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Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans*
Kinetic, structural, and spectral data revealed a detailed picture of the bifurcation process, which enables anaerobic bacteria and archaea to reduce the low-potential [4Fe-4S] clusters of ferredoxin, which increases the efficiency of the substrate level and electron transport phosphorylations.
Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically
An X-ray structure of the 280 kDa heterohexameric ANME-1 MCR complex is reported, indicating the same substrates for MCR from methanotrophic and methanogenic archaea.
Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway.
- Ingo Rekittke, J. Wiesner, U. Ermler
- ChemistryJournal of the American Chemical Society
- 24 December 2008
The structure of Aquifex aeolicus LytB is presented, which adopts a cloverleaf or trefoil-like structure with each monomer in the dimer containing three alpha/beta domains surrounding a central [Fe3S4] cluster ligated to Cys13, Cys96, and Cys193.
Structural, Biochemical and Genetic Characterization of Dissimilatory ATP Sulfurylase from Allochromatium vinosum
The purple bacterial sat-encoded ATP sulfurylase from the sulfur-oxidizing purple sulfur bacterium Allochromatium vinosum is produced as a recombinant protein in E. coli, crucial kinetic parameters are determined and a crystal structure in an open state with a ligand-free active site is obtained.
Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme a dehydrogenases.
- S. Wischgoll, U. Demmer, E. Warkentin, R. Günther, M. Boll, U. Ermler
- 29 June 2010
The interaction between the glutaconyl carboxylate and the guanidinium group of a conserved arginine is stronger in GDH(Des) than in the decarboxylating human GDH (longer and monodentate hydrogen bond), which is corroborated by molecular dynamics studies.
Structure of the ATPase subunit CysA of the putative sulfate ATP‐binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius
Structure of the E‐1‐hydroxy‐2‐methyl‐but‐2‐enyl‐4‐diphosphate synthase (GcpE) from Thermus thermophilus
Structure of the (E)‐4‐hydroxy‐3‐methyl‐but‐2‐enyl‐diphosphate reductase from Plasmodium falciparum
Active site analysis of yeast flavohemoglobin based on its structure with a small ligand or econazole
- Emna El Hammi, E. Warkentin, U. Demmer, N. Marzouki, U. Ermler, L. Baciou
- BiologyThe FEBS journal
- 1 December 2012
Yeast Yhb and Ralstonia eutropha flavoHb both structurally studied in complex with econazole indicate conformational differences between the inhibitors and the polypeptide primarily caused by stable binding of a phospholipid to the latter and by distinct loop D structures.
Structure of Ralstonia eutropha flavohemoglobin in complex with three antibiotic azole compounds.
The ligand-induced open-to-closed transition involves a reorientation of the NADH domain accompanied by conformational changes in the C-terminal arm, helix E, and the CE loop resulting in an encapsulation of the heme-binding pocket.