Journal
ACS CATALYSIS
Volume 8, Issue 8, Pages 7251-7260Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.8b01806
Keywords
CO2; reduction; mesoporous silica; biocatalysis; Forster resonance energy transfer; carbocyanine dyes; labeled protein
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Funding
- Swedish Research Council (VR) as a part of the Linnaeus Centre for Bioinspired Supramolecular Function and Design-SUPRA
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By combining two enzymes, formate dehydrogenase (FateDH) and formaldehyde dehydrogenase (FaldDH), it is possible to drive the thermodynamically unfavorable conversion of CO2 to formaldehyde. For this purpose, the enzymes were coimmobilized in siliceous mesostructured cellular foams (MCFs). A high degree of adsorption of both enzymes was achieved by coimmobilizing the enzymes sequentially, i.e., first FateDH and then FaldDH. The highest conversion rate was obtained with an enzyme mass ratio of 1:15 (FateDH/FaldDH). Using MCF functionalized with mercaptopropyl groups (MCF-MP), the activity increased similar to 4 times compared to the enzymes free in solution. To probe the distance between the two enzymes, they were separately labeled with either Cy3 or Cy5 dyes and studied with Forster resonance energy transfer (FRET). An increased energy transfer was observed when the enzymes were coimmobilized in MCF-MP, suggesting that the two enzymes are in close proximity, resulting in higher conversion of CO2 to formaldehyde.
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