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.
Original language | English (US) |
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Pages (from-to) | 3657-3665 |
Number of pages | 9 |
Journal | International Journal of Hydrogen Energy |
Volume | 39 |
Issue number | 8 |
DOIs | |
State | Published - Mar 6 2014 |
Keywords
- Chlamydomonas
- Chloroplast
- Gene expression
- Green algae
- [FeFe] hydrogenase
ASJC Scopus subject areas
- Renewable Energy, Sustainability and the Environment
- Fuel Technology
- Condensed Matter Physics
- Energy Engineering and Power Technology