Ulrich Ermler – Enzyme Mechanism

We are focused on the enzyme structure-based analysis of challenging biochemical processes in anaerobic biomass degradation.

Figure: a) F420 dependent [Ni,Fe] hydrogenase (Frh) in colloboration with S. Shima and R.K. Thauer, Marburg. b) Electron-transferring flavoprotein/butyryl-CoA dehydrogenase with W. Buckel, Marburg. c) Catalytic fragment of type II benzoyl-CoA reductase with M. Boll, Freiburg. d) Molybdenum storage protein with K. Schneider, Bielefeld. — Figure: a) F₄₂₀ dependent [Ni,Fe] hydrogenase (Frh) in colloboration with S. Shima and R.K. Thauer, Marburg. b) Electron-transferring flavoprotein/butyryl-CoA dehydrogenase with W. Buckel, Marburg. c) Catalytic fragment of type II benzoyl-CoA reductase with M. Boll, Freiburg. d) Molybdenum storage protein with K. Schneider, Bielefeld.

Figure: a) F₄₂₀ dependent [Ni,Fe] hydrogenase (Frh) in colloboration with S. Shima and R.K. Thauer, Marburg. b) Electron-transferring flavoprotein/butyryl-CoA dehydrogenase with W. Buckel, Marburg. c) Catalytic fragment of type II benzoyl-CoA reductase with M. Boll, Freiburg. d) Molybdenum storage protein with K. Schneider, Bielefeld.

Our research is focussed on structural biology primarily based on X-ray crystallography as a method for structure determination. We are predominantly interested in proteins involved in the (anaerobic) degradation of biomass, in particular, on those of methanogenic, fermenting and inert aliphatic and aromatic hydrocarbon metabolising pathways. The investigated enzymes catalyse challenging biochemical reactions with novel mechanisms, chemically driven ion-translocations across the cell membrane and flavin-based electron bifurcation processes in which the production of energy-rich reduced ferredoxins is coupled with exergonic reduction reactions. Furthermore, we are, in general, interested in the structure of (unusual) organic or metallic cofactors, their formation, and their function in cooperation with the polypeptide. As an example, four protein structures are given in the figure on the left.

Selected Publications

Huang G., Wagner T., Wodrich M.D., Ataka K., Bill K.E., Ermler U., Hu X., Shima S.

The atomic-resolution crystal structure of activated [Fe]-hydrogenase

Nature Catalysis 2, 537–543 (2019).

DOI

Demmer J.K., Bertsch J., Öppinger C., Wohlers H., Kayastha K., Demmer U., Ermler U., Müller V.

Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction.

FEBS Lett. 592, 332-342 (2018).

DOI

Demmer J.K., Pal Chowdhury N., Selmer T., Ermler U., Buckel W.

The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile.

Nat Commun. 8,1577, (2017).

DOI

Wagner T., Koch J., Ermler U., Shima S.

Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction.

Science 357, 699-703, (2017).

DOI

Weidenweber S., Schühle K., Demmer U., Warkentin E., Ermler U., Heider J.

Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases.

Sci Rep. doi: 10.1038/srep39674 (2017).

DOI