Publications of S. Shima

Fujishiro, T., Tamura, H., Schick, M., Kahnt, J., Xie, X. L., Ermler, U. and Shima, S.: (2013) Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis, Angewandte Chemie, International Edition in English, Weinheim, Wiley-VCH, 52 (48), pp. 12555–12558.

Tamura, Haruka, Salomone-Stagni, M., Fujishiro, Takashi, Warkentin, E., Meyer-Klaucke, W., Ermler, U. and Shima, Seigo: (2013) Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H₂-Activation Site, Angewandte Chemie-International Edition, WEINHEIM, WILEY-V C H VERLAG GMBH, 52 (37), pp. 9656–9659.

Takano, Y., Kaneko, M., Kahnt, Jörg, Imachi, H., Shima, Seigo and Ohkouchi, N.: (2013) Detection of coenzyme F430 in deep sea sediments: A key molecule for biological methanogenesis, Organic Geochemistry, Oxford, Pergamon, 58, May, pp. 137–140.

Mills, Deryck J., Vitt, Stella, Strauss, Mike, Shima, Seigo and Vonck, Janet: (2013) De novo modeling of the F₄₂₀-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy, eLife, Cambridge, eLife Sciences Publications, 2, March.

Milucka, Jana, Widdel, Friedrich and Shima, Seigo: (2013) Immunological detection of enzymes for sulfate reduction in anaerobic methane-oxidizing consortia, Environmental Microbiology, Oxford, England, Blackwell Science, (15), pp. 1561–1571.

Upadhyay, V., Demmer, U., Warkentin, E., Moll, J., Shima, S. and Ermler, U.: (2012) Structure and Catalytic Mechanism of N-5,N-10-Methenyltetrahydromethanopterin Cyclohydrolase, Biochemistry, WASHINGTON, AMER CHEMICAL SOC, 51 (42), pp. 8435–8443.

Shima, Seigo and Ermler, Ulrich: (2012) Crystal structure and biochemistry of methyl-coenzyme M reductase from Black Sea mats mediating anaerobic oxidation of methane, Biseibutsu Seitai, WASHINGTON, NATL ACAD SCIENCES, 27, September, pp. 55–62.

Schick, M., Xie, X. L., Ataka, K., Kahnt, J., Linne, U. and Shima, S.: (2012) Biosynthesis of the Iron-Guanylylpyridinol Cofactor of [Fe]-Hydrogenase in Methanogenic Archaea as Elucidated by Stable-Isotope Labeling, Journal of the American Chemical Society, Washington, DC, American Chemical Society, 134 (6), pp. 3271–3280.

Shima, S., Krueger, M., Weinert, T., Demmer, U., Kahnt, J., Thauer, R. K. and Ermler, U.: (2012) Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically, Nature, London, Nature Publishing Group, 481 (7379), pp. 98–101.

Shima, S., Schick, M., Kahnt, J., Ataka, K., Steinbach, K. and Linne, U.: (2012) Evidence for acyl-iron ligation in the active site of [Fe]-hydrogenase provided by mass spectrometry and infrared spectroscopy, Dalton Transactions, Cambridge, UK, Royal Society of Chemistry, 41 (3), pp. 767–771.

Basen, M., Kruger, M., Milucka, J., Kuever, J., Kahnt, J., Grundmann, O., Meyerdierks, A., Widdel, F. and Shima, S.: (2011) Bacterial enzymes for dissimilatory sulfate reduction in a marine microbial mat (Black Sea) mediating anaerobic oxidation of methane, Environmental Microbiology, Oxford, England, Blackwell Science, 13 (5), pp. 1370–1379.

Shima, S. and Ermler, U.: (2011) Structure and Function of [Fe]-Hydrogenase and its Iron-Guanylylpyridinol (FeGP) Cofactor, European Journal of Inorganic Chemistry, Weinheim, Germany, Wiley-VCH, (7 Sp. Iss. SI) March, pp. 963–972.

Shima, S. and Ataka, K.: (2011) Isocyanides inhibit [Fe]-hydrogenase with very high affinity, FEBS Letters, Amsterdam, Elsevier, 585 (2), pp. 353–356.

Shima, S., Schick, M. and Tamura, H.: (2011) PREPARATION OF [FE]-HYDROGENASE FROM METHANOGENIC ARCHAEA, Methods in Enzymology, New York, NY, Academic Press, (494), pp. 119–137.

Salomone-Stagni, M., Stellato, F., Whaley, C. M., Vogt, S., Morante, S., Shima, S., Rauchfuss, T. B. and Meyer-Klaucke, W.: (2010) The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near edge spectroscopy study, Dalton Transactions, Cambridge, UK, Royal Society of Chemistry, 39 (12), pp. 3057–3064.

Shima, S., Vogt, S., Gobels, A. and Bill, E.: (2010) Iron-chromophore circular dichroism of [Fe]-hydrogenase: the conformational change required for H2 activation, Angewandte Chemie, International Edition in English, Weinheim, Wiley-VCH, 49 (51), pp. 9917–9921.

Ceh, Katharina, Demmer, Ulrike, Warkentin, Eberhard, Moll, Johanna, Thauer, Rudolf K., Shima, Seigo and Ermler, Ulrich: (2009) Structural basis of the Hhydride transfer mechanism in F₄₂₀ -dependent methylenetetrahydromethanopterin dehydrogenase, Biochemistry, Columbus, Ohio, American Chemical Society, 48, September, pp. 10098–10105.

Hiromoto, Takeshi, Ataka, Kenichi, Pilak, Oliver, Vogt, Sonja, Stagni, Marco Salomone, Meyer-Klaucke, Wolfram, Warkentin, Eberhard, Thauer, Rudolf Kurt, Shima, Seigo and Ermler, Ulrich: (2009) The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex, FEBS Letters, Amsterdam, Elsevier, 583 (3), pp. 585–590.

Hiromoto, Takeshi, Warkentin, Eberhard, Moll, Johanna, Ermler, Ulrich and Shima, Seigo: (2009) The Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H2 Activation, Angewandte Chemie Int. ed., 48, pp. 6457–6460.

Mayr, Stefan, Latkoczy, Christopher, Krüger Martin, Günther Detlef, Shima, Seigo, Thauer, Rudolf K., Widdel, Friedrich and Jaun, Bernhard: (2008) Structure of an F430 variant from archaea associated with anaerobic oxidation of methane, Journal of the American Chemical Society, Washington, DC, American Chemical Society, 130 (32), pp. 10758–10767.