Photocatalytic chemical
synthesis by coupling abiotic photosensitizers
to purified enzymes provides an effective way to overcome the low
conversion efficiencies of natural photosynthesis while exploiting
the high catalytic rates and selectivity of enzymes as renewable,
earth-abundant electrocatalysts. However, the selective synthesis
of multiple products requires more versatile approaches and should
avoid the time-consuming and costly processes of enzyme purification.
Here we demonstrate a cell-based strategy supporting light-driven
H2 evolution or the hydrogenation of CC and CO
bonds in a nonphotosynthetic microorganism. Methylviologen shuttles
photoenergized electrons from water-soluble photosensitizers to enzymes
that catalyze H2 evolution and the reduction of fumarate,
pyruvate, and CO2 in Shewanella oneidensis. The predominant reaction is selected by the experimental conditions,
and the results allow rational development of cell-based strategies
to harness nature’s intrinsic catalytic diversity for selective
light-driven synthesis of a wide range of products.
Edited by Ruma BanerjeeThe enzymes of the thiosulfate dehydrogenase (TsdA) family are wide-spread diheme c-type cytochromes. Here, redox carriers were studied mediating the flow of electrons arising from thiosulfate oxidation into respiratory or photosynthetic electron chains. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, the tsdA gene is immediately preceded by tsdB encoding for another diheme cytochrome. Spectrophotometric experiments in combination with enzymatic assays in solution showed that TsdB acts as an effective electron acceptor of TsdA in vitro when TsdA and TsdB originate from the same source organism. Although TsdA covers a range from ؊300 to ؉150 mV, TsdB is redox active between ؊100 and ؉300 mV, thus enabling electron transfer between these hemoproteins. The three-dimensional structure of the TsdB-TsdA fusion protein from the purple sulfur bacterium Marichromatium purpuratum was solved by X-ray crystallography to 2.75 Å resolution providing insights into internal electron transfer. In the oxidized state, this tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Interestingly, thiosulfate is covalently bound to Cys 330 on heme 3. In several bacteria, including Allochromatium vinosum, TsdB is not present, precluding a general and essential role for electron flow. Both AvTsdA and the MpTsdBA fusion react efficiently in vitro with high potential iron-sulfur protein from A. vinosum (E m ؉350 mV). High potential ironsulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains.
The decahaem cytochrome MtrC from Shewanella oneidensis MR-1 was employed as a protein electron conduit between a porous indium tin oxide electrode and redox enzymes. Using a hydrogenase and a fumarate reductase, MtrC was shown as a suitable and efficient diode to shuttle electrons to and from the electrode with the MtrC redox activity regulating the direction of the enzymatic reactions.
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