This project aims at exploring novel innovative ways of biologically-inspired CO2-fixation, with the ultimate goal to convert the «waste product» and greenhouse gas CO2 into organic compounds that can be used as building blocks in biotechnology, synthetic chemistry, and pharmaceutical industry.
For that purpose, a recently discovered CO2-fixing enzyme («biocatalyst») and its close relatives will be systematically investigated in respect to substrate and reaction specificity to identify crucial parts of these enzymes that are important for CO2-binding and catalysis.
Directed mutation of these catalytic sites and transplantation onto other protein scaffolds will allow to modify the reaction products and to transfer the feature of CO2-fixation also on other enzymes. In consequence, novel products and «designer enzymes» will be created that open up new biotechnological and applied perspectives for society and industry.
What is special about the project?
Although highly desired, enzyme-based processes that allow the conversion of the waste gas CO2 into value-added compounds under ambient conditions are limited up to now by the availability of suitable CO2-fixing enzymes. Thus, our approach will break new grounds by systematically exploring and expanding the spectrum of CO2-fixing biocatalysts for sustainable green chemistry and biotechnology.
With its funding, the Gebert Rüf Stiftung supports a project of true pioneering character that is located at the interface of fundamental sciences and applicability, and that aims at providing novel, unorthodox solutions to the challenge of raising CO2 concentrations in the atmosphere.
In the first part of the project a substrate library and a mass spectrometric analytics platform were established that allow to screen for novel CO2-fixation reactions in medium to high throughput fashion. We used this analytical platform to characterize 40 novel CO2-fixing enzymes in collaboration with the Joint Genome Institute of the US Department of Energy. This allowed us to identify novel CO2-fixation reactions.
In the second part of the project we investigated the molecular basis of substrate specificity in these CO2-fixing enzymes. By changing the active site of these enzymes with mutagenesis, we could create CO2-fixing enzymes of improved activity and extend the substrate spectrum.
In summary we were able to identify and create a set of highly active CO2-fixing enzymes that allow us to produce 18 different chemical building blocks for the chemical industry, biotechnology and synthetic biology.
Peter, D., Vögeli, B., Cortina, N.S., and *Erb, T.J. (2016) A chemo-enzymatic road map to the synthesis of CoA esters. Molecules 21:E157;
Peter, D., Schada von Borzyskowski, L., Kiefer, P., Christen, P., Vorholt, J.A., and *Erb, T.J. (2015) Screening and engineering the synthetic potential of carboxylating reductases from central metabolism and polyketide biosynthesis. Angewandte Chemie International Edition 45:13457-13461;
Publikationen in Vorbereitung:
Peter, D., Stoffel, G., Schada von Borzyskowski, L., Vögeli, B., and *Erb, T.J. A systems biochemical study of enoyl-CoA carboxylases/reductases identifies evolutionary pressures driving efficient CO2 fixation;
Vögeli, B., Peter, D., Benkstein S., Gerlinger, P., and *Erb, T.J. A proofreading in vitro system for the generation and incorporation of alkylmalonyl-Coenzyme A esters into polyketides.
Persons involved in the project
Last update to this project presentation 17.10.2018