Education
PhD in Microbiology, Department of Microbiology and Biotechnology, University Bonn, Germany
Current position
Professor for Biochemistry and Molecular Biology, Medical Faculty, University Freiburg, Germany
Publications
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Koch, H. G. and Schneider, D. (2016). Assembly of Transmembrane b-type Cytochromes and Cytochrome complexes. In: Cramer, W.A. and Kallas, T. (eds). Cytochrome complexes: Evolution, Structures, Energy Transduction, and Signaling, Springer, Dordrecht.
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Khalfaoui-Hassani, B., Verissimo, A. F., Shroff, N., Ekici, S., Trasnea, P-I., Utz, M., Koch, H-G. and Daldal, F. (2016). Biogenesis of Cytochrome c Complexes: From Insertion of Redox Cofactors to Assembly of Different Subunits. In: Cramer, W. A. and Kallas, T. (eds). Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling, Advances in Photosynthesis and Respiration 41, pp. 527-554.
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Hannemann, L., Suppanz, I., Ba, Q., MacInnes, K., Drepper, F., Warscheid, B. and Koch, H. G. (2016). Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1. Antioxid Redox Signal 24(3): 141-156.
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Trasnea, P. I., Utz, M., Khalfaoui-Hassani, B., Lagies, S., Daldal, F. and Koch, H. G. (2016). Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus. Mol Microbiol 100(2): 345-361.
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Khalfaoui-Hassani, B., Verissimo, A. F., Koch, H. G. and Daldal, F. (2016). Uncovering the Transmembrane Metal Binding Site of the Novel Bacterial Major Facilitator Superfamily-Type Copper Importer CcoA. MBio 7(1): e01981-01915.
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Petriman, N. A., Jauß, B. and Koch, H. G. (2015). Proteintransport in Bakterien: Einblicke in die Funktionsweise komplexer Transportmaschinerien. Biospektrum 7,696-698.
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Kuhn, P., Draycheva, A., Vogt, A., Petriman, N. A., Sturm, L., Drepper, F., Warscheid, B., Wintermeyer, W. and Koch, H. G. (2015). Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon. J Cell Biol 211(1): 91-104.
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Denks, K., Vogt, A., Sachelaru, I., Petriman, N. A., Kudva, R. and Koch, H. G. (2014). The Sec translocon mediated protein transport in prokaryotes and eukaryotes. Mol Membr Biol 31(2-3): 58-84.
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Sachelaru, I., Petriman, N. A., Kudva, R. and Koch, H. G. (2014). Dynamic interaction of the sec translocon with the chaperone PpiD. J Biol Chem 289(31): 21706-21715.
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Kuhn, P., Kudva, R., Welte, T., Sturm, L. and Koch, H. G. (2014). Targeting and integration of bacterial membrane proteins. In: Remaut, H. and Fronzes, R. (eds). Bacterial Membranes: Structural and Molecular Biology, Horizon Press, Norwich, U. K.
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Braig, D., Kaiser, B., Thiele, J. R., Bannasch, H., Peter, K., Stark, G. B., Koch, H. G. and Eisenhardt, S. U. (2014). A conformational change of C-reactive protein in burn wounds unmasks its proinflammatory properties. Int Immunol 26(8): 467-478.
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Ekici, S., Turkarslan, S., Pawlik, G., Dancis, A., Baliga, N. S., Koch, H. G. and Daldal, F. (2014). Intracytoplasmic copper homeostasis controls cytochrome c oxidase production. MBio 5(1): e01055-01013.
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Sachelaru, I., Petriman, N. A., Kudva, R., Kuhn, P., Welte, T., Knapp, B., Drepper, F., Warscheid, B. and Koch, H. G. (2013). YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein. J Biol Chem 288(23): 16295-16307.
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Koch, H. G. (2013). Keine Pause bei Prolinen: Wie der Elongationsfaktor EF-P die Proteinsynthese rettet. Biospektrum 3, 13.
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Kudva, R., Denks, K., Kuhn, P., Vogt, A., Muller, M. and Koch, H. G. (2013). Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways. Res Microbiol 164(6): 505-534.
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Ekici, S., Jiang, X., Koch, H. G. and Daldal, F. (2013). Missense mutations in cytochrome c maturation genes provide new insights into Rhodobacter capsulatus cbb3-type cytochrome c oxidase biogenesis. J Bacteriol 195(2): 261-269.
