direkt zum Inhalt springen

direkt zum Hauptnavigationsmenü

Sie sind hier

TU Berlin

Page Content

Search

Search for publications




all Publications (Reviews, Articles, Meetings and Proceedings)

P

Kabuss, J., Werner, S., Hoffmann, A., Hildebrandt, P., Knorr, A. and Richter, M. (2010). Theory of time-resolved Raman scattering and fluorescence emission from semiconductor quantum dots. Phys. Rev. B. AMER PHYSICAL SOC.


Georg, S., Kabuss, J., Weidinger, I. M., Murgida, D. H., Hildebrandt, P., Knorr, A. and Richter, M. (2010). Distance-dependent electron transfer rate of immobilized redox proteins: A statistical physics approach. Phys. Rev. E. AMER PHYSICAL SOC.


DiPaolo, R. E., Rivas, L., Murgida, D. H. and Hildebrandt, P. (2005). Redox Equilibria of Cytochrome c(3) Immobilized on Self-Assembled Monolayers Coated Silver Electrodes. Phys. Script., 225-227.


Tschirner, N., Brose, K., Schenderlein, M., Zouni, A., Schlodder, E., Mroginski, M. A., Hildebrandt, P. and Thomsen, C. (2009). The anomaly of the v1 resonance Raman band of β-carotene in solution and in photosystems I and II. Phys. stat. solidi B, 2790-2793.


Tschirner, N., Schenderlein, M., Brose, K., Schlodder, E., Mroginski, M. A., Hildebrandt, P. and Thomsen, C. (2008). Raman excitation profiles of beta-carotene - novel insights into the nature of the nu(1)-band. Phys. stat. solidi B. WILEY-V C H VERLAG GMBH, 2225-2228.


Rippers, Y., Utesch, T., Hildebrandt, P., Zebger, I. and Mroginski, M. A. (2011). Insights into the structure of the active site of the O(2)-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modelling. Physical Chemistry Chemical Physics, 16146–16149.


Sezer, M., Feng, J.-J., Ly, H. K., Shen, Y., Nakanishi, T., Kuhlmann, U., Hildebrandt, P., Moehwald, H. and Weidinger, I. M. (2010). Multi-layer electron transfer across nanostructured Ag-SAM-Au-SAM junctions probed by surface enhanced Raman spectroscopy. Physical Chemistry Chemical Physics, 9822–9829.


Sezer, M., Spricigo, R., Utesch, T., Millo, D., Leimkuehler, S., Mroginski, M. A., Wollenberger, U., Hildebrandt, P. and Weidinger, I. M. (2010). Redox properties and catalytic activity of surface-bound human sulfite oxidase studied by a combined surface enhanced resonance Raman spectroscopic and electrochemical approach. PHYSICAL CHEMISTRY CHEMICAL PHYSICS. ROYAL SOC CHEMISTRY, 7894-7903.


Horch, M., Pinto, A. F., Utesch, T., Mroginski, M. A., Romao, C. V., Teixeira, M., Hildebrandt, P. and Zebger, I. (2014). Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study. Physical Chemistry Chemical Physics, 14220–14230.


Kozuch, J., Weichbrodt, C., Millo, D., Giller, K., Becker, S., Hildebrandt, P. and Steinem, C. (2014). Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy. Physical Chemistry Chemical Physics, 9546–9555.


Todorovic, S., Hildebrandt, P. and Martins, L. O. (2015). Surface enhanced resonance Raman detection of a catalytic intermediate of DyP-type peroxidase. Physical Chemistry Chemical Physics, 11954–11957.


Schumann, S., Terao, M., Garattini, E., Saggu, M., Lendzian, F., Hildebrandt, P. and Leimk�hler, S. (2009). Site directed mutagenesis of amino acis residues at the active site of mouse aldehyde oxidase AOXI. PloS One, e5348.


Nobre, L. S., Garcia-Serres, R., Todorovic, S., Hildebrandt, P., Teixeira, M., Latour, J.-M. and Saraiva, L. M. (2014). Escherichia coli RIC Is Able to Donate Iron to Iron-Sulfur Clusters. Plos One, e95222.


Heidary, N., Utesch, T., Zerball, M., Horch, M., Millo, D., Fritsch, J., Lenz, O., von Klitzing, R., Hildebrandt, P., Fischer, A., Mroginski, M. A. and Zebger, I. (2015). Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase. Plos One, e0143101.


Silveira, C. M., Quintas, P. O., Moura, I., Moura, J. J. G., Hildebrandt, P., Gabriela Almeida, M. and Todorovic, S. (2015). SERR Spectroelectrochemical Study of Cytochrome cd(1) Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c(552) on Biocompatible Metal Electrodes. Plos One, e0129940.


Zusatzinformationen / Extras

Quick Access:

Schnellnavigation zur Seite über Nummerneingabe

This site uses Matomo for anonymized webanalysis. Visit Data Privacy for more information and opt-out options.