Publications of Seigo Shima

Hemmann, Jethro L., Wagner, Tristan, Shima, Seigo and Vorholt, Julia A.: (2019) Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites, Proceedings of the National Academy of Sciences of the United States of America, Washington, D.C., National Academy of Sciences, 116 (51), pp. 25583–25590.

Watanabe, Tomohiro, Wagner, Tristan, Huang, Gangfeng, Kahnt, Jörg, Ataka, Kenichi, Ermler, Ulrich and Shima, Seigo: (2019) The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates, Angewandte Chemie International Edition in English, Weinheim, Wiley-VCH, 58 (11), pp. 3506–3510.

Engilberge, Sylvain, Wagner, Tristan, Santoni, Gianluca, Breyton, Cecile, Shima, Seigo, Franzetti, Bruno, Riobe, Francois, Maury, Olivier and Girard, Eric: (2019) Protein crystal structure determination with the crystallophore, a nucleating and phasing agent, JOURNAL OF APPLIED CRYSTALLOGRAPHY, 52, pp. 722–731.

Huang, Gangfeng, Wagner, Tristan, Wodrich, Matthew D., Ataka, Kenichi, Bill, Eckhard, Ermler, Ulrich, Hu, Xile and Shima, Seigo: (2019) The atomic-resolution crystal structure of activated [Fe]-hydrogenase, Nature Catalysis, New York, Nature Publishing Group, 2 (6), pp. 537–543.

Ilina, Yulia, Lorent, Christian, Katz, Sagie, Jeoung, Jae-Hun, Shima, Seigo, Horch, Marius, Zebger, Ingo and Dobbek, Holger: (2019) X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 58 (51), pp. 18710–18714.

Pan, Hui-Jie, Huang, Gangfeng, Wodrich, Matthew D., Tirani, Farzaneh Fadaei, Ataka, Kenichi, Shima, Seigo and Hu, Xile: (2019) A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor, NATURE CHEMISTRY, 11 (7), pp. 669–675.

Voegeli, Bastian, Shima, Seigo, Erb, Tobias J. and Wagner, Tristan: (2019) Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme, FEBS LETTERS, 593 (5), pp. 543–553.

Berhardsgrütter, I., Vögeli, B., Wagner, T., Peter, D., Cortina, N. S., Kahnt, J., Bange, G., Engilberge, S., Girard, E., Riobe, F., Maury, O., Shima, S., Zarzycki, J. and Erb, T. J.: (2018) The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite, NATURE CHEMICAL BIOLOGY, 14 (12), p. 1127.

Wagner, T., Huang, G., Ermler, U. and Shima, S.: (2018) How [Fe]-Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 57 (46), pp. 15056–15059.

Vögeli, Bastian, Rosenthal, Raoul, Stoffel, Gabriele, Wagner, Tristan, Kiefer, P., Cortina, Nina Socorro, Shima, Seigo and Erb, Tobias J.: (2018) InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis, JOURNAL OF BIOLOGICAL CHEMISTRY, 293 (44), pp. 17200–17207.

Engilberge, S., Riobe, F., Wagner, T., Di Pietro, S., Breyton, C., Franzetti, B., Shima, S., Girard, E., Dumont, E. and Maury, O.: (2018) Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography, CHEMISTRY-A EUROPEAN JOURNAL, 24 (39), pp. 9739–9746.

Huang, G., Wagner, T., Ermler, U., Bill, E., Ataka, K. and Shima, S.: (2018) Dioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 57 (18), pp. 4917–4920.

Vögeli, B., Engilberge, S., Girard, E., Riobe, F., Maury, O., Erb, T. J., Shima, S. and Wagner, T.: (2018) Archaeal acetoacetyl-CoA thiolase/HMG-CoA synthase complex channels the intermediate via a fused CoA-binding site, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 115 (13), pp. 3380–3385.

Bai, L., Wagner, T., Xu, T., Hu, X., Ermler, U. and Shima, S.: (2017) A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC, Angewandte Chemie International Edition, Weinheim, Wiley-VCH, 56 (36), pp. 10806–10809.

Wagner, T., Koch, J., Ermler, U. and Shima, S.: (2017) Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction, Science, Washington, D.C., American Association for the Advancement of Science, 357 (6352), pp. 699–702.

Wagner, T., Wegner, C., Kahnt, J., Ermler, U. and Shima, S.: (2017) Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase from Methanococcales and Methanobacteriales, Journal of Bacteriology, Washington, DC, American Society for Microbiology (ASM), 199 (16).

Rosenthal, R., Vogeli, B., Wagner, T., Shima, S. and Erb, T.: (2017) A conserved threonine prevents self-intoxication of enoyl-thioester reductases, Nature Chemical Biology, New York, NY, Nature Pub. Group, 13 (7), pp. 745–749.

Bai, L., Fujishiro, T., Huang, G., Koch, J., Takabayashi, A., Yokono, M., Tanaka, A., Xu, T., Hu, X., Ermler, U. and Shima, S.: (2017) Towards artificial methanogenesis: biosynthesis of the [Fe]-hydrogenase cofactor and characterization of the semisynthetic hydrogenase, Faraday Discussions, London, Royal Society of Chemistry, 198, June, pp. 37–58.

Wang, M., Artero, V., Hammarstrom, L., Martinez, J., Karlsson, J., Gust, D., Summers, P., Machan, C., Brueggeller, P., Windle, C., Kageshima, Y., Cogdell, R., Tolod, K., Kibler, A., Apaydin, D., Fujita, E., Ehrmaier, J., Shima, S., Gibson, E., Karadas, F., Harriman, A., Inoue, H., Kudo, A., Takayama, T., Wasielewski, M., Cassiola, F., Yagi, M., Ishida, H., Franco, F., Kang, S., Nocera, D., Li, C., Di Fonzo, F., Park, H., Sun, L., Setoyama, T., Kang, Y., Ishitani, O., Shen, J., Son, H. and Masaoka, S.: (2017) Molecular catalysts for artificial photosynthesis: general discussion, Faraday Discussions, 198, June, pp. 353–395.

Wagner, T., Ermler, U. and Shima, S.: (2016) The methanogenic CO₂ reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters, Science, Washington, D.C., American Association for the Advancement of Science, 354 (6308 Sp. Iss. SI), pp. 114–117.