Publikationen von Ulrich Ermler
Alle Typen
Zeitschriftenartikel (146)
81.
Zeitschriftenartikel
329 (5989), S. 327 - 330 (2010)
The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping. Science 82.
Zeitschriftenartikel
D66 (7), S. 850 - 854 (2010)
Structure at 1.5 Å resolution of cytochrome c552 with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen) 83.
Zeitschriftenartikel
49 (25), S. 5350 - 5357 (2010)
Structural Basis for Promoting and Preventing Decarboxylation in Glutaryl-Coenzyme A Dehydrogenases. Biochemistry 84.
Zeitschriftenartikel
78 (5), S. 1073 - 1083 (2010)
A new structure-based classification of sulfide:quinone oxidoreductases. Proteins: Structure, Function, and Bioinformatics 85.
Zeitschriftenartikel
61 (1-2), S. 47 - 49 (2009)
Cyclohexane-1,2-dione hydrolase: A new tool to degrade alicyclic compounds. Journal of Molecular Catalysis B: Enzymatic 86.
Zeitschriftenartikel
49 (42), S. 10098 - 10105 (2009)
Structural Basis of the Hydride Transfer Mechanism in F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase. Biochemistry 87.
Zeitschriftenartikel
48 (35), S. 6457 - 6460 (2009)
The Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H2 Activation. Angewandte Chemie, International Edition in English 88.
Zeitschriftenartikel
106 (24), S. 9625 - 9630 (2009)
The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proceedings of the National Academy of Sciences of the United States of America 89.
Zeitschriftenartikel
583 (3), S. 585 - 590 (2009)
The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Letters 90.
Zeitschriftenartikel
321 (5888), S. 572 - 575 (2008)
The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site. Science 91.
Zeitschriftenartikel
379 (5), S. 1063 - 1074 (2008)
Structure of the Dissimilatory Sulfite Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus. Journal of Molecular Biology (London) 92.
Zeitschriftenartikel
47 (17), S. 4964 - 4972 (2008)
Inhibitors of the Molybdenum Cofactor Containing 4-Hydroxybenzoyl-CoA Reductase. Biochemistry 93.
Zeitschriftenartikel
46 (14), S. 2408 - 2413 (2007)
Towards Biological Supramolecular Chemistry: A Variety of Pocket-Templated Metal Oxide Cluster Nucleations in the Cavity of a Mo/W-Storage Protein. Angewandte Chemie, International Edition in English 94.
Zeitschriftenartikel
274 (6), S. 1588 - 1599 (2007)
Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalysing the reduction of O2 to H2O. The FEBS Journal 95.
Zeitschriftenartikel
70 (1), S. 185 - 191 (2007)
Preliminary electrochemical studies of the flavohaemoprotein from Ralstonia eutropha entrapped in a film of methyl cellulose: activation of the reduction of dioxygen. Bioelectrochemistry 96.
Zeitschriftenartikel
103 (50), S. 18917 - 18922 (2006)
Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex. Proceedings of the National Academy of Sciences of the United States of America 97.
Zeitschriftenartikel
358 (3), S. 798 - 809 (2006)
The Crystal Structure of the Apoenzyme of the Iron-Sulphur Cluster-free Hydrogenase. Journal of Molecular Biology (London) 98.
Zeitschriftenartikel
357 (3), S. 870 - 879 (2006)
The structure of a Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with its Coenzymes. Journal of Molecular Biology (London) 99.
Zeitschriftenartikel
45 (9), S. 2960 - 2967 (2006)
Reaction Mechanism of the Iron-Sulfur Flavoenzyme Adenosine-5 '-Phosphosulfate Reductase Based on the Structural Characterization of Different Enzymatic States. Biochemistry 100.
Zeitschriftenartikel
579 (21), S. 4600 - 4604 (2005)
X-ray structure of the γ-subunit of a dissimilatory sulfite reductase: Fixed and flexible C-terminal arms. FEBS Letters