Mathias Lübben
  • Department of Biophysics, Ruhr-Universität Bochum, Germany
Research fields
  • Biochemistry
Personal information


PhD in Biochemistry at the University of Hannover (Germany) in 1988

Current position

Lecturer of Biophysics and Group Leader at the Department of Biophysics of the University of Bochum

Publications (since 2000)

  1. 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.

  2. 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)

  3. 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.

  4. 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.

  5.  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)

  6. 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.

  7. 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.

  8. 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.

  9. 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.

  10. 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)

  11. 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.

  12. 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.

  13. 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.

  14. 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.

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