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

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Budisa,  Nediljko
Protein modification by non-natural amino acids

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Dau, Holger
X-ray  spectroscopy,  QCL-IR/FTIR

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Dobbek, Holger
Enzymology, X-ray crystallography, Fe/S-enzymes

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Driess, Matthias
Molecular (heterobimetallic) active site mimics

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Hildebrandt, Peter
Raman spectroscopy (surface-sensitive, in situ)

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Leimkühler, Silke
Molecular enzymology, molybdoenzymes

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Lenz,  Oliver
Biochemistry, enzyme engineering, hydrogenases

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Limberg, Christian
Model compounds, O2- and CO2-activation

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Mroginski, Maria Andrea
Theory (QM/MM, MD)

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Müller-Werkmeister, Henrike
(transient) 2D-IR & ultrafast UV-Vis spectroscopy

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Neubauer,  Peter
Bioprocess engineering, enzyme overproduction

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Ray, Kallol
Bioinorganic chemistry, O2 activation

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Scheerer, Patrick
X-ray crystallography, XFEL

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Spahn, Christian
Cryo electron microscopy

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Süssmuth, Roderich
Biochemistry, analytics, lanthipeptide synthetases

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Wendler, Petra
Cryo electron microscopy

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Wollenberger, Ulla
Protein electrochemistry

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Zebger, Ingo
IR spectroscopy (surface-sensitive, in situ)

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Zouni, Athina
Biochemistry, X-ray crystallography, XFEL

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Contact Unit B

Prof. Dr. Holger Dobbek
HU Berlin
Department of Biology
Philippstraße 13
10115 Berlin
+49 (0)30 2093-6369
holger.dobbek(at)biologie.hu-berlin.de

Prof. Dr. Silke Leimkühler
U Potsdam
Department of Biology and Biochemistry
Karl-Liebknecht-Straße 24–25
14476 Potsdam-Golm
+49 (0)331 977-5603
sleim(at)uni-potsdam.de