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Unbiased biocatalytic solar-to-chemical conversion by FeOOH/BiVO4/perovskite tandem structure.

ABSTRACT: Redox enzymes catalyze fascinating chemical reactions with excellent regio- and stereo-specificity. Nicotinamide adenine dinucleotide cofactor is essential in numerous redox biocatalytic reactions and needs to be regenerated because it is consumed as an equivalent during the enzymatic turnover. Here we report on unbiased photoelectrochemical tandem assembly of a photoanode (FeOOH/BiVO4) and a perovskite photovoltaic to provide sufficient potential for cofactor-dependent biocatalytic reactions. We obtain a high faradaic efficiency of 96.2% and an initial conversion rate of 2.4 mM h-1 without an external applied bias for the photoelectrochemical enzymatic conversion of α-ketoglutarate to L-glutamate via L-glutamate dehydrogenase. In addition, we achieve a total turnover number and a turnover frequency of the enzyme of 108,800 and 6200 h-1, respectively, demonstrating that the tandem configuration facilitates redox biocatalysis using light as the only energy source.

SUBMITTER: Lee YW 

PROVIDER: S-EPMC6181951 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Unbiased biocatalytic solar-to-chemical conversion by FeOOH/BiVO<sub>4</sub>/perovskite tandem structure.

Lee Yang Woo YW   Boonmongkolras Passarut P   Son Eun Jin EJ   Kim Jinhyun J   Lee Sahng Ha SH   Kuk Su Keun SK   Ko Jong Wan JW   Shin Byungha B   Park Chan Beum CB  

Nature communications 20181011 1

Redox enzymes catalyze fascinating chemical reactions with excellent regio- and stereo-specificity. Nicotinamide adenine dinucleotide cofactor is essential in numerous redox biocatalytic reactions and needs to be regenerated because it is consumed as an equivalent during the enzymatic turnover. Here we report on unbiased photoelectrochemical tandem assembly of a photoanode (FeOOH/BiVO<sub>4</sub>) and a perovskite photovoltaic to provide sufficient potential for cofactor-dependent biocatalytic r  ...[more]

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