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Semiartificial CO₂ Fixation Using Metal-Dependent Formate Dehydrogenase.

Yongpeng Liu¹, Beverly Q L Low¹, William E Robinson²

¹Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

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Summary

Semiartificial photosynthesis uses enzymes like formate dehydrogenases (Fdhs) with synthetic components to convert carbon dioxide (CO2) into formate using solar energy. This review explores metal-dependent Fdhs in biohybrid systems for efficient solar fuel production.

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Area of Science:

Biohybrid systems
Solar chemistry
Enzymology

Background:

Semiartificial photosynthesis combines synthetic light absorbers with biological catalysts for solar energy conversion.
Formate dehydrogenases (Fdhs) are key enzymes for converting carbon dioxide (CO2), protons, and electrons into formate, a crucial metabolic intermediate.

Purpose of the Study:

To review the use of metal-dependent formate dehydrogenases (Fdhs) in semiartificial photosynthesis.
To highlight advancements in biohybrid systems for CO2-to-formate conversion.
To guide future research at the intersection of enzymology, photo(electro)chemistry, and materials science.

Main Methods:

Examination of structural, mechanistic, and redox properties of molybdenum- and tungsten-dependent Fdhs.
Analysis of biotic-abiotic interfaces in functional biohybrid systems.
Review of (photo)electrochemical and photochemical systems utilizing Fdhs for CO2 fixation.

Main Results:

Metal-dependent Fdhs are effectively wired to electrodes and synthetic light absorbers in semiartificial photosynthesis.
Advanced interfacial characterization techniques are crucial for optimizing enzyme loading and charge carrier dynamics.
Significant progress has been made in CO2-to-formate conversion using Fdhs as model catalysts.

Conclusions:

Semiartificial photosynthesis with Fdhs offers a promising route for solar chemistry and CO2 utilization.
Understanding and engineering biotic-abiotic interfaces is critical for efficient biohybrid system performance.
Further research is needed to overcome challenges in enzyme stability and system integration for practical applications.