PORTFOLIO
Project presentations on the website
Every project supported by Gebert Rüf Stiftung is made accessible with a web presentation that informs about the core data of the project. With this public presentation, the foundation publishes the funding results achieved and contributes to the communication of science to society.
Exploring Novel Catalysts for CO2-Fixation
Editorial
Für den Inhalt der Angaben zeichnet die Projektleitung verantwortlich.
Cooperation
Dieses von der Gebert Rüf Stiftung geförderte Projekt wird von folgenden weiteren Projektpartnern mitgetragen: Institute of Microbiology, ETH Zurich; Laboratory of Organic Chemistry, ETH Zurich.
Project data
- Project no: GRS-062/12
- Amount of funding: CHF 205'000
- Approved: 24.01.2013
- Duration: 07.2013 - 03.2017
- Area of activity: Pilotprojekte, 1998 - 2018
Project management
- Dr. Tobias J. Erb, Junior-Group Leader
- ETH Zürich
- Instiute of Microbiology
- Wolfgang-Pauli Str. 10
- 8093 Zürich (Schweiz)
- toerb@mpi-marburg.mpg.de
Project description
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.
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.
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.
Status/Results
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.
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.
Publications
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.
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.
Links
Persons involved in the project
Institute of Microbiology, ETH Zurich
Dr. Tobias J. Erb
Dominik M. Peter
Prof. Julia Vorholt
Dr. Patrick Kiefer
Laboratory for Organic Chemistry, ETH Zurich
Dr. Marc-Olivier Ebert
Dr. Tobias J. Erb
Dominik M. Peter
Prof. Julia Vorholt
Dr. Patrick Kiefer
Laboratory for Organic Chemistry, ETH Zurich
Dr. Marc-Olivier Ebert
Last update to this project presentation 18.10.2023