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Publikationen

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Revealing the Absolute Configuration of the CO and CN- Ligands at the Active Site of a [NiFe] Hydrogenase

Rippers, Y., Horch, M., Hildebrandt, P., Zebger, I. and Mroginski, M. A.

CHEMPHYSCHEM 13, 3852-3856. 2012

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Protein-Protein Complex Formation Affects the Ni-Fe and Fe-S Centers in the H-2-Sensing Regulatory Hydrogenase from Ralstonia eutropha H16

Loescher, S., Gebler, A., Stein, M., Sanganas, O., Buhrke, T., Zebger, I., Dau, H., Friedrich, B., Lenz, O. and Haumann, M.

CHEMPHYSCHEM 11, 1297-1306. 2010

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Impact of Amino Acid Substitutions near the Catalytic Site on the Spectral Properties of an O-2-Tolerant Membrane-Bound [NiFe] Hydrogenase

Saggu, M., Ludwig, M., Friedrich, B., Hildebrandt, P., Bittl, R., Lendzian, F., Lenz, O. and Zebger, I.

CHEMPHYSCHEM 11, 1215-1224. 2010

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Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution

Katz, S., Noth, J., Horch, M., Shafaat, H. S., Happe, T., Hildebrandt, P. and Zebger, I.

CHEMICAL SCIENCE 7, 6746-6752. 2016

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Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O-2-tolerant NAD(+)-reducing [NiFe] hydrogenase

Lauterbach, L., Wang, H., Horch, M., Gee, L. B., Yoda, Y., Tanaka, Y., Zebger, I., Lenz, O. and Cramer, S. P.

CHEMICAL SCIENCE 6, 1055-1060. 2015

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When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase

Ciaccafava, A., Tombolelli, D., Domnik, L., Fesseler, J., Jeoung, J.-H., Dobbek, H., Mroginski, M. A., Zebger, I. and Hildebrandt, P.

CHEMICAL SCIENCE 7, 3162-3171. 2016

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Microporous polymer network films covalently bound to gold electrodes

Becker, D., Heidary, N., Horch, M., Gernert, U., Zebger, I., Schmidt, J., Fischer, A. and Thomas, A.

CHEMICAL COMMUNICATIONS 51, 4283-4286. 2015

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Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?

Zhang, X., Yarman, A., Erdossy, J., Katz, S., Zebger, I., Jetzschmann, K. J., Altintas, Z., Wollenberger, U., Gyurcsanyi, R. E. and Scheller, F. W.

BIOSENSORS & BIOELECTRONICS 105, 29-35. 2018

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Investigation of the NADH/NAD(+) ratio in Ralstonia eutropha using the fluorescence reporter protein Peredox

Tejwani, V., Schmitt, F.-J., Wilkening, S., Zebger, I., Horch, M., Lenz, O. and Friedrich, T.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1858, 86-94. 2017

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Enzymatic and spectroscopic properties of a thermostable [NiFe]-hydrogenase performing H-2-driven NAD(+)-reduction in the presence of O-2

Preissler, J., Wahlefeld, S., Lorent, C., Teutloff, C., Horch, M., Lauterbach, L., Cramer, S. P., Zebger, I. and Lenz, O.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1859, 8-18. 2018

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Impact of the Iron-Sulfur Cluster Proximal to the Active Site on the Catalytic Function of an O-2-Tolerant NAD(+)-Reducing [NiFe]-Hydrogenase

Karstens, K., Wahlefeld, S., Horch, M., Grunzel, M., Lauterbach, L., Lendzian, F., Zebger, I. and Lenz, O.

BIOCHEMISTRY 54, 389-403. 2015

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Substrate-Protein Interactions of Type II NADH:Quinone Oxidoreductase from Escherichia coli

Salewski, J., Batista, A. P., Sena, F. V., Millo, D., Zebger, I., Pereira, M. M. and Hildebrandt, P.

BIOCHEMISTRY 55, 2722-2734. 2016

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O-2-Tolerant H-2 Activation by an Isolated Large Subunit of a [NiFe] Hydrogenase

Hartmann, S., Frielingsdorf, S., Ciaccafava, A., Lorent, C., Fritsch, J., Siebert, E., Priebe, J., Haumann, M., Zebger, I. and Lenz, O.

BIOCHEMISTRY 57, 5339-5349. 2018

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An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O-2-Tolerant Hydrogenase

Lindenmaier, N. J., Wahlefeld, S., Bill, E., Szilvasi, T., Eberle, C., Yao, S., Hildebrandt, P., Horch, M., Zebger, I. and Driess, M.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION 56, 2208-2211. 2017

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Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases

Siebert, E., Horch, M., Rippers, Y., Fritsch, J., Frielingsdorf, S., Lenz, O., Escobar, F. V., Siebert, F., Paasche, L., Kuhlmann, U., Lendzian, F., Mroginski, M.-A., Zebger, I. and Hildebrandt, P.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION 52, 5162-5165. 2013

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