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Review
. 2008 Mar;1(2):107-25.
doi: 10.1111/j.1751-7915.2007.00009.x.

Metabolically Engineered Bacteria for Producing Hydrogen via Fermentation

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Free PMC article
Review

Metabolically Engineered Bacteria for Producing Hydrogen via Fermentation

Gönül Vardar-Schara et al. Microb Biotechnol. .
Free PMC article

Abstract

Hydrogen, the most abundant and lightest element in the universe, has much potential as a future energy source. Hydrogenases catalyse one of the simplest chemical reactions, 2H(+) + 2e(-) ↔ H(2), yet their structure is very complex. Biologically, hydrogen can be produced via photosynthetic or fermentative routes. This review provides an overview of microbial production of hydrogen by fermentation (currently the more favourable route) and focuses on biochemical pathways, theoretical hydrogen yields and hydrogenase structure. In addition, several examples of metabolic engineering to enhance fermentative hydrogen production are presented along with some examples of expression of heterologous hydrogenases for enhanced hydrogen production.

Figures

Figure 1
Figure 1
A. Location of the four structural hydrogenase operons on the E. coli K12 chromosome (AC000091) (Hayashi et al., 2006). The values in brackets signify the locations of the respective genes on the genome map.
B. Organization of the genes of each hydrogenase operon in E. coli.Arrows indicate the direction of transcription. For details for each gene see Table 1 (Hayashi et al., 2006).
Figure 2
Figure 2
Fermentative hydrogen production from glucose by E. coli, a well‐studied facultative anaerobic bacterium. Hydrogen is produced through the action of the FHL complex. The maximum theoretical hydrogen yield is 2 mol of H2 per mole of glucose. The glucose metabolic pathway yields succinate, lactate, acetate, ethanol and formate, as fermentation end‐products. The proteins shown in bold with an asterisk have been studied through metabolic engineering in order to enhance the biohydrogen production. PFL, pyruvate formate lyase; FDH, formate dehydrogenase; FHL, formate hydrogen lyase; Hyd, hydrogenase; CoA, coenzyme A.
Figure 3
Figure 3
Fermentative hydrogen production from glucose by C. acetobutylicum, a strict anaerobic bacterium. Hydrogen can be produced through the action of PFOR and NFOR. The maximum theoretical hydrogen yield is 4 mol of H2 per mole of glucose, with acetate or acetone as the fermentation end‐product. The glucose metabolic pathway results in lactate, acetate, ethanol, acetone, butanol and butyrate as fermentation end‐products. The proteins shown in bold with an asterisk have been studied in Clostridium species through metabolic engineering in order to enhance biohydrogen production. G3PDH, glyceraldehyde‐3‐phosphate dehydrogenase; PFOR, pyruvate ferredoxin oxidoreductase; NFOR, NADH:ferredoxin oxidoreductase; NADH, nicotineamide‐adenine dinucleotide; red, reduced.
Figure 4
Figure 4
Three‐dimensional structure of [NiFe]‐hydrogenase from D. gigas(PDB:2FRV). The large subunit which contains the Ni‐Fe catalytic centre is shown in yellow. The small subunit which contains the Fe‐S clusters is shown in blue. Metals and sulfur atoms are depicted as spheres. Colour scheme: nickel is black, carbonmonoxide‐(dicyano) iron is red and Fe‐S cluster is orange.
Figure 5
Figure 5
Structure of the oxidized [NiFe]‐hydrogenase active centre from D. gigas(PDB:2FRV). Colour scheme: nickel is black, iron is orange, oxygen is red, carbon is green and nitrogen is blue.
Figure 6
Figure 6
Structure of the [FeFe]‐hydrogenase active centre from Desulfovibrio desulfuricans ATCC 7757 (PDB:1HFE). The bridging CO that connects both Fe atoms and the water molecule that binds to the Fe atom can be viewed using the structure from C. pasteurianum (PDB:1FEH). Colour scheme is iron is orange, oxygen is red, carbon is green and nitrogen is blue. PDT, 1,3‐propanedithiol.

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