/10.1016/j.femsle.2004.05.049; https://dx.doi.org/10.1111/j.1574-6968.2004.tb09652.x; https://academic.oup.com/femsle/article-abstract/236/2/235/536086?redirectedFrom=fulltext; https://dx.doi.org/10.1016/j.femsle.2004.05.049
Oxford University Press (OUP)
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