
Unit B
Coupled biocatalytic reactions
While the central objective of increasing efficiency and minimizing energy barriers in the respective coupled chemocatalytic processes is already realized in most biocatalytic systems in nature, it ‘only’ needs to be deciphered or recombined in alternative ways.
Thus, our efforts are first directed to understanding in detail natural enzymes, focusing on the catalytic mechanisms and dynamics of multi-functional biocatalysts capable of controlling coupled biocatalytic reactions.
The addressed key questions are how:
- Two catalytic reactions are coordinated at a single active site
- Interfaced catalytic centers allow rapid substrate channeling, sequestering of reactive intermediates, and servicing between active sites
- Complex formation controls electron transfer between enzymes
- These insights can be employed to realize newly designed catalytic systems.
Thus, our studies strive to elucidate the molecular bases of various aspects of catalytic multi-functionality, thereby inspiring research in all Research Units.
A particularly challenging example are bi- and multifunctional carbon monoxide dehydrogenases, in which the catalytic activities of three coupled metal-containing active sites are coordinated in a way that allows the efficient conversion of CO2, CoA, and CH3+ into acetyl-CoA. We will analyze how these centers communicate and their different oxidation/catalytic states trigger conformational changes in order to sequester and channel the one-carbon intermediates.
Keeping electrons at a high energy level between separate oxidative and reductive reactions is a widely employed concept in nature to enable biocatalytic processes. This concept will be explored for O2-tolerant hydrogenases and formate dehydrogenase, and subsequently exploited for coupling these biocatalysts with electron-demanding processes such as CO2 reduction.
Our Challenge
Smart design of engineered electron transfer chains
Team
Bittl, Robert
(Pulsed) EPR spectroscopy
Budisa, Nediljko
Protein modification by non-natural amino acids
Dau, Holger
X-ray spectroscopy, QCL-IR/FTIR
Dobbek, Holger
Enzymology, X-ray crystallography, Fe/S-enzymes
Driess, Matthias
Molecular (heterobimetallic) active site mimics
Hildebrandt, Peter
Raman spectroscopy (surface-sensitive, in situ)
Leimkühler, Silke
Molecular enzymology, molybdoenzymes
Lenz, Oliver
Biochemistry, enzyme engineering, hydrogenases
Limberg, Christian
Model compounds, O2- and CO2-activation
Mroginski, Maria Andrea
Theory (QM/MM, MD)
Müller-Werkmeister, Henrike
(transient) 2D-IR & ultrafast UV-Vis spectroscopy
Neubauer, Peter
Bioprocess engineering, enzyme overproduction
Ray, Kallol
Bioinorganic chemistry, O2 activation
Scheerer, Patrick
X-ray crystallography, XFEL
Spahn, Christian
Cryo electron microscopy
Süssmuth, Roderich
Biochemistry, analytics, lanthipeptide synthetases
Wendler, Petra
Cryo electron microscopy
Wollenberger, Ulla
Protein electrochemistry
Zebger, Ingo
IR spectroscopy (surface-sensitive, in situ)
Zouni, Athina
Biochemistry, X-ray crystallography, XFEL