Transcription of the Hydrogenase Gene during H2 Production in Scenedesmus Obliquus and Chlorella Vulgaris

There is ongoing research related to the production of molecular hydrogen today and algae have proven to be good biological models for producing several compounds of interest. We analyzed how genetic variations in hydrogenase genes (hyd) can affect the production of molecular hydrogen in the algae Chlorella vulgaris and Scenedesmus obliquus. Through isolation and genetic characterization of hyd genes in S. obliquus and C. vulgaris, we made in-silico 3D modeling of the hydrogenase proteins and compared these in 11 algal genera. The 3D structure of hydrogenases indicated its structural conservation in 10 genera of algae, and the results of our grouping according to the aa characteristics of the proteins showed the formation of two groups, which were unrelated to the algae’s phylogenetic classification. By growing C. vulgaris and S. obliquus in anaerobic conditions (in darkness) during 24 h and after exposing the cultures to light, we observed H2 production values of 9.0 ± 0.40 mL H2/L and 16 ± 0.50 mL H2/L, respectively. The highest global relative expression of hyd genes was reached during the first 30 min of exposure to light. The behavior of the expression of the hyd genes in these species of algae proved to be species specific and involved in the production of H2. Future identification of isoforms of hyd genes in algae would allow a better understanding of the regulation of the hydrogenase enzyme.

Unraveling the mechanism of biomimetic hydrogen fuel production – a first principles molecular dynamics study

The Fe2(bdt)(CO)6 [bdt = benzenedithiolato] complex, a synthetic mimic of the [FeFe] hydrogenase enzyme can electrochemically convert protons into molecular hydrogen. The free energy landscape reveals a different mechanism for the biomimetic cycle.

Optimizing electron transfer from CdSe QDs to hydrogenase for photocatalytic H2 production

A series of viologen related redox mediators of varying reduction potential has been characterized and their utility as electron shuttles between CdSe quantum dots and hydrogenase enzyme has been demonstrated.

Models of the iron-only hydrogenase enzyme: structure, electrochemistry and catalytic activity of Fe2(CO)3(μ-dithiolate)(μ,κ1,κ2-triphos)

A series of Fe2(triphos)(CO)3(μ-dithiolate) complexes have been prepared and studied as models of the diiron centre in [FeFe]-hydrogenases.