Publications of S. Shima

Shima, S.: (2016) The Biological Methane-Forming Reaction: Mechanism Confirmed Through Spectroscopic Characterization of a Key Intermediate, Angewandte Chemie, International Edition in English, Weinheim, Wiley-VCH, 55 (44), pp. 13648–13649.

Upadhyay, V., Ceh, K., Tumulka, F., Abele, R., Hoffmann, J., Langer, J., Shima, S. and Ermler, U.: (2016) Molecular characterization of methanogenic N-5-methyl-tetrahydromethanopterin: Coenzyme M methyltransferase, Biochimica et Biophysica Acta-Biomembranes, 1858 (9), pp. 2140–2144.

Wagner, T., Kahnt, J., Ermler, U. and Shima, S.: (2016) Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing Methane Formation, Angewandte Chemie-International Edition, 55 (36), pp. 10630–10633.

Fujishiro, T., Bai, L., Xu, T., Xie, X., Schick, M., Kahnt, J., Rother, M., Hu, X., Ermler, U. and Shima, S.: (2016) Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis, Angewandte Chemie International Edition, Weinheim, Wiley-VCH, 55 (33), pp. 9648–9651.

Wagner, T., Ermler, U. and Shima, S.: (2016) MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode, Scientific Reports, London, UK, Nature Publishing Group, 6, June.

Duin, E.C., Wagner, T., Shima, S., Prakash, D., Cronin, B., Yanez-Ruiz, D.R., Duval, S., Rümbeli, R., Stemmler, R.T., Thauer, R.K. and Kindermann, M.: (2016) Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol, Proceedings of the National Academy of Sciences of the United States of America, Washington, D.C., National Academy of Sciences, 113 (22), pp. 6172–6177.

Shima, Seigo and Fujishiro, T.: (2016) Identification of the biosynthetic enzymes of the [Fe]-hydrogenase cofactor based on the crystal structure of the proteins, Kouso-Kogaku News, 76, pp. 26–30.

Shima, S., Chen, D., Xu, T., Wodrich, M. D., Fujishiro, T., Schultz, K. M., Kahnt, J., Ataka, K. and Hu, X.: (2015) Reconstitution of [Fe]-hydrogenase using model complexes, Nature Chemistry, London, UK, Nature Publishing Group, 7 (12), pp. 995–1002.

Hidese, R., Ataka, K., Bill, E. and Shima, S.: (2015) Cu^I and H₂O₂ inactivate and Fe^II inhibits [Fe]-hydrogenase at very low concentrations, ChemBioChem: A European Journal of Chemical Biology, Weinheim, Germany, Wiley-VCH, 16 (13), pp. 1861–1865.

Fujishiro, T., Ataka, K., Ermler, U. and Shima, S.: (2015) Towards a functional identification of catalytically inactive [Fe]-hydrogenase paralogs, The FEBS Journal, Wiley-Blackwell, 282 (17), pp. 3412–3423.

Fujishiro, T., Kahnt, J., Ermler, U. and Shima, S.: (2015) Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor, Nature Communications, London, Nature Publishing Group, 6, April.

Shima, Seigo: (2015) An energy metabolism under anoxic conditions: Enzyme chemistry of methanogenesis, Kagakutokogyo, (68), pp. 706–708.

Kojima, H., Moll, J., Kahnt, J., Fukui, M. and Shima, S.: (2014) A reversed genetic approach reveals the coenzyme specificity and other catalytic properties of three enzymes putatively involved in anaerobic oxidation of methane with sulfate, Environmental Microbiology, Oxford, England, Blackwell Science, 16 (11 Sp. Iss. SI), pp. 3431–3442.

Fujishiro, T., Ermler, U. and Shima, S.: (2014) A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis, FEBS Letters, Amsterdam, Elsevier, 588 (17), pp. 2789–2793.

Fujishiro, T., Tamura, H., Schick, M., Kahnt, J., Xie, X., Ermler, U. and Shima, S.: (2014) Identification of the Hcg enzymes in biosynthesis of [Fe]-hydrogenase cofactor by a structural genomics-based approach, Journal of Biological Inorganic Chemistry, 19 (Suppl. 2), pp. S767–S767.

Vitt, Stella, Ma, Kesen, Warkentin, Eberhard, Moll, Johanna, Pierik, Antonio J. , Shima, Seigo and Ermler, Ulrich: (2014) The F₄₂₀-Reducing [NiFe]-Hydrogenase Complex from Methanothermobacter marburgensis, the First X-ray Structure of a Group 3 Family Member, Journal of Molecular Biology (London), London, Academic Press, 426 (15), pp. 2813–2826.

Kaneko, M., Takano, Y., Chikaraishi, Y., Ogawa, N., Asakawa, S., Watanabe, T., Shima, S., Kruger, M., Matsushita, M., Kimura, H. and Ohkouchi, N.: (2014) Quantitative Analysis of Coenzyme F430 in Environmental Samples: A New Diagnostic Tool for Methanogenesis and Anaerobic Methane Oxidation, Analytical Chemistry, Washington, D.C., American Chemical Society, 86 (7), pp. 3633–3638.

Fujishiro, T., Tamura, H., Schick, M., Kahnt, J., Shima, S., Xie, X., Ermler, U. and Shima, S.: (2014) Biochemical and X-ray crystal structure analyses of Hcg proteins involved in biosynthesis of the FeGP cofactor of [Fe]-hydrogenase, Journal of Biological Inorganic Chemistry, NEW YORK, SPRINGER, 19 (Suppl. 1), pp. S223–S223.

Fujishiro, T. and Shima, S.: (2014) Functional analysis based on tertiary structure of proteins, Seibutsukougakukaishi, (92).

Shima, Seigo: (2014) Enzyme chemistry of methanogenesis and anaerobic oxidation of methane, Kagakutoseibutsu, 52, pp. 307–312.