Lecturer of Biophysics and Group Leader at the Department of Biophysics of the University of Bochum
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Drees, S. L., Beyer, D. F., Lenders-Lomscher, C. and Lubben, M. (2015). Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA. Mol Microbiol 97(3): 423-438.
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M. Lübben & R. Gasper, Kapitel 3: „Prokaryotes as protein production facilities“ in Biotechnology (Kück, U., Frankenberg-Dinkel, N., eds.), pp. 47-87. Walter de Gruyter GmbH, Berlin/Boston (2015)
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Vollmecke, C., Drees, S. L., Reimann, J., Albers, S. V. and Lubben, M. (2012). The ATPases CopA and CopB both contribute to copper resistance of the thermoacidophilic archaeon Sulfolobus solfataricus. Microbiology 158(Pt 6): 1622-1633.
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Vollmecke, C., Kotting, C., Gerwert, K. and Lubben, M. (2009). Spectroscopic investigation of the reaction mechanism of CopB-B, the catalytic fragment from an archaeal thermophilic ATP-driven heavy metal transporter. FEBS J 276(21): 6172-6186.
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M. Lübben, Kapitel 2 "Aminosäuren und Proteine" und Kapitel 3 "Enzyme" in: Biochemie des Menschen (Schartl, M., Gessler, M., v. Eckardstein, A., eds.), pp. 31-116. Urban und Fischer Verlag, München (2009)
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Lubben, M., Portmann, R., Kock, G., Stoll, R., Young, M. M. and Solioz, M. (2009). Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking. Biometals 22(2): 363-375.
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Lubben, M., Guldenhaupt, J., Zoltner, M., Deigweiher, K., Haebel, P., Urbanke, C. and Scheidig, A. J. (2007). Sulfate acts as phosphate analog on the monomeric catalytic fragment of the CPx-ATPase CopB from Sulfolobus solfataricus. J Mol Biol 369(2): 368-385.
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Deigweiher, K., Drell, T. L. t., Prutsch, A., Scheidig, A. J. and Lubben, M. (2004). Expression, isolation, and crystallization of the catalytic domain of CopB, a putative copper transporting ATPase from the thermoacidophilic archaeon Sulfolobus solfataricus. J Bioenerg Biomembr 36(1): 151-159.
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Bettinger, K., Prutsch, A., Vogtt, K. and Lubben, M. (2004). Noninvasive auto-photoreduction used as a tool for studying structural changes in heme-copper oxidases by FTIR spectroscopy. Biophys J 86(5): 3230-3240.
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M. Lübben & H.-H. Kiltz: Kapitel A-3: "Proteine", pp. 83 – 134. In: Lehrbuch der vorlinischen Medizin. Kurtz, A., Schartl, M., Schmidt, R. F., Unsicker, K., eds. Deutscher Ärzte-Verlag, Köln (2003)
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Ludovici, C., Frohlich, R., Vogtt, K., Mamat, B. and Lubben, M. (2002). Caged O(2). Reaction of cytochrome bo(3) oxidase with photochemically released dioxygen from a cobalt peroxo complex. Eur J Biochem 269(10): 2630-2637.
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Prutsch, A., Vogtt, K., Ludovici, C. and Lubben, M. (2002). Electron transfer at the low-spin heme b of cytochrome bo(3) induces an environmental change of the catalytic enhancer glutamic acid-286. Biochim Biophys Acta 1554(1-2): 22-28.
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Romao, C. V., Louro, R., Timkovich, R., Lubben, M., Liu, M. Y., LeGall, J., Xavier, A. V. and Teixeira, M. (2000). Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the anaerobic bacterium Desulfovibrio desulfuricans. FEBS Lett 480(2-3): 213-216.
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Prutsch, A., Lohaus, C., Green, B., Meyer, H. E. and Lubben, M. (2000). Multiple posttranslational modifications at distinct sites contribute to heterogeneity of the lipoprotein cytochrome bo(3). Biochemistry 39(21): 6554-6563.