Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7719828 | International Journal of Hydrogen Energy | 2014 | 9 Pages |
Abstract
Biological hydrogen generation from phototrophic organisms is a promising source of renewable fuel. The nuclear-expressed [FeFe] hydrogenase from Chlamydomonas reinhardtii has an extremely high turnover rate, and so has been a target of intense research. Here, we demonstrate that a codon-optimized native hydrogenase can be successfully expressed in the chloroplast. We also demonstrate a curiously strong negative selective pressure resulting from unregulated hydrogenase expression in this location, and discuss management of its expression with a vitamin-controlled gene repression system. To the best of our knowledge, this represents the first example of a nuclear-expressed, chloroplast-localized metalloprotein being synthesized in situ. Control of this process opens up several bioengineering possibilities for the production of biohydrogen.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Electrochemistry
Authors
Kiera Reifschneider-Wegner, Andrey Kanygin, Kevin E. Redding,