Articles with public access mandates - Ingo ZebgerLearn more
Not available anywhere: 30
Probing the Active Site of an O2‐Tolerant NAD+‐Reducing [NiFe]‐Hydrogenase from Ralstonia eutropha H16 by In Situ EPR and FTIR Spectroscopy
M Horch, L Lauterbach, M Saggu, P Hildebrandt, F Lendzian, R Bittl, ...
Angewandte Chemie International Edition 49 (43), 8026-8029, 2010
Mandates: German Research Foundation
Spectroelectrochemical study of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F in solution and immobilized on biocompatible gold surfaces
D Millo, ME Pandelia, T Utesch, N Wisitruangsakul, MA Mroginski, ...
The Journal of Physical Chemistry B 113 (46), 15344-15351, 2009
Mandates: German Research Foundation
Resonance Raman spectroscopy on [NiFe] hydrogenase provides structural insights into catalytic intermediates and reactions
M Horch, J Schoknecht, MA Mroginski, O Lenz, P Hildebrandt, I Zebger
Journal of the American Chemical Society 136 (28), 9870-9873, 2014
Mandates: German Research Foundation
The Hydrogenase Subcomplex of the NAD+‐Reducing [NiFe] Hydrogenase from Ralstonia eutropha – Insights into Catalysis and Redox Interconversions
L Lauterbach, J Liu, M Horch, P Hummel, A Schwarze, M Haumann, ...
European Journal of Inorganic Chemistry 2011 (7), 1067-1079, 2011
Mandates: German Research Foundation
Monitoring Catalysis of the Membrane‐Bound Hydrogenase from Ralstonia eutropha H16 by Surface‐Enhanced IR Absorption Spectroscopy
N Wisitruangsakul, O Lenz, M Ludwig, B Friedrich, F Lendzian, ...
Angewandte Chemie International Edition 48 (3), 611-613, 2009
Mandates: German Research Foundation
Reversible Active Site Sulfoxygenation Can Explain the Oxygen Tolerance of a NAD+-Reducing [NiFe] Hydrogenase and Its Unusual Infrared Spectroscopic …
M Horch, L Lauterbach, MA Mroginski, P Hildebrandt, O Lenz, I Zebger
Journal of the American Chemical Society 137 (7), 2555-2564, 2015
Mandates: German Research Foundation
Role of the HoxZ Subunit in the Electron Transfer Pathway of the Membrane-Bound [NiFe]-Hydrogenase from Ralstonia eutropha Immobilized on Electrodes
M Sezer, S Frielingsdorf, D Millo, N Heidary, T Utesch, MA Mroginski, ...
The Journal of Physical Chemistry B 115 (34), 10368-10374, 2011
Mandates: German Research Foundation
[NiFe] and [FeS] cofactors in the membrane-bound hydrogenase of Ralstonia eutropha investigated by X-ray absorption spectroscopy: insights into O2-tolerant H2 cleavage
J Fritsch, S Löscher, O Sanganas, E Siebert, I Zebger, M Stein, ...
Biochemistry 50 (26), 5858-5869, 2011
Mandates: German Research Foundation, Government of Spain
Resonance Raman Spectroscopic Analysis of the [NiFe] Active Site and the Proximal [4Fe-3S] Cluster of an O2-Tolerant Membrane-Bound Hydrogenase in the …
E Siebert, Y Rippers, S Frielingsdorf, J Fritsch, A Schmidt, J Kalms, S Katz, ...
The Journal of Physical Chemistry B 119 (43), 13785-13796, 2015
Mandates: German Research Foundation
In situ spectroelectrochemical studies into the formation and stability of robust diazonium-derived interfaces on gold electrodes for the immobilization of an oxygen-tolerant …
TGAA Harris, N Heidary, J Kozuch, S Frielingsdorf, O Lenz, MA Mroginski, ...
ACS applied materials & interfaces 10 (27), 23380-23391, 2018
Mandates: German Research Foundation, Federal Ministry of Education and Research, Germany
Revealing the Absolute Configuration of the CO and CN− Ligands at the Active Site of a [NiFe] Hydrogenase
Y Rippers, M Horch, P Hildebrandt, I Zebger, MA Mroginski
ChemPhysChem 13 (17), 3852-3856, 2012
Mandates: German Research Foundation
An S‐Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2‐Tolerant Hydrogenase
NJ Lindenmaier, S Wahlefeld, E Bill, T Szilvási, C Eberle, S Yao, ...
Angewandte Chemie International Edition 56 (8), 2208-2211, 2017
Mandates: German Research Foundation
Impact of the Iron–Sulfur Cluster Proximal to the Active Site on the Catalytic Function of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase
K Karstens, S Wahlefeld, M Horch, M Grunzel, L Lauterbach, F Lendzian, ...
Biochemistry 54 (2), 389-403, 2015
Mandates: German Research Foundation
Substrate–Protein Interactions of Type II NADH:Quinone Oxidoreductase from Escherichia coli
J Salewski, AP Batista, FV Sena, D Millo, I Zebger, MM Pereira, ...
Biochemistry 55 (19), 2722-2734, 2016
Mandates: German Research Foundation, Leibniz Association, Netherlands Organisation …
Bias from H2 Cleavage to Production and Coordination Changes at the Ni−Fe Active Site in the NAD+-Reducing Hydrogenase from Ralstonia eutropha
S Löscher, T Burgdorf, I Zebger, P Hildebrandt, H Dau, B Friedrich, ...
Biochemistry 45 (38), 11658-11665, 2006
Mandates: German Research Foundation
O2-Tolerant H2 Activation by an Isolated Large Subunit of a [NiFe] Hydrogenase
S Hartmann, S Frielingsdorf, A Ciaccafava, C Lorent, J Fritsch, E Siebert, ...
Biochemistry 57 (36), 5339-5349, 2018
Mandates: German Research Foundation
Impact of Amino Acid Substitutions near the Catalytic Site on the Spectral Properties of an O2‐Tolerant Membrane‐Bound [NiFe] Hydrogenase
M Saggu, M Ludwig, B Friedrich, P Hildebrandt, R Bittl, F Lendzian, ...
ChemPhysChem 11 (6), 1215-1224, 2010
Mandates: German Research Foundation
Catalytic activity and proton translocation of reconstituted respiratory complex I monitored by surface-enhanced infrared absorption spectroscopy
O Gutierrez-Sanz, E Forbrig, AP Batista, MM Pereira, J Salewski, ...
Langmuir 34 (20), 5703-5711, 2018
Mandates: German Research Foundation, Fundação para a Ciência e a Tecnologia, Portugal …
Comparison of molybdenum and rhenium oxo bis-pyrazine-dithiolene complexes–in search of an alternative metal centre for molybdenum cofactor models
N Chrysochos, M Ahmadi, S Wahlefeld, Y Rippers, I Zebger, ...
Dalton transactions 48 (8), 2701-2714, 2019
Mandates: German Research Foundation, European Commission
Combining Spectroscopy and Theory to Evaluate Structural Models of Metalloenzymes: A Case Study on the Soluble [NiFe] Hydrogenase from Ralstonia eutropha
M Horch, Y Rippers, MA Mroginski, P Hildebrandt, I Zebger
ChemPhysChem 14 (1), 185-191, 2013
Mandates: German Research Foundation
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