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Neumann, M., Mittelstaedt, G., Iobbi-Nivol, C., Saggu, M., Lendzian, F., Hildebrandt, P. and Leimkuehler, S. (2009). A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli. FEBS. J.. WILEY-BLACKWELL PUBLISHING, INC, 2762-2774.

Saggu, M., Zebger, I., Ludwig, M., Lenz, O., Friedrich, B., Hildebrandt, P. and Lendzian, F. (2009). Spectroscopic Insights into the Oxygen-tolerant Membrane-associated [NiFe] Hydrogenase of eutropha H16. J. Biol. Chem.. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 16264-16276.

Anzenbacher, P., Anzenbacherova, E., Hendrychova, T., Otyepka, M., Hudecek, J., Hildebrandt, P. and Lange, R. (2009). Flexibility and plasticity of the structures of cytochromes P450 as a property determining their function. FEBS J.. WILEY-BLACKWELL PUBLISHING, INC, 26.

Wackerbarth, H., Kuhlmann, U., Tintchev, F., Heinz, V. and Hildebrandt, P. (2009). Structural changes of myoglobin in pressure-treated pork meat probed by resonance Raman spectroscopy. Food Chem.. ELSEVIER SCI LTD, 1194-1198.

Millo, D., Pandelia, M.-E., Utesch, T., Wisitruangsakul, N., Mroginski, M. A., Lubitz, W., Hildebrandt, P. and Zebger, I. (2009). Spectroelectrochemical Study of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F in Solution and Immobilized on Biocompatible Gold Surfaces. J. Phys. Chem. B. American Chemical Society, 15344-15351.

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Saggu, M., Teutloff, C., Ludwig, M., Brecht, M., Pandelia, M.-E., Lenz, O., Friedrich, B., Lubitz, W., Hildebrandt, P., Lendzian, F. and Bittl, R. (2010). Comparison of the membrane-bound [NiFe] hydrogenases from R. eutropha H16 and D. vulgaris Miyazaki F in the oxidized ready state by pulsed EPR. Phys. Chem. Chem. Phys.. ROYAL SOC CHEMISTRY, 2139-2148.

Chen, Z., Durao, P., Silva, C. S., Pereira, M. M., Todorovic, S., Hildebrandt, P., Bento, I., Lindley, P. F. and Martins, L. O. (2010). The role of Glu(498) in the dioxygen reactivity of CotA-laccase from Bacillus subtilis. Dalton Trans.. ROYAL SOC CHEMISTRY, 2875-2882.

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.

Feng, J., Wang, A. J. and Hildebrandt, P. (2010). Electron Transfer of Proteins at Nano-biointerfaces. Biocompatible Nanomaterials: Synthesis, Characterization and Applications. Nova Publisher, New York, 243 - 265.

Hildebrandt, P. (2010). A Spectral Window to the Cell. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION. WILEY-V C H VERLAG GMBH, 4540-4541.

Hildebrandt, P. (2010). Ein spektrales Fenster in die Zelle. Angewandte Chemie. WILEY-VCH Verlag, 4642-4644.

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Hildebrandt, P., Feng, J.-J., Kranich, A., Ly, K. H., Martín, D. F., Martí, M., Murgida, D. H., Paggi, D. A., Wisitruangsakul, N., Sezer, M., Weidinger, I. M. and Zebger, I. (2010). Electron Transfer of Proteins at Membrane Models. Surface Enhanced Raman Spectroscopy. Wiley-VCH Verlag GmbH & Co. KGaA, 219–240.

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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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Monari, S., Millo, D., Ranieri, A., Di Rocco, G., van der Zwan, G., Gooijer, C., Peressini, S., Tavagnacco, C., Hildebrandt, P. and Borsari, M. (2010). The impact of urea-induced unfolding on the redox process of immobilised cytochrome \<i\>c\</i\>. Journal of Biological Inorganic Chemistry. Springer Berlin / Heidelberg, 1233-1242.

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