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Wenk, M., Ba, Q., Erichsen, V., MacInnes, K., Wiese, H., Warscheid, B. and Koch, H. G. (2012). A universally conserved ATPase regulates the oxidative stress response in Escherichia coli. J Biol Chem 287(52): 43585-43598.
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Eikici, S., Pawlik, G., Lohmeyer, E., Koch, H. G. and Daldal, F. (2012). Biogenesis of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus. Biochim. Biophys. Acta, 1817, 898-910.
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Lohmeyer, E., Schroder, S., Pawlik, G., Trasnea, P. I., Peters, A., Daldal, F. and Koch, H. G. (2012). The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb(3)-type cytochrome oxidase in Rhodobacter capsulatus. Biochim Biophys Acta 1817(11): 2005-2015.
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Ekici, S., Yang, H., Koch, H. G. and Daldal, F. (2012). Novel transporter required for biogenesis of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus. MBio 3(1)
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Welte, T., Kudva, R., Kuhn, P., Sturm, L., Braig, D., Muller, M., Warscheid, B., Drepper, F. and Koch, H. G. (2012). Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle. Mol Biol Cell 23(3): 464-479.
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Braig, D., Mircheva, M., Sachelaru, I., van der Sluis, E. O., Sturm, L., Beckmann, R. and Koch, H. G. (2011). Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle. Mol Biol Cell 22(13): 2309-2323.
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Kuhn, P., Weiche, B., Sturm, L., Sommer, E., Drepper, F., Warscheid, B., Sourjik, V. and Koch, H. G. (2011). The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon. Traffic 12(5): 563-578.
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Pawlik, G., Kulajta, C., Sachelaru, I., Schroder, S., Waidner, B., Hellwig, P., Daldal, F. and Koch, H. G. (2010). The putative assembly factor CcoH is stably associated with the cbb3-type cytochrome oxidase. J Bacteriol 192(24): 6378-6389.
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Mircheva, M., Boy, D., Weiche, B., Hucke, F., Graumann, P. and Koch, H. G. (2009). Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor. BMC Biol 7: 76.
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Burk, J., Weiche, B., Wenk, M., Boy, D., Nestel, S., Heimrich, B. and Koch, H. G. (2009). Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli. J Bacteriol 191(22): 7017-7026.
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Braig, D., Bar, C., Thumfart, J. O. and Koch, H. G. (2009). Two cooperating helices constitute the lipid-binding domain of the bacterial SRP receptor. J Mol Biol 390(3): 401-413.
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Boy, D. and Koch, H. G. (2009). Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins. Mol Biol Cell 20(6): 1804-1815.
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Sanders, C., Turkasalan, S., Onder, O., Frawley, E. R., Kranz, R. G., Koch, H. G. and Daldal, F. (2008). Biogenesis of cytochromes and cytochrome complexes. In: Hunter, C. N., Daldal, F., Thurnauer, M. C. and Beatty, J. T. (eds). The Purple Phototrophic Bacteria., Springer Verlag, Heidelberg.
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Peters, A., Kulajta, C., Pawlik, G., Daldal, F. and Koch, H. G. (2008). Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP interactions. J Bacteriol 190(16): 5576-5586.
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Weiche, B., Burk, J., Angelini, S., Schiltz, E., Thumfart, J. O. and Koch, H. G. (2008). A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor. J Mol Biol 377(3): 761-773.
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Angelini, S., Boy, D., Schiltz, E. and Koch, H. G. (2006). Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites. J Cell Biol 174(5): 715-724.
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Koch, H. G. und Schneider, D. (2007). Folding, assembly and stability of transmembrane cytochromes. Current Chemical Biology 1; 59-74.
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Aygun-Sunar, S., Mandaci, S., Koch, H. G., Murray, I. V., Goldfine, H. and Daldal, F. (2006). Ornithine lipid is required for optimal steady-state amounts of c-type cytochromes in Rhodobacter capsulatus. Mol Microbiol 61(2): 418-435.
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Kulajta, C., Thumfart, J. O., Haid, S., Daldal, F. and Koch, H. G. (2006). Multi-step assembly pathway of the cbb3-type cytochrome c oxidase complex. J Mol Biol 355(5): 989-1004.
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Deitermann, S., Sprie, G. S. and Koch, H. G. (2005). A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli. J Biol Chem 280(47): 39077-39085.
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Angelini, S., Deitermann, S. and Koch, H. G. (2005). FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon. EMBO Rep 6(5): 476-481.