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H

Horch, M., Schoknecht, J., Mroginski, M. A., Lenz, O., Hildebrandt, P. and Zebger, I. (2014). Resonance Raman Spectroscopy on [NiFe] Hydrogenase Provides Structural Insights into Catalytic Intermediates and Reactions. Journal of the American Chemical Society, 9870–9873.


Horch, M., Hildebrandt, P. and Zebger, I. (2015). Concepts in bio-molecular spectroscopy: vibrational case studies on metalloenzymes. Phys. Chem. Chem. Phys.. The Royal Society of Chemistry, 18222-18237.

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Horch, M., Lauterbach, L., Mroginski, M. A., Hildebrandt, P., Lenz, O. and Zebger, I. (2015). Reversible Active Site Sulfoxygenation Can Explain the Oxygen Tolerance of a NAD(+)-Reducing [NiFe] Hydrogenase and Its Unusual Infrared Spectroscopic Properties. Journal of the American Chemical Society, 2555–2564.


Horch, M., Lauterbach, L., Lenz, O., Hildebrandt, P. and Zebger, I. (2012). NAD(H)-coupled hydrogen cycling - structure-function relationships of bidirectional [NiFe] hydrogenases. Febs Letters, 545–556.


Horch, M., Lauterbach, L., Saggu, M., Hildebrandt, P., Lendzian, F., Bittl, R., Lenz, O. and Zebger, I. (2010). Probing the Active Site of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 by In Situ EPR and FTIR Spectroscopy. Angewandte Chemie International Edition. WILEY-VCH Verlag, 8026-8029.

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Horch, M., Rippers, Y., Mroginski, M. A., Hildebrandt, P. and Zebger, I. (2013). Combining Spectroscopy and Theory to Evaluate Structural Models of Metalloenzymes: A Case Study on the Soluble [NiFe] Hydrogenase from Ralstonia eutropha. Chemphyschem, 185–191.


Horch, M., Utesch, T., Hildebrandt, P., Mroginski, M. A. and Zebger, I. (2016). Domain motions and electron transfer dynamics in 2Fe-superoxide reductase. Phys. Chem. Chem. Phys.. The Royal Society of Chemistry, 23053-23066.

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Horch, M., Siebert, E., Rippers, Y., Katz, S., Noth, J., Wahlefeld, S., Lindenmaier, N. J., Happe, T., Driess, M., Lenz, O., Mroginski, M. A., Hildebrandt, P. and Zebger, I. (2017). Resonance raman spectroscopy provides insights into biological hydrogen conversion. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, S161.


Horch, M., Utesch, T., Pinto, A. F., Valente Romao, C., Teixeira, M., Mroginski, M. A., Hildebrandt, P. and Zebger, I. (2017). Structural transitions and enzymatic function: Case studies on superoxide reductase. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, S161.


Hrabakova, J., Ataka, K., Heberle, J., Hildebrandt, P. and Murgida, D. H. (2006). Long distance electron transfer in cytochrome c oxidase immobilised on electrodes. A surface enhanced resonance Raman spectroscopic study. Phys. chem. chem. phys. ROYAL SOC CHEMISTRY, 759-766.


Hudecek, J., Anzenbacher, P., Hildebrandt, P. and Munro, A. W. (1998). Resonance Raman spectral analysis of CYP102 and CYP1A2. Chemical papers-Chemicke zvesti. SLOVAK ACADEMIC PRESS LTD, 519.


Hudecek, J., Anzenbacher, P., Munro, A. W. and Hildebrand, P. (2000). Raman Evidence for Differences in Heme Vinyl Orientations in Cytochromes P-450 Isoforms. Proc. Int. Conf. Raman Spectrosc. XVII. Wiley, 974-975.


Hudecek, J., Anzenbacherova, E., Anzenbacher, P., Munro, A. W. and Hildebrandt, P. (2000). Structural similarities and differences of the heme pockets of various P450 isoforms as revealed by resonance Raman spectroscopy. Archives of biochemistry and biophysics. ACADEMIC PRESS INC, 70-78.


Hudecek, Y., Hildebrandt, P., Marsh, D. and Heimburg, T. (1997). Spectroscopic studies of cytochrome c interaction with lipid membranes - The coupling of cytochrome c function with surface absorption and integration. SPECTROSCOPY OF BIOLOGICAL MOLECULES: MODERN TRENDS. SPRINGER, 297-300.


J

Jeon, H., Yoon, C., Song, Y.-G., Han, J., Kwon, S., Kim, S., Chang, I. and Lee, K. (2018). Reducing the Coefficient of Thermal Expansion of Polyimide Films in Microelectronics Processing Using ZnS Particles at Low Concentrations. ACS Applied Nano Materials, 1076-1082.

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