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Abstract
The unicellular cyanobacterium Synechocystis sp. strain PCC 6803 contains a single bidirectional NiFe-Hox-hydrogenase, which evolves hydrogen under certain environmental conditions. The nitrate assimilation pathway is a potential competing pathway that may reduce the electron flow to the hydrogenase and thereby limit hydrogen production. To improve H 2 production, the nitrate assimilation pathway was disrupted by genetic engineering to redirect the electron flow towards the Hox-hydrogenase. Mutant strains disrupted in either nitrate reductase (Δ narB) or nitrite reductase (Δ nirA) or both nitrate reductase and nitrite reductase (Δ narB:Δ nirA) were constructed and tested for their ability to produce hydrogen. H 2 production and Hox-hydrogenase activities in all the mutant strains were higher than those in wild-type. Highest H 2 production was observed in the Δ narB:Δ nirA strain. Small changes were observed for Hox-hydrogenase enzyme activities and only minor changes in transcript levels of hoxH and hoxY were not correlated with H 2 production. The results suggest that the high rate of H 2 production observed in the Δ narB:Δ nirA strain of the cyanobacterium Synechocystis sp. strain PCC 6803 is the result of redirecting the electron supply from the nitrate assimilation pathway, through genetic engineering, towards the Hox-hydrogenase.
Published Version
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