Efficient hydrogen‐dependent carbon dioxide reduction by Escherichia coli.

Magali Roger, Fraser Brown, William Gabrielli, Frank Sargent (Lead / Corresponding author)

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Abstract

Hydrogen‐dependent reduction of carbon dioxide to formic acid offers a promising route to greenhouse gas sequestration; carbon abatement technologies; hydrogen transport and storage; and the sustainable generation of renewable chemical feedstocks [1]. The most common approach to performing direct hydrogenation of CO2 to formate is to use chemical catalysts in homogeneous or heterogeneous reactions [2]. An alternative approach is to use the ability of living organisms to perform this reaction biologically. However, although CO2 fixation pathways are widely distributed in nature, only a few enzymes have been described that have the ability to perform the direct hydrogenation of CO2 [3‐5]. The formate hydrogenlyase (FHL) enzyme from Escherichia coli normally oxidises formic acid to carbon dioxide and couples that reaction directly to the reduction of protons to molecular hydrogen [6]. In this work, the reverse reaction of FHL is unlocked. It is established that FHL can operate as a highly efficient hydrogen‐dependent carbon dioxide reductase when gaseous CO2 and H2 are placed under pressure (up to 10 bar). Using intact whole cells, the pressurised system was observed to rapidly convert 100% of gaseous CO2 to formic acid and >500 mM formate was observed to accumulate in solution. Harnessing the reverse reaction has the potential to allow the versatile E. coli system to be employed as an exciting new carbon capture technology, or as a cell factory dedicated to formic acid production, which is a commodity in itself as well as a feedstock for the synthesis of other valued chemicals.
Original languageEnglish
Pages (from-to)140-145.e2
Number of pages8
JournalCurrent Biology
Volume28
Issue number1
Early online date28 Dec 2017
DOIs
Publication statusPublished - 8 Jan 2018

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Keywords

  • Escherichia coli
  • carbon capture
  • carbon dioxide
  • formate chemosynthesis
  • formate dehydrogenase
  • formate hydrogenase
  • hydrogenase

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