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all Publications (Reviews, Articles, Meetings and Proceedings)

A

Oellerich, S., Bill, E. and Hildebrandt, P. (2000). Freeze-quench resonance raman and electron paramagnetic resonance spectroscopy for studying enzyme kinetics: Application to azide binding to myoglobin. Applied spectroscopy. SOC APPLIED SPECTROSCOPY, 1480-1484.


Gkogkou, D., Shaykhutdinov, T., Oates, T. W., Gernert, U., Schreiber, B., Facsko, S., Hildebrandt, P., Weidinger, I. M., Esser, N. and Hinrichs, K. (2016). Characterization of anisotropically shaped silver nanoparticle arrays via spectroscopic ellipsometry supported by numerical optical modeling. Applied Surface Science, -.

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Gkogkou, D., Shaykhutdinov, T., Oates, T. W., Gernert, U., Schreiber, B., Facsko, S., Hildebrandt, P., Weidinger, I. M., Esser, N. and Hinrichs, K. (2016). Characterization of anisotropically shaped silver nanoparticle arrays via spectroscopic ellipsometry supported by numerical optical modeling. Applied Surface Science, -.

Link to publication

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.


B

Strehlow, H. and Hildebrandt, P. (1990). The dissociation of trifluoroacetic-acid. Berichte der Bunsen-Gesellschaft-phys. chem. chem. phys. VCH PUBLISHERS INC, 173-179.


Strehlow, H., Wagner, I. and Hildebrandt, P. (1983). Chemical-exchange and Raman line broadening - the rate of protolysis of nitric-acid. Berichte der Bunsen-Gesellschaft-phys. chem. chem. phys. VCH PUBLISHERS INC, 516-522.


Anzenbacherova, E., Hudecek, J., Murgida, D., Hildebrandt, P., Marchal, S., Lange, R. and Anzenbacher, P. (2005). Active sites of two orthologous cytochromes P450 2E1: Differences revealed by spectroscopic methods. Biochem. Biophys. Res. Commun.. ACADEMIC PRESS INC ELSEVIER SCIENCE, 477-482.


Durao, P., Chen, Z., Silva, C. S., Soares, C. M., Pereira, M. M., Todorovic, S., Hildebrandt, P., Bento, I., Lindley, P. F. and Martins, L. O. (2008). Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants. Biochem. J.. PORTLAND PRESS LTD, 339-346.


Schkolnik, G., Utesch, T., Zhao, J., Jiang, S., Thompson, M. K., Mroginski, M.-A., Hildebrandt, P. and Franzen, S. (2013). Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics - application of the vibrational Stark effect to understand enzyme kinetics. Biochemical and Biophysical Research Communications, 1011–1015.


Remberg, A., Lindner, I., Lamparter, T., Hughes, J., Kneip, C., Hildebrandt, P., Braslavsky, S. E., Gartner, W. and Schaffner, K. (1997). Raman spectroscopic and light-induced kinetic characterization of a recombinant phytochrome of the cyanobacterium Synechocystis. Biochemistry. AMER CHEMICAL SOC, 13389-13395.


Rosell, F. I., Harris, T. R., Hildebrand, D., Dopner, S., Hildebrandt, P. and Mauk, A. G. (2000). Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c. Biochemistry. AMER CHEMICAL SOC, 9047-9054.


Battistuzzi, G., Bortolotti, C. A., Bellei, M., Di Rocco, G., Salewski, J., Hildebrandt, P. and Sola, M. (2012). Role of Met80 and Tyr67 in the Low-pH Conformational Equilibria of Cytochrome c. Biochemistry, 5967–5978.


Fiege, K., Querebillo, C. J., Hildebrandt, P. and Frankenberg-Dinkel, N. (2018). Improved Method for the Incorporation of Heme Cofactors into Recombinant Proteins Using Escherichia coli Nissle 1917. Biochemistry, 2747-2755.

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Gerscher, S., Dopner, S., Hildebrandt, P., Gleissner, M. and Schafer, G. (1996). Resonance Raman spectroscopy of the integral quinol oxidase complex of Sulfolobus acidocaldarius. Biochemistry. AMER CHEMICAL SOC, 12796-12803.


Todorovic, S., Leal, S. S., Salgueiro, C. A., Zebger, I., Hildebrandt, P., Murgida, D. H. and Gomes, C. M. (2007). A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties. Biochemistry. AMER CHEMICAL SOC, 10733-10738.


